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Conserved domains on  [gi|1149123047|ref|NP_001335874|]
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ATP-dependent translocase ABCB1 isoform 1 [Homo sapiens]

Protein Classification

ABC transporter B family protein( domain architecture ID 1000096)

ABC transporter B (ABCB) family protein, similar to human phosphatidylcholine translocator ABCB4 that functions as a floppase that translocates specifically phosphatidylcholine (PC) from the inner to the outer leaflet of the canalicular membrane bilayer into the canaliculi of hepatocytes

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
PTZ00265 super family cl36537
multidrug resistance protein (mdr1); Provisional
123-1337 0e+00

multidrug resistance protein (mdr1); Provisional


The actual alignment was detected with superfamily member PTZ00265:

Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 613.96  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  123 VGTLAAIIHGAGLPLMMLVFGEmtdifanagnledLMSNitnrsdindtgffMNLEEDMTRYAYYYSGIGAGVLVAAYIq 202
Cdd:PTZ00265    64 VSFVCATISGGTLPFFVSVFGV-------------IMKN-------------MNLGENVNDIIFSLVLIGIFQFILSFI- 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  203 vSFWCL--AAGRQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQSMATFFTGFIVGFTR 280
Cdd:PTZ00265   117 -SSFCMdvVTTKILKTLKLEFLKSVFYQDGQFHDNNPGSKLTSDLDFYLEQVNAGIGTKFITIFTYASAFLGLYIWSLFK 195
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  281 GWKLTLVILAISPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKRIGIK 360
Cdd:PTZ00265   196 NARLTLCITCVFPLIYICGVICNKKVKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGEKTILKKFNLSEKLYSKYILK 275
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  361 KAITANISIGAAFLLIYASYALAFWYGTTLVLS--------GEYSIGQVLTVFFSVLIGAFSVGQASPSIEAFANARGAA 432
Cdd:PTZ00265   276 ANFMESLHIGMINGFILASYAFGFWYGTRIIISdlsnqqpnNDFHGGSVISILLGVLISMFMLTIILPNITEYMKSLEAT 355
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  433 YEIFKIIDNKPSIDSySKSGHKPDNIKgNLEFRNVHFSYPSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQR 512
Cdd:PTZ00265   356 NSLYEIINRKPLVEN-NDDGKKLKDIK-KIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIER 433
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  513 LYDPTEGMVSV-DGQDIRTINVRFLREIIGVVSQEPVLFATTIAENIRYG------------------------------ 561
Cdd:PTZ00265   434 LYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSlyslkdlealsnyynedgndsqenknkrns 513
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  562 ------------RENVTMDEIEKAVKEANA---------------YDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARA 614
Cdd:PTZ00265   514 crakcagdlndmSNTTDSNELIEMRKNYQTikdsevvdvskkvliHDFVSALPDKYETLVGSNASKLSGGQKQRISIARA 593
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  615 LVRNPKILLLDEATSALDTESEAVVQVALD--KARKGRTTIVIAHRLSTVRNADVI------------------------ 668
Cdd:PTZ00265   594 IIRNPKILILDEATSSLDNKSEYLVQKTINnlKGNENRITIIIAHRLSTIRYANTIfvlsnrergstvdvdiigedptkd 673
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  669 -----------------------AGFDDGVIVEKGNHDELMKEK-GIYFKLVTMQTAGNEVELENAAD---ESKSEI--- 718
Cdd:PTZ00265   674 nkennnknnkddnnnnnnnnnnkINNAGSYIIEQGTHDALMKNKnGIYYTMINNQKVSSKKSSNNDNDkdsDMKSSAykd 753
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  719 -----DALEMSSN--DSRSSLIRKRSTRRSVRGSQAQDR--KLSTKEALDESIPPV-SFWRIMKLNLTEWPYFVVGVFCA 788
Cdd:PTZ00265   754 sergyDPDEMNGNskHENESASNKKSCKMSDENASENNAggKLPFLRNLFKRKPKApNNLRIVYREIFSYKKDVTIIALS 833
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  789 II-NGGLQPAFAIIFSKIIGVFTRIDDPETkrqNSNLFSLLFLALGIISFITFFLQGFTFGKAGEILTKRLRYMVFRSML 867
Cdd:PTZ00265   834 ILvAGGLYPVFALLYAKYVSTLFDFANLEA---NSNKYSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMKRRLFENIL 910
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  868 RQDVSWFDDPKNTTGALTTRLANDAAQVKGAIGSRLAVITQNIANLGTGIIISFIYGWQLTLLLLAIVPIIAIAGVVEMK 947
Cdd:PTZ00265   911 YQEISFFDQDKHAPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSMVMSFYFCPIVAAVLTGTYFIFMRVFAIRAR 990
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  948 MLSGQALkDKKELEGSGKI----------------ATEAIENFRTVVSLTQEQKFEHMYAQSLQVPYRNSLRKAHIFGIT 1011
Cdd:PTZ00265   991 LTANKDV-EKKEINQPGTVfaynsddeifkdpsflIQEAFYNMNTVIIYGLEDYFCNLIEKAIDYSNKGQKRKTLVNSML 1069
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1012 FSFTQAMMYFSYAGCFRFGAYLVAHKLMSFEDVLLVFSAVVFGAMAVGQVSSFAPDYAKAKISAAHIIMIIEKTPLIDSY 1091
Cdd:PTZ00265  1070 WGFSQSAQLFINSFAYWFGSFLIRRGTILVDDFMKSLFTFLFTGSYAGKLMSLKGDSENAKLSFEKYYPLIIRKSNIDVR 1149
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1092 STEGLM---PNTLEGNVTFGEVVFNYPTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD---------- 1158
Cdd:PTZ00265  1150 DNGGIRiknKNDIKGKIEIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfk 1229
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1159 --------------------------------------------PLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEPILFD 1194
Cdd:PTZ00265  1230 nehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFN 1309
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1195 CSIAENIAYGDNSrvVSQEEIVRAAKEANIHAFIESLPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATS 1274
Cdd:PTZ00265  1310 MSIYENIKFGKED--ATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATS 1387
                         1370      1380      1390      1400      1410      1420      1430
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1149123047 1275 ALDTESEKVVQEAL----DKAreGRTCIVIAHRLSTIQNADLIVVFQN-----GRVKEHGTHQQLL-AQKGIY 1337
Cdd:PTZ00265  1388 SLDSNSEKLIEKTIvdikDKA--DKTIITIAHRIASIKRSDKIVVFNNpdrtgSFVQAHGTHEELLsVQDGVY 1458
 
Name Accession Description Interval E-value
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
123-1337 0e+00

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 613.96  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  123 VGTLAAIIHGAGLPLMMLVFGEmtdifanagnledLMSNitnrsdindtgffMNLEEDMTRYAYYYSGIGAGVLVAAYIq 202
Cdd:PTZ00265    64 VSFVCATISGGTLPFFVSVFGV-------------IMKN-------------MNLGENVNDIIFSLVLIGIFQFILSFI- 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  203 vSFWCL--AAGRQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQSMATFFTGFIVGFTR 280
Cdd:PTZ00265   117 -SSFCMdvVTTKILKTLKLEFLKSVFYQDGQFHDNNPGSKLTSDLDFYLEQVNAGIGTKFITIFTYASAFLGLYIWSLFK 195
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  281 GWKLTLVILAISPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKRIGIK 360
Cdd:PTZ00265   196 NARLTLCITCVFPLIYICGVICNKKVKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGEKTILKKFNLSEKLYSKYILK 275
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  361 KAITANISIGAAFLLIYASYALAFWYGTTLVLS--------GEYSIGQVLTVFFSVLIGAFSVGQASPSIEAFANARGAA 432
Cdd:PTZ00265   276 ANFMESLHIGMINGFILASYAFGFWYGTRIIISdlsnqqpnNDFHGGSVISILLGVLISMFMLTIILPNITEYMKSLEAT 355
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  433 YEIFKIIDNKPSIDSySKSGHKPDNIKgNLEFRNVHFSYPSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQR 512
Cdd:PTZ00265   356 NSLYEIINRKPLVEN-NDDGKKLKDIK-KIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIER 433
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  513 LYDPTEGMVSV-DGQDIRTINVRFLREIIGVVSQEPVLFATTIAENIRYG------------------------------ 561
Cdd:PTZ00265   434 LYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSlyslkdlealsnyynedgndsqenknkrns 513
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  562 ------------RENVTMDEIEKAVKEANA---------------YDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARA 614
Cdd:PTZ00265   514 crakcagdlndmSNTTDSNELIEMRKNYQTikdsevvdvskkvliHDFVSALPDKYETLVGSNASKLSGGQKQRISIARA 593
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  615 LVRNPKILLLDEATSALDTESEAVVQVALD--KARKGRTTIVIAHRLSTVRNADVI------------------------ 668
Cdd:PTZ00265   594 IIRNPKILILDEATSSLDNKSEYLVQKTINnlKGNENRITIIIAHRLSTIRYANTIfvlsnrergstvdvdiigedptkd 673
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  669 -----------------------AGFDDGVIVEKGNHDELMKEK-GIYFKLVTMQTAGNEVELENAAD---ESKSEI--- 718
Cdd:PTZ00265   674 nkennnknnkddnnnnnnnnnnkINNAGSYIIEQGTHDALMKNKnGIYYTMINNQKVSSKKSSNNDNDkdsDMKSSAykd 753
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  719 -----DALEMSSN--DSRSSLIRKRSTRRSVRGSQAQDR--KLSTKEALDESIPPV-SFWRIMKLNLTEWPYFVVGVFCA 788
Cdd:PTZ00265   754 sergyDPDEMNGNskHENESASNKKSCKMSDENASENNAggKLPFLRNLFKRKPKApNNLRIVYREIFSYKKDVTIIALS 833
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  789 II-NGGLQPAFAIIFSKIIGVFTRIDDPETkrqNSNLFSLLFLALGIISFITFFLQGFTFGKAGEILTKRLRYMVFRSML 867
Cdd:PTZ00265   834 ILvAGGLYPVFALLYAKYVSTLFDFANLEA---NSNKYSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMKRRLFENIL 910
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  868 RQDVSWFDDPKNTTGALTTRLANDAAQVKGAIGSRLAVITQNIANLGTGIIISFIYGWQLTLLLLAIVPIIAIAGVVEMK 947
Cdd:PTZ00265   911 YQEISFFDQDKHAPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSMVMSFYFCPIVAAVLTGTYFIFMRVFAIRAR 990
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  948 MLSGQALkDKKELEGSGKI----------------ATEAIENFRTVVSLTQEQKFEHMYAQSLQVPYRNSLRKAHIFGIT 1011
Cdd:PTZ00265   991 LTANKDV-EKKEINQPGTVfaynsddeifkdpsflIQEAFYNMNTVIIYGLEDYFCNLIEKAIDYSNKGQKRKTLVNSML 1069
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1012 FSFTQAMMYFSYAGCFRFGAYLVAHKLMSFEDVLLVFSAVVFGAMAVGQVSSFAPDYAKAKISAAHIIMIIEKTPLIDSY 1091
Cdd:PTZ00265  1070 WGFSQSAQLFINSFAYWFGSFLIRRGTILVDDFMKSLFTFLFTGSYAGKLMSLKGDSENAKLSFEKYYPLIIRKSNIDVR 1149
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1092 STEGLM---PNTLEGNVTFGEVVFNYPTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD---------- 1158
Cdd:PTZ00265  1150 DNGGIRiknKNDIKGKIEIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfk 1229
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1159 --------------------------------------------PLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEPILFD 1194
Cdd:PTZ00265  1230 nehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFN 1309
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1195 CSIAENIAYGDNSrvVSQEEIVRAAKEANIHAFIESLPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATS 1274
Cdd:PTZ00265  1310 MSIYENIKFGKED--ATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATS 1387
                         1370      1380      1390      1400      1410      1420      1430
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1149123047 1275 ALDTESEKVVQEAL----DKAreGRTCIVIAHRLSTIQNADLIVVFQN-----GRVKEHGTHQQLL-AQKGIY 1337
Cdd:PTZ00265  1388 SLDSNSEKLIEKTIvdikDKA--DKTIITIAHRIASIKRSDKIVVFNNpdrtgSFVQAHGTHEELLsVQDGVY 1458
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
118-702 0e+00

ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 549.00  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  118 KLYMVVGTLAAIIHGAGLPLMMLVFGEMTDIFANAGNLEDLMsnitnrsdindtgffmnleedmtRYAYYYSGIGAGVLV 197
Cdd:COG1132     20 RGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALL-----------------------LLLLLLLGLALLRAL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  198 AAYIQVSFWCLAAGRQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQSMATFFTGFIVG 277
Cdd:COG1132     77 LSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVL 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  278 FTRGWKLTLVILAISPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKRI 357
Cdd:COG1132    157 FVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRA 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  358 GIKKAITANISIGAAFLLIYASYALAFWYGTTLVLSGEYSIGQVLTVFFSVLIGAFSVGQASPSIEAFANARGAAYEIFK 437
Cdd:COG1132    237 NLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFE 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  438 IIDNKPSIDSySKSGHKPDNIKGNLEFRNVHFSYPSRKEVkiLKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPT 517
Cdd:COG1132    317 LLDEPPEIPD-PPGAVPLPPVRGEIEFENVSFSYPGDRPV--LKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPT 393
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  518 EGMVSVDGQDIRTINVRFLREIIGVVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPHKFDTLVGER 597
Cdd:COG1132    394 SGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGER 473
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  598 GAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIV 677
Cdd:COG1132    474 GVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIV 553
                          570       580
                   ....*....|....*....|....*
gi 1149123047  678 EKGNHDELMKEKGIYFKLVTMQTAG 702
Cdd:COG1132    554 EQGTHEELLARGGLYARLYRLQFGE 578
ABC_6TM_Pgp_ABCB1 cd18558
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ...
121-435 6.63e-163

Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1(ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.


Pssm-ID: 350002 [Multi-domain]  Cd Length: 312  Bit Score: 489.87  E-value: 6.63e-163
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  121 MVVGTLAAIIHGAGLPLMMLVFGEMTDIFANAGNLEdlmSNITNRSDINDTGFFMNLEEDMTRYAYYYSGIGAGVLVAAY 200
Cdd:cd18558      1 MVVGILCAIIHGGLLPAFMVIFGDMTDSFTNGGMTN---ITGNSSGLNSSAGPFEKLEEEMTLYAYYYLIIGAIVLITAY 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  201 IQVSFWCLAAGRQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQSMATFFTGFIVGFTR 280
Cdd:cd18558     78 IQGSFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIR 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  281 GWKLTLVILAISPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKRIGIK 360
Cdd:cd18558    158 GWKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIK 237
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1149123047  361 KAITANISIGAAFLLIYASYALAFWYGTTLVLSGEYSIGQVLTVFFSVLIGAFSVGQASPSIEAFANARGAAYEI 435
Cdd:cd18558    238 KAITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGEVLTVFFSVLIGAFSAGQQVPSIEAFANARGAAYHI 312
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
106-696 9.99e-140

Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 443.78  E-value: 9.99e-140
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  106 VFSMFRYSNwLDKLYMVVGTLAAIIHGAGLPLMMLVFGEMTDIFANAGNLEDLMSNItnrsdindtgFFMNLeedMTRYA 185
Cdd:TIGR00958  149 LFRLLGLSG-RDWPWLISAFVFLTLSSLGEMFIPFYTGRVIDTLGGDKGPPALASAI----------FFMCL---LSIAS 214
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  186 YYYSGIGAGVLVAAYiqvsfwclaaGRQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQ 265
Cdd:TIGR00958  215 SVSAGLRGGSFNYTM----------ARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLR 284
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  266 SMATFFTGFIVGFTRGWKLTLVILAISPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELE 345
Cdd:TIGR00958  285 NLVMLLGLLGFMLWLSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEAS 364
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  346 RYNKNLEEAKRIGIKKAITANISIGAAFLLIYASYALAFWYGTTLVLSGEYSIGQVLtvffSVLIGAFSVGQASPSIEAF 425
Cdd:TIGR00958  365 RFKEALEETLQLNKRKALAYAGYLWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLV----SFLLYQEQLGEAVRVLSYV 440
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  426 AN----ARGAAYEIFKIIDNKPSIDSysKSGHKPDNIKGNLEFRNVHFSYPSRKEVKILKGLNLKVQSGQTVALVGNSGC 501
Cdd:TIGR00958  441 YSgmmqAVGASEKVFEYLDRKPNIPL--TGTLAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGS 518
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  502 GKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIGVVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYD 581
Cdd:TIGR00958  519 GKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHD 598
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  582 FIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQValDKARKGRTTIVIAHRLST 661
Cdd:TIGR00958  599 FIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRLST 676
                          570       580       590
                   ....*....|....*....|....*....|....*
gi 1149123047  662 VRNADVIAGFDDGVIVEKGNHDELMKEKGIYFKLV 696
Cdd:TIGR00958  677 VERADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
ABC_membrane pfam00664
ABC transporter transmembrane region; This family represents a unit of six transmembrane ...
121-413 2.95e-84

ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.


Pssm-ID: 459896 [Multi-domain]  Cd Length: 274  Bit Score: 276.45  E-value: 2.95e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  121 MVVGTLAAIIHGAGLPLMMLVFGEMTDIFanagnledlmsnitnrSDINDTGFFmnleeDMTRYAYYYSGIGAGVLVAAY 200
Cdd:pfam00664    1 LILAILLAILSGAISPAFPLVLGRILDVL----------------LPDGDPETQ-----ALNVYSLALLLLGLAQFILSF 59
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  201 IQVSFWCLAAGRQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQSMATFFTGFIVGFTR 280
Cdd:pfam00664   60 LQSYLLNHTGERLSRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYY 139
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  281 GWKLTLVILAISPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKRIGIK 360
Cdd:pfam00664  140 GWKLTLVLLAVLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIK 219
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1149123047  361 KAITANISIGAAFLLIYASYALAFWYGTTLVLSGEYSIGQ--VLTVFFSVLIGAF 413
Cdd:pfam00664  220 KAVANGLSFGITQFIGYLSYALALWFGAYLVISGELSVGDlvAFLSLFAQLFGPL 274
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
1118-1316 1.90e-20

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 90.76  E-value: 1.90e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1118 PDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQwlrahlgiVSQEPILFDCSI 1197
Cdd:NF040873     3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQ--------RSEVPDSLPLTV 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1198 AENIAYGDNSRVVSQEEIVRAAKEANIHAF----IESLPNKystKVGDkgtqLSGGQKQRIAIARALVRQPHILLLDEAT 1273
Cdd:NF040873    75 RDLVAMGRWARRGLWRRLTRDDRAAVDDALervgLADLAGR---QLGE----LSGGQRQRALLAQGLAQEADLLLLDEPT 147
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1149123047 1274 SALDTESEKVVQEAL-DKAREGRTCIVIAHRLSTIQNADLIVVF 1316
Cdd:NF040873   148 TGLDAESRERIIALLaEEHARGATVVVVTHDLELVRRADPCVLL 191
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
470-666 2.54e-19

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 87.29  E-value: 2.54e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  470 SYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGqdirTINVRFLREIIGVVSQEPVl 549
Cdd:NF040873     1 GYGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG----GARVAYVPQRSEVPDSLPL- 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  550 fatTIAENIRYGR-------ENVTMDEiEKAVKEAnaydfIMKLphKFDTLVGERGAQLSGGQKQRIAIARALVRNPKIL 622
Cdd:NF040873    73 ---TVRDLVAMGRwarrglwRRLTRDD-RAAVDDA-----LERV--GLADLAGRQLGELSGGQRQRALLAQGLAQEADLL 141
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1149123047  623 LLDEATSALDTESEAVVQVAL-DKARKGRTTIVIAHRLSTVRNAD 666
Cdd:NF040873   142 LLDEPTTGLDAESRERIIALLaEEHARGATVVVVTHDLELVRRAD 186
GguA NF040905
sugar ABC transporter ATP-binding protein;
462-678 1.41e-16

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 84.46  E-value: 1.41e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSrkeVKILKGLNLKVQSGQTVALVGNSGCGKSTtvqLMQRL-----YDPTEGMVSVDGQ-----DIRTi 531
Cdd:NF040905     2 LEMRGITKTFPG---VKALDDVNLSVREGEIHALCGENGAGKST---LMKVLsgvypHGSYEGEILFDGEvcrfkDIRD- 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  532 nvrflREIIGVV--SQE----PVLfatTIAENIRYGRENVTMDEI--EKAVKEANAYDFIMKLPHKFDTLVGERGAqlsg 603
Cdd:NF040905    75 -----SEALGIViiHQElaliPYL---SIAENIFLGNERAKRGVIdwNETNRRARELLAKVGLDESPDTLVTDIGV---- 142
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1149123047  604 GQKQRIAIARALVRNPKILLLDEATSAL-DTESEAVVQVALDKARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVE 678
Cdd:NF040905   143 GKQQLVEIAKALSKDVKLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIRRvADSITVLRDGRTIE 219
GguA NF040905
sugar ABC transporter ATP-binding protein;
1116-1323 1.20e-15

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 81.37  E-value: 1.20e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1116 TRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYdP---LAGKVLLDGKEIKRLNvqwLRA--HLGIV--SQ 1188
Cdd:NF040905    10 TFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PhgsYEGEILFDGEVCRFKD---IRDseALGIViiHQ 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1189 E----PILfdcSIAENIAYGdNSR----VVSQEEIVRAAKEANIHAFIESLPNkysTKVGDKGTqlsgGQKQRIAIARAL 1260
Cdd:NF040905    86 ElaliPYL---SIAENIFLG-NERakrgVIDWNETNRRARELLAKVGLDESPD---TLVTDIGV----GKQQLVEIAKAL 154
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1149123047 1261 VRQPHILLLDEATSAL-DTESEKVVQEALDKAREGRTCIVIAHRLSTI-QNADLIVVFQNGRVKE 1323
Cdd:NF040905   155 SKDVKLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIrRVADSITVLRDGRTIE 219
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
489-681 1.08e-13

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 69.71  E-value: 1.08e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047   489 SGQTVALVGNSGCGKSTTVQ-LMQRLYDPTEGMVSVDGQDIRTINVRFLREIIgvvsqepvlfattiaenirygrenvtm 567
Cdd:smart00382    1 PGEVILIVGPPGSGKTTLARaLARELGPPGGGVIYIDGEDILEEVLDQLLLII--------------------------- 53
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047   568 deiekavkeanaydfimklphkfdtlVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALD--- 644
Cdd:smart00382   54 --------------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrl 107
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|.
gi 1149123047   645 ----KARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGN 681
Cdd:smart00382  108 llllKSEKNLTVILTTNDEKDLGPALLRRRFDRRIVLLLIL 148
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
497-632 6.21e-07

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 53.98  E-value: 6.21e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  497 GNSGCGKSTTVQLMQRLYDPTEGMV-----SVDGQDIRTinvrflREIIGVVSQEPVLfattiaenirYG----REN--- 564
Cdd:NF033858   299 GSNGCGKSTTMKMLTGLLPASEGEAwlfgqPVDAGDIAT------RRRVGYMSQAFSL----------YGeltvRQNlel 362
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1149123047  565 ------VTMDEIEKAVKEanaydfimkLPHKFD--TLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALD 632
Cdd:NF033858   363 harlfhLPAAEIAARVAE---------MLERFDlaDVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
476-690 1.07e-05

oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 49.35  E-value: 1.07e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  476 EVKILKGLNLKVQSGQTVALVGNSGCGKSTTVqLMQRLYDPTEGMvsvdgQDIR----TINVRFLREIIGVvsQEPVLFA 551
Cdd:NF000106    25 EVKAVDGVDLDVREGTVLGVLGP*GAA**RGA-LPAHV*GPDAGR-----RPWRf*twCANRRALRRTIG*--HRPVR*G 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  552 TTIAENiryGRENVTM--DEIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATS 629
Cdd:NF000106    97 RRESFS---GRENLYMigR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTT 173
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1149123047  630 ALD--TESEAVVQVAlDKARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKGNHDELMKEKG 690
Cdd:NF000106   174 GLDprTRNEVWDEVR-SMVRDGATVLLTTQYMEEAEQlAHELTVIDRGRVIADGKVDELKTKVG 236
GguA NF040905
sugar ABC transporter ATP-binding protein;
1104-1300 1.76e-05

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 49.02  E-value: 1.76e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1104 NVTFGEVVF-------NYPTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKS-TVVQLLERFYDP-LAGKVLLDGKEIKRL 1174
Cdd:NF040905   250 TPKIGEVVFevknwtvYHPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTeLAMSVFGRSYGRnISGTVFKDGKEVDVS 329
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1175 NVQWL-----------RAHLGIVSQEPILFDCSIA--ENIAygdNSRVVSQEEIVRAAKEanihaFIESLPNKYSTkVGD 1241
Cdd:NF040905   330 TVSDAidaglayvtedRKGYGLNLIDDIKRNITLAnlGKVS---RRGVIDENEEIKVAEE-----YRKKMNIKTPS-VFQ 400
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1149123047 1242 KGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDT----ESEKVVQEAldkAREGRTCIVI 1300
Cdd:NF040905   401 KVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVgakyEIYTIINEL---AAEGKGVIVI 460
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
1240-1335 3.10e-04

oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 44.73  E-value: 3.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1240 GDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESE-KVVQEALDKAREGRTCIVIAHRLSTI-QNADLIVVFQ 1317
Cdd:NF000106   139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRnEVWDEVRSMVRDGATVLLTTQYMEEAeQLAHELTVID 218
                           90
                   ....*....|....*...
gi 1149123047 1318 NGRVKEHGTHQQLLAQKG 1335
Cdd:NF000106   219 RGRVIADGKVDELKTKVG 236
 
Name Accession Description Interval E-value
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
123-1337 0e+00

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 613.96  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  123 VGTLAAIIHGAGLPLMMLVFGEmtdifanagnledLMSNitnrsdindtgffMNLEEDMTRYAYYYSGIGAGVLVAAYIq 202
Cdd:PTZ00265    64 VSFVCATISGGTLPFFVSVFGV-------------IMKN-------------MNLGENVNDIIFSLVLIGIFQFILSFI- 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  203 vSFWCL--AAGRQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQSMATFFTGFIVGFTR 280
Cdd:PTZ00265   117 -SSFCMdvVTTKILKTLKLEFLKSVFYQDGQFHDNNPGSKLTSDLDFYLEQVNAGIGTKFITIFTYASAFLGLYIWSLFK 195
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  281 GWKLTLVILAISPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKRIGIK 360
Cdd:PTZ00265   196 NARLTLCITCVFPLIYICGVICNKKVKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGEKTILKKFNLSEKLYSKYILK 275
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  361 KAITANISIGAAFLLIYASYALAFWYGTTLVLS--------GEYSIGQVLTVFFSVLIGAFSVGQASPSIEAFANARGAA 432
Cdd:PTZ00265   276 ANFMESLHIGMINGFILASYAFGFWYGTRIIISdlsnqqpnNDFHGGSVISILLGVLISMFMLTIILPNITEYMKSLEAT 355
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  433 YEIFKIIDNKPSIDSySKSGHKPDNIKgNLEFRNVHFSYPSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQR 512
Cdd:PTZ00265   356 NSLYEIINRKPLVEN-NDDGKKLKDIK-KIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIER 433
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  513 LYDPTEGMVSV-DGQDIRTINVRFLREIIGVVSQEPVLFATTIAENIRYG------------------------------ 561
Cdd:PTZ00265   434 LYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSlyslkdlealsnyynedgndsqenknkrns 513
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  562 ------------RENVTMDEIEKAVKEANA---------------YDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARA 614
Cdd:PTZ00265   514 crakcagdlndmSNTTDSNELIEMRKNYQTikdsevvdvskkvliHDFVSALPDKYETLVGSNASKLSGGQKQRISIARA 593
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  615 LVRNPKILLLDEATSALDTESEAVVQVALD--KARKGRTTIVIAHRLSTVRNADVI------------------------ 668
Cdd:PTZ00265   594 IIRNPKILILDEATSSLDNKSEYLVQKTINnlKGNENRITIIIAHRLSTIRYANTIfvlsnrergstvdvdiigedptkd 673
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  669 -----------------------AGFDDGVIVEKGNHDELMKEK-GIYFKLVTMQTAGNEVELENAAD---ESKSEI--- 718
Cdd:PTZ00265   674 nkennnknnkddnnnnnnnnnnkINNAGSYIIEQGTHDALMKNKnGIYYTMINNQKVSSKKSSNNDNDkdsDMKSSAykd 753
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  719 -----DALEMSSN--DSRSSLIRKRSTRRSVRGSQAQDR--KLSTKEALDESIPPV-SFWRIMKLNLTEWPYFVVGVFCA 788
Cdd:PTZ00265   754 sergyDPDEMNGNskHENESASNKKSCKMSDENASENNAggKLPFLRNLFKRKPKApNNLRIVYREIFSYKKDVTIIALS 833
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  789 II-NGGLQPAFAIIFSKIIGVFTRIDDPETkrqNSNLFSLLFLALGIISFITFFLQGFTFGKAGEILTKRLRYMVFRSML 867
Cdd:PTZ00265   834 ILvAGGLYPVFALLYAKYVSTLFDFANLEA---NSNKYSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMKRRLFENIL 910
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  868 RQDVSWFDDPKNTTGALTTRLANDAAQVKGAIGSRLAVITQNIANLGTGIIISFIYGWQLTLLLLAIVPIIAIAGVVEMK 947
Cdd:PTZ00265   911 YQEISFFDQDKHAPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSMVMSFYFCPIVAAVLTGTYFIFMRVFAIRAR 990
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  948 MLSGQALkDKKELEGSGKI----------------ATEAIENFRTVVSLTQEQKFEHMYAQSLQVPYRNSLRKAHIFGIT 1011
Cdd:PTZ00265   991 LTANKDV-EKKEINQPGTVfaynsddeifkdpsflIQEAFYNMNTVIIYGLEDYFCNLIEKAIDYSNKGQKRKTLVNSML 1069
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1012 FSFTQAMMYFSYAGCFRFGAYLVAHKLMSFEDVLLVFSAVVFGAMAVGQVSSFAPDYAKAKISAAHIIMIIEKTPLIDSY 1091
Cdd:PTZ00265  1070 WGFSQSAQLFINSFAYWFGSFLIRRGTILVDDFMKSLFTFLFTGSYAGKLMSLKGDSENAKLSFEKYYPLIIRKSNIDVR 1149
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1092 STEGLM---PNTLEGNVTFGEVVFNYPTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD---------- 1158
Cdd:PTZ00265  1150 DNGGIRiknKNDIKGKIEIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfk 1229
                         1210      1220      1230      1240      1250      1260      1270      1280
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1159 --------------------------------------------PLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEPILFD 1194
Cdd:PTZ00265  1230 nehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFN 1309
                         1290      1300      1310      1320      1330      1340      1350      1360
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1195 CSIAENIAYGDNSrvVSQEEIVRAAKEANIHAFIESLPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATS 1274
Cdd:PTZ00265  1310 MSIYENIKFGKED--ATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATS 1387
                         1370      1380      1390      1400      1410      1420      1430
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1149123047 1275 ALDTESEKVVQEAL----DKAreGRTCIVIAHRLSTIQNADLIVVFQN-----GRVKEHGTHQQLL-AQKGIY 1337
Cdd:PTZ00265  1388 SLDSNSEKLIEKTIvdikDKA--DKTIITIAHRIASIKRSDKIVVFNNpdrtgSFVQAHGTHEELLsVQDGVY 1458
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
118-702 0e+00

ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 549.00  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  118 KLYMVVGTLAAIIHGAGLPLMMLVFGEMTDIFANAGNLEDLMsnitnrsdindtgffmnleedmtRYAYYYSGIGAGVLV 197
Cdd:COG1132     20 RGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALL-----------------------LLLLLLLGLALLRAL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  198 AAYIQVSFWCLAAGRQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQSMATFFTGFIVG 277
Cdd:COG1132     77 LSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVL 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  278 FTRGWKLTLVILAISPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKRI 357
Cdd:COG1132    157 FVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRA 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  358 GIKKAITANISIGAAFLLIYASYALAFWYGTTLVLSGEYSIGQVLTVFFSVLIGAFSVGQASPSIEAFANARGAAYEIFK 437
Cdd:COG1132    237 NLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFE 316
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  438 IIDNKPSIDSySKSGHKPDNIKGNLEFRNVHFSYPSRKEVkiLKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPT 517
Cdd:COG1132    317 LLDEPPEIPD-PPGAVPLPPVRGEIEFENVSFSYPGDRPV--LKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPT 393
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  518 EGMVSVDGQDIRTINVRFLREIIGVVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPHKFDTLVGER 597
Cdd:COG1132    394 SGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGER 473
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  598 GAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIV 677
Cdd:COG1132    474 GVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIV 553
                          570       580
                   ....*....|....*....|....*
gi 1149123047  678 EKGNHDELMKEKGIYFKLVTMQTAG 702
Cdd:COG1132    554 EQGTHEELLARGGLYARLYRLQFGE 578
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
766-1346 3.65e-167

ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 511.63  E-value: 3.65e-167
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  766 SFWRIMKLNLTEWPYFVVGVFCAIINGGLQPAFAIIFSKIIGVFTRIDDPETkrqnSNLFSLLFLALGIISFITFFLQGF 845
Cdd:COG1132      8 LLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSA----LLLLLLLLLGLALLRALLSYLQRY 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  846 TFGKAGEILTKRLRYMVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIGSRLAVITQNIANLGTGIIISFIYGW 925
Cdd:COG1132     84 LLARLAQRVVADLRRDLFEHLLRLPLSFFD--RRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDW 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  926 QLTLLLLAIVPIIAIAGVVEMKMLSGQALKDKKELEGSGKIATEAIENFRTVVSLTQEQKFEHMYAQSLQVPYRNSLRKA 1005
Cdd:COG1132    162 RLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAA 241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1006 HIFGITFSFTQAMMYFSYAGCFRFGAYLVAHKLMSFEDVLLVFSAVVFGAMAVGQVSSFAPDYAKAKISAAHIIMIIEKT 1085
Cdd:COG1132    242 RLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEP 321
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1086 PLIDSySTEGLMPNTLEGNVTFGEVVFNYPtrPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVL 1165
Cdd:COG1132    322 PEIPD-PPGAVPLPPVRGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRIL 398
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1166 LDGKEIKRLNVQWLRAHLGIVSQEPILFDCSIAENIAYGDNSrvVSQEEIVRAAKEANIHAFIESLPNKYSTKVGDKGTQ 1245
Cdd:COG1132    399 IDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPD--ATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVN 476
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1246 LSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHG 1325
Cdd:COG1132    477 LSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQG 556
                          570       580
                   ....*....|....*....|.
gi 1149123047 1326 THQQLLAQKGIYFSMVSVQAG 1346
Cdd:COG1132    557 THEELLARGGLYARLYRLQFG 577
ABC_6TM_Pgp_ABCB1 cd18558
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ...
121-435 6.63e-163

Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1(ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.


Pssm-ID: 350002 [Multi-domain]  Cd Length: 312  Bit Score: 489.87  E-value: 6.63e-163
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  121 MVVGTLAAIIHGAGLPLMMLVFGEMTDIFANAGNLEdlmSNITNRSDINDTGFFMNLEEDMTRYAYYYSGIGAGVLVAAY 200
Cdd:cd18558      1 MVVGILCAIIHGGLLPAFMVIFGDMTDSFTNGGMTN---ITGNSSGLNSSAGPFEKLEEEMTLYAYYYLIIGAIVLITAY 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  201 IQVSFWCLAAGRQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQSMATFFTGFIVGFTR 280
Cdd:cd18558     78 IQGSFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIR 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  281 GWKLTLVILAISPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKRIGIK 360
Cdd:cd18558    158 GWKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIK 237
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1149123047  361 KAITANISIGAAFLLIYASYALAFWYGTTLVLSGEYSIGQVLTVFFSVLIGAFSVGQASPSIEAFANARGAAYEI 435
Cdd:cd18558    238 KAITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGEVLTVFFSVLIGAFSAGQQVPSIEAFANARGAAYHI 312
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
463-699 1.06e-152

ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.


Pssm-ID: 213216 [Multi-domain]  Cd Length: 238  Bit Score: 460.08  E-value: 1.06e-152
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  463 EFRNVHFSYPSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIGV 542
Cdd:cd03249      2 EFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  543 VSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKIL 622
Cdd:cd03249     82 VSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKIL 161
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1149123047  623 LLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELMKEKGIYFKLVTMQ 699
Cdd:cd03249    162 LLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
1105-1344 3.60e-152

ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.


Pssm-ID: 213216 [Multi-domain]  Cd Length: 238  Bit Score: 458.54  E-value: 3.60e-152
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1105 VTFGEVVFNYPTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLG 1184
Cdd:cd03249      1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1185 IVSQEPILFDCSIAENIAYGDNSRvvSQEEIVRAAKEANIHAFIESLPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQP 1264
Cdd:cd03249     81 LVSQEPVLFDGTIAENIRYGKPDA--TDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNP 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1265 HILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQKGIYFSMVSVQ 1344
Cdd:cd03249    159 KILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
191-700 7.47e-145

ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];


Pssm-ID: 441875 [Multi-domain]  Cd Length: 711  Bit Score: 457.37  E-value: 7.47e-145
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  191 IGAGVLVAAYIQVSF-----WCLA-AGRQI-HKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDdVSKINEGIGDKIGMF 263
Cdd:COG2274    198 LAIGLLLALLFEGLLrllrsYLLLrLGQRIdLRLSSRFFRHLLRLPLSFFESRSVGDLASRFRD-VESIREFLTGSLLTA 276
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  264 FQSMATFFTGFIVGFTRGWKLTLVILAISPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKE 343
Cdd:COG2274    277 LLDLLFVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRF 356
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  344 LERYNKNLEEAKRIGIKKAITANISIGAAFLLIYASYALAFWYGTTLVLSGEYSIGQVLTvfFSVLIGAF--SVGQASPS 421
Cdd:COG2274    357 RRRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTLGQLIA--FNILSGRFlaPVAQLIGL 434
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  422 IEAFANARGAAYEIFKIIDNKPSIDSYSKSGHKPdNIKGNLEFRNVHFSYPSRkEVKILKGLNLKVQSGQTVALVGNSGC 501
Cdd:COG2274    435 LQRFQDAKIALERLDDILDLPPEREEGRSKLSLP-RLKGDIELENVSFRYPGD-SPPVLDNISLTIKPGERVAIVGRSGS 512
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  502 GKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIGVVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYD 581
Cdd:COG2274    513 GKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHD 592
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  582 FIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLST 661
Cdd:COG2274    593 FIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLST 672
                          490       500       510
                   ....*....|....*....|....*....|....*....
gi 1149123047  662 VRNADVIAGFDDGVIVEKGNHDELMKEKGIYFKLVTMQT 700
Cdd:COG2274    673 IRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQQL 711
ABC_6TM_Pgp_ABCB1_D2_like cd18578
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ...
771-1088 4.30e-143

Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.


Pssm-ID: 350022 [Multi-domain]  Cd Length: 317  Bit Score: 438.04  E-value: 4.30e-143
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  771 MKLNLTEWPYFVVGVFCAIINGGLQPAFAIIFSKIIGVFTRIDDPETKRQnSNLFSLLFLALGIISFITFFLQGFTFGKA 850
Cdd:cd18578      1 LKLNKPEWPLLLLGLIGAIIAGAVFPVFAILFSKLISVFSLPDDDELRSE-ANFWALMFLVLAIVAGIAYFLQGYLFGIA 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  851 GEILTKRLRYMVFRSMLRQDVSWFDDPKNTTGALTTRLANDAAQVKGAIGSRLAVITQNIANLGTGIIISFIYGWQLTLL 930
Cdd:cd18578     80 GERLTRRLRKLAFRAILRQDIAWFDDPENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLALV 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  931 LLAIVPIIAIAGVVEMKMLSGQALKDKKELEGSGKIATEAIENFRTVVSLTQEQKFEHMYAQSLQVPYRNSLRKAHIFGI 1010
Cdd:cd18578    160 GLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGL 239
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1149123047 1011 TFSFTQAMMYFSYAGCFRFGAYLVAHKLMSFEDVLLVFSAVVFGAMAVGQVSSFAPDYAKAKISAAHIIMIIEKTPLI 1088
Cdd:cd18578    240 GFGLSQSLTFFAYALAFWYGGRLVANGEYTFEQFFIVFMALIFGAQSAGQAFSFAPDIAKAKAAAARIFRLLDRKPEI 317
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
106-696 9.99e-140

Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 443.78  E-value: 9.99e-140
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  106 VFSMFRYSNwLDKLYMVVGTLAAIIHGAGLPLMMLVFGEMTDIFANAGNLEDLMSNItnrsdindtgFFMNLeedMTRYA 185
Cdd:TIGR00958  149 LFRLLGLSG-RDWPWLISAFVFLTLSSLGEMFIPFYTGRVIDTLGGDKGPPALASAI----------FFMCL---LSIAS 214
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  186 YYYSGIGAGVLVAAYiqvsfwclaaGRQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQ 265
Cdd:TIGR00958  215 SVSAGLRGGSFNYTM----------ARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLR 284
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  266 SMATFFTGFIVGFTRGWKLTLVILAISPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELE 345
Cdd:TIGR00958  285 NLVMLLGLLGFMLWLSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEAS 364
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  346 RYNKNLEEAKRIGIKKAITANISIGAAFLLIYASYALAFWYGTTLVLSGEYSIGQVLtvffSVLIGAFSVGQASPSIEAF 425
Cdd:TIGR00958  365 RFKEALEETLQLNKRKALAYAGYLWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLV----SFLLYQEQLGEAVRVLSYV 440
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  426 AN----ARGAAYEIFKIIDNKPSIDSysKSGHKPDNIKGNLEFRNVHFSYPSRKEVKILKGLNLKVQSGQTVALVGNSGC 501
Cdd:TIGR00958  441 YSgmmqAVGASEKVFEYLDRKPNIPL--TGTLAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGS 518
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  502 GKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIGVVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYD 581
Cdd:TIGR00958  519 GKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHD 598
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  582 FIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQValDKARKGRTTIVIAHRLST 661
Cdd:TIGR00958  599 FIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRLST 676
                          570       580       590
                   ....*....|....*....|....*....|....*
gi 1149123047  662 VRNADVIAGFDDGVIVEKGNHDELMKEKGIYFKLV 696
Cdd:TIGR00958  677 VERADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
ABC_6TM_Pgp_ABCB1 cd18558
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ...
781-1078 1.77e-135

Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1(ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.


Pssm-ID: 350002 [Multi-domain]  Cd Length: 312  Bit Score: 417.45  E-value: 1.77e-135
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  781 FVVGVFCAIINGGLQPAFAIIFSKIIGVFT----------------RIDDPETKRQNSNLFSLLFLALGIISFITFFLQG 844
Cdd:cd18558      1 MVVGILCAIIHGGLLPAFMVIFGDMTDSFTnggmtnitgnssglnsSAGPFEKLEEEMTLYAYYYLIIGAIVLITAYIQG 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  845 FTFGKAGEILTKRLRYMVFRSMLRQDVSWFddPKNTTGALTTRLANDAAQVKGAIGSRLAVITQNIANLGTGIIISFIYG 924
Cdd:cd18558     81 SFWGLAAGRQTKKIRYKFFHAIMRQEIGWF--DVNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRG 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  925 WQLTLLLLAIVPIIAIAGVVEMKMLSGQALKDKKELEGSGKIATEAIENFRTVVSLTQEQKFEHMYAQSLQVPYRNSLRK 1004
Cdd:cd18558    159 WKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKK 238
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1149123047 1005 AHIFGITFSFTQAMMYFSYAGCFRFGAYLVAHKLMS-FEDVLLVFSAVVFGAMAVGQVSSFAPdYAKAKISAAHI 1078
Cdd:cd18558    239 AITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSiGEVLTVFFSVLIGAFSAGQQVPSIEA-FANARGAAYHI 312
MsbA_rel TIGR02204
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ...
170-699 6.42e-132

ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.


Pssm-ID: 131259 [Multi-domain]  Cd Length: 576  Bit Score: 418.33  E-value: 6.42e-132
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  170 DTGFFMNLEEDMTRYAYYYSGIGAGVLVAAYIQVSFWCLAAGRQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDV 249
Cdd:TIGR02204   46 DHGFSKDSSGLLNRYFAFLLVVALVLALGTAARFYLVTWLGERVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDT 125
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  250 SKINEGIGDKIGMFFQSMATFFTGFIVGFTRGWKLTLVILAISPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLA 329
Cdd:TIGR02204  126 TLLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLG 205
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  330 AIRTVIAFGGQKKELERYNKNLEEAKRIGIKKAITANISIGAAFLLIYASYALAFWYGTTLVLSGEYSIGQVLTVFFSVL 409
Cdd:TIGR02204  206 AIRTVQAFGHEDAERSRFGGAVEKAYEAARQRIRTRALLTAIVIVLVFGAIVGVLWVGAHDVIAGKMSAGTLGQFVFYAV 285
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  410 IGAFSVGQASPSIEAFANARGAAYEIFKIIDNKPSIDSYSKSGHKPDNIKGNLEFRNVHFSYPSRKEVKILKGLNLKVQS 489
Cdd:TIGR02204  286 MVAGSIGTLSEVWGELQRAAGAAERLIELLQAEPDIKAPAHPKTLPVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRP 365
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  490 GQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIGVVSQEPVLFATTIAENIRYGRENVTMDE 569
Cdd:TIGR02204  366 GETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEE 445
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  570 IEKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARKG 649
Cdd:TIGR02204  446 VEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKG 525
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|
gi 1149123047  650 RTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELMKEKGIYFKLVTMQ 699
Cdd:TIGR02204  526 RTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGGLYARLARLQ 575
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
754-1345 2.31e-131

ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];


Pssm-ID: 441875 [Multi-domain]  Cd Length: 711  Bit Score: 421.55  E-value: 2.31e-131
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  754 TKEALDESIPPVSFWRIMKLNLTEWPYFVVGVFCAIINGGLQ---PAFA-IIFSKIIGvftriddpetkrqNSNLFSLLF 829
Cdd:COG2274    131 TPEFDKRGEKPFGLRWFLRLLRRYRRLLLQVLLASLLINLLAlatPLFTqVVIDRVLP-------------NQDLSTLWV 197
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  830 LALGIISFITF-----FLQGFTFGKAGEILTKRLRYMVFRSMLRQDVSWFDdpKNTTGALTTRLaNDAAQVKGAIGSRLA 904
Cdd:COG2274    198 LAIGLLLALLFegllrLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFE--SRSVGDLASRF-RDVESIREFLTGSLL 274
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  905 VITQNIANLGTGIIISFIYGWQLTLLLLAIVPIIAIAGVV---EMKMLSGQALKDKKELEGsgkIATEAIENFRTVVSLT 981
Cdd:COG2274    275 TALLDLLFVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLfqpRLRRLSREESEASAKRQS---LLVETLRGIETIKALG 351
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  982 QEQKFEHMYAQSLQVPYRNSLRKAHIFGITFSFTQAMMYFSYAGCFRFGAYLVAHKLMSFeDVLLVFSAVVFGAMA-VGQ 1060
Cdd:COG2274    352 AESRFRRRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTL-GQLIAFNILSGRFLApVAQ 430
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1061 VSSFAPDYAKAKISAAHIIMIIEKTPLIDSYSTEGLMPNtLEGNVTFGEVVFNYPTRpDIPVLQGLSLEVKKGQTLALVG 1140
Cdd:COG2274    431 LIGLLQRFQDAKIALERLDDILDLPPEREEGRSKLSLPR-LKGDIELENVSFRYPGD-SPPVLDNISLTIKPGERVAIVG 508
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1141 SSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEPILFDCSIAENIAYGDNSrvVSQEEIVRAAK 1220
Cdd:COG2274    509 RSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPD--ATDEEIIEAAR 586
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1221 EANIHAFIESLPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVI 1300
Cdd:COG2274    587 LAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIII 666
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....*
gi 1149123047 1301 AHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQKGIYFSMVSVQA 1345
Cdd:COG2274    667 AHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQQL 711
ABC_6TM_Pgp_ABCB1_D1_like cd18577
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ...
121-435 2.51e-130

Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.


Pssm-ID: 350021 [Multi-domain]  Cd Length: 300  Bit Score: 403.39  E-value: 2.51e-130
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  121 MVVGTLAAIIHGAGLPLMMLVFGEMTDIFANAGNLEDLMSNitnrsdindtgffmnLEEDMTRYAYYYSGIGAGVLVAAY 200
Cdd:cd18577      1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFTDFGSGESSPDE---------------FLDDVNKYALYFVYLGIGSFVLSY 65
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  201 IQVSFWCLAAGRQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQSMATFFTGFIVGFTR 280
Cdd:cd18577     66 IQTACWTITGERQARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIY 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  281 GWKLTLVILAISPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKRIGIK 360
Cdd:cd18577    146 SWKLTLVLLATLPLIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIK 225
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1149123047  361 KAITANISIGAAFLLIYASYALAFWYGTTLVLSGEYSIGQVLTVFFSVLIGAFSVGQASPSIEAFANARGAAYEI 435
Cdd:cd18577    226 KGLVSGLGLGLLFFIIFAMYALAFWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
768-1341 1.02e-119

Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 389.85  E-value: 1.02e-119
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  768 WRIMKLNLTEWPYFVVG---VFCAIINGGLQPAF-AIIFSKIIGVFtridDPETkrQNSNLFSLLFLALGiiSFITFFLQ 843
Cdd:TIGR00958  150 FRLLGLSGRDWPWLISAfvfLTLSSLGEMFIPFYtGRVIDTLGGDK----GPPA--LASAIFFMCLLSIA--SSVSAGLR 221
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  844 GFTFGKAGEILTKRLRYMVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIGSRLAVITQNIANLGTGIIISFIY 923
Cdd:TIGR00958  222 GGSFNYTMARINLRIREDLFRSLLRQDLGFFD--ENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWL 299
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  924 GWQLTLLLLAIVPIIAIAGVVEMKMLSGQALKDKKELEGSGKIATEAIENFRTVVSLTQE----QKFEHMYAQSLQVPYR 999
Cdd:TIGR00958  300 SPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEegeaSRFKEALEETLQLNKR 379
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1000 NSLRKahifgITFSFTQAMM-YFSYAGCFRFGAYLVAHKLMSFEDvLLVFsavVFGAMAVGQ----VSSFAPDYAKAKIS 1074
Cdd:TIGR00958  380 KALAY-----AGYLWTTSVLgMLIQVLVLYYGGQLVLTGKVSSGN-LVSF---LLYQEQLGEavrvLSYVYSGMMQAVGA 450
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1075 AAHIIMIIEKTPLIDSysTEGLMPNTLEGNVTFGEVVFNYPTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLE 1154
Cdd:TIGR00958  451 SEKVFEYLDRKPNIPL--TGTLAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQ 528
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1155 RFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEPILFDCSIAENIAYGDNSrvVSQEEIVRAAKEANIHAFIESLPNK 1234
Cdd:TIGR00958  529 NLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTD--TPDEEIMAAAKAANAHDFIMEFPNG 606
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1235 YSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEalDKAREGRTCIVIAHRLSTIQNADLIV 1314
Cdd:TIGR00958  607 YDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRLSTVERADQIL 684
                          570       580
                   ....*....|....*....|....*..
gi 1149123047 1315 VFQNGRVKEHGTHQQLLAQKGIYFSMV 1341
Cdd:TIGR00958  685 VLKKGSVVEMGTHKQLMEDQGCYKHLV 711
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
197-699 8.45e-117

lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]


Pssm-ID: 131258 [Multi-domain]  Cd Length: 571  Bit Score: 377.52  E-value: 8.45e-117
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  197 VAAYIQVSFWCLAAGRQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQSMATFFTGFIV 276
Cdd:TIGR02203   69 ICSFVSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIV 148
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  277 GFTRGWKLTLVILAISPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKR 356
Cdd:TIGR02203  149 LLYYSWQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRR 228
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  357 IGIKKAITANISIGAAFLLIYASYALAFWYGTTLVLSGEYSIGQvLTVFFSvligafSVGQASPSIEAFANARG------ 430
Cdd:TIGR02203  229 LAMKMTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGD-FTAFIT------AMIALIRPLKSLTNVNApmqrgl 301
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  431 -AAYEIFKIIDNKPSIDsysKSGHKPDNIKGNLEFRNVHFSYPSRkEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQL 509
Cdd:TIGR02203  302 aAAESLFTLLDSPPEKD---TGTRAIERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNL 377
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  510 MQRLYDPTEGMVSVDGQDIRTINVRFLREIIGVVSQEPVLFATTIAENIRYGR-ENVTMDEIEKAVKEANAYDFIMKLPH 588
Cdd:TIGR02203  378 IPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRtEQADRAEIERALAAAYAQDFVDKLPL 457
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  589 KFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVRNADVI 668
Cdd:TIGR02203  458 GLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRI 537
                          490       500       510
                   ....*....|....*....|....*....|.
gi 1149123047  669 AGFDDGVIVEKGNHDELMKEKGIYFKLVTMQ 699
Cdd:TIGR02203  538 VVMDDGRIVERGTHNELLARNGLYAQLHNMQ 568
MsbA_rel TIGR02204
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ...
823-1344 1.14e-116

ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.


Pssm-ID: 131259 [Multi-domain]  Cd Length: 576  Bit Score: 377.12  E-value: 1.14e-116
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  823 NLFSLLFLALGIISFITFFlQGFTFGKAGEILTKRLRYMVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIGSR 902
Cdd:TIGR02204   59 RYFAFLLVVALVLALGTAA-RFYLVTWLGERVVADIRRAVFAHLISLSPSFFD--KNRSGEVVSRLTTDTTLLQSVIGSS 135
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  903 LAVITQNIANLGTGIIISFIYGWQLTLLLLAIVPIIAIAGVVEMKMLSGQALKDKKELEGSGKIATEAIENFRTVVSLTQ 982
Cdd:TIGR02204  136 LSMALRNALMCIGGLIMMFITSPKLTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGH 215
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  983 EQKFEHMYAQSLQVPYRNSLRKAHIFGITFSFTQAMMYFSYAGCFRFGAYLVAHKLMSFEDV-LLVFSAVvFGAMAVGQV 1061
Cdd:TIGR02204  216 EDAERSRFGGAVEKAYEAARQRIRTRALLTAIVIVLVFGAIVGVLWVGAHDVIAGKMSAGTLgQFVFYAV-MVAGSIGTL 294
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1062 SSFAPDYAKAKISAAHIIMIIEKTPLIDSYSTEGLMPNTLEGNVTFGEVVFNYPTRPDIPVLQGLSLEVKKGQTLALVGS 1141
Cdd:TIGR02204  295 SEVWGELQRAAGAAERLIELLQAEPDIKAPAHPKTLPVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGETVALVGP 374
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1142 SGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEPILFDCSIAENIAYGdnsRV-VSQEEIVRAAK 1220
Cdd:TIGR02204  375 SGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYG---RPdATDEEVEAAAR 451
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1221 EANIHAFIESLPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVI 1300
Cdd:TIGR02204  452 AAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLII 531
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....
gi 1149123047 1301 AHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQKGIYFSMVSVQ 1344
Cdd:TIGR02204  532 AHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGGLYARLARLQ 575
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
203-699 5.96e-113

lipid A ABC transporter ATP-binding protein/permease MsbA;


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 367.42  E-value: 5.96e-113
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  203 VSFWCLA--AGRQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDD------------VSKINEG---IGDKIGMFFQ 265
Cdd:PRK11176    84 ISSYCISwvSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDseqvassssgalITVVREGasiIGLFIMMFYY 163
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  266 SmatfftgfivgftrgWKLTLVILAISPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELE 345
Cdd:PRK11176   164 S---------------WQLSLILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETK 228
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  346 RYNKNLEEAKRIGIKKAITANISIGAAFLLiyASYALAFwygtTLVLSGEYSIGQVL-----TVFFSVLIGAFSVGQASP 420
Cdd:PRK11176   229 RFDKVSNRMRQQGMKMVSASSISDPIIQLI--ASLALAF----VLYAASFPSVMDTLtagtiTVVFSSMIALMRPLKSLT 302
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  421 SIEA-FANARGAAYEIFKIIDNKPSIDSyskSGHKPDNIKGNLEFRNVHFSYPSrKEVKILKGLNLKVQSGQTVALVGNS 499
Cdd:PRK11176   303 NVNAqFQRGMAACQTLFAILDLEQEKDE---GKRVIERAKGDIEFRNVTFTYPG-KEVPALRNINFKIPAGKTVALVGRS 378
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  500 GCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIGVVSQEPVLFATTIAENIRYGRENV-TMDEIEKAVKEAN 578
Cdd:PRK11176   379 GSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAY 458
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  579 AYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHR 658
Cdd:PRK11176   459 AMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHR 538
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|.
gi 1149123047  659 LSTVRNADVIAGFDDGVIVEKGNHDELMKEKGIYFKLVTMQ 699
Cdd:PRK11176   539 LSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQLHKMQ 579
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
333-711 1.59e-112

ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444078 [Multi-domain]  Cd Length: 605  Bit Score: 366.84  E-value: 1.59e-112
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  333 TVIAFGGQKKELERYNKNLEEAKRIGIKKAITAN-ISIGAAfLLIYASYALAFWYGTTLVLSGEYSIGQVltvffsVLIG 411
Cdd:COG5265    230 TVKYFGNEAREARRYDEALARYERAAVKSQTSLAlLNFGQA-LIIALGLTAMMLMAAQGVVAGTMTVGDF------VLVN 302
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  412 AFSvgqaspsIEAFA--NARGAAY-EI----------FKIIDNKPSIdsYSKSGHKPDNIK-GNLEFRNVHFSY-PSRKe 476
Cdd:COG5265    303 AYL-------IQLYIplNFLGFVYrEIrqaladmermFDLLDQPPEV--ADAPDAPPLVVGgGEVRFENVSFGYdPERP- 372
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  477 vkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIGVVSQEPVLFATTIAE 556
Cdd:COG5265    373 --ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAY 450
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  557 NIRYGRENVTMDEIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESE 636
Cdd:COG5265    451 NIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTE 530
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1149123047  637 AVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELMKEKGIYFKLVTMQTAGNEVELENAA 711
Cdd:COG5265    531 RAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQQEEEEAEEALAA 605
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
462-695 1.50e-108

ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213218 [Multi-domain]  Cd Length: 234  Bit Score: 341.90  E-value: 1.50e-108
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIG 541
Cdd:cd03251      1 VEFKNVTFRYPG-DGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  542 VVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKI 621
Cdd:cd03251     80 LVSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1149123047  622 LLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELMKEKGIYFKL 695
Cdd:cd03251    160 LILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
766-1347 4.52e-107

lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]


Pssm-ID: 131258 [Multi-domain]  Cd Length: 571  Bit Score: 350.94  E-value: 4.52e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  766 SFWRIMKLNLTEWPYFVVGVFCAIINGGLQPAFAIIFSKIIgvftriDDPETKRQNSNLFSL------LFLALGIISFIT 839
Cdd:TIGR02203    1 TFRRLWSYVRPYKAGLVLAGVAMILVAATESTLAALLKPLL------DDGFGGRDRSVLWWVplvvigLAVLRGICSFVS 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  840 FFLQGFTFGKageiLTKRLRYMVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIGSRLAVITQNIANLGTGIII 919
Cdd:TIGR02203   75 TYLLSWVSNK----VVRDIRVRMFEKLLGLPVSFFD--RQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIV 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  920 SFIYGWQLTLLLLAIVPIIAIAGVVEMKMLSGQALKDKKELEGSGKIATEAIENFRTVVSLTQEQKFEHMYAQSLQVPYR 999
Cdd:TIGR02203  149 LLYYSWQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRR 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1000 NSLRKAHIFGITFSFTQ-----AMMYFSYAGCFRFGA-YLVAHKLMSFedvllvFSAVVFGAMAVGQVSSFAPDYAKAKI 1073
Cdd:TIGR02203  229 LAMKMTSAGSISSPITQliaslALAVVLFIALFQAQAgSLTAGDFTAF------ITAMIALIRPLKSLTNVNAPMQRGLA 302
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1074 SAAHIIMIIEKTPLIDsysTEGLMPNTLEGNVTFGEVVFNYPTRpDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL 1153
Cdd:TIGR02203  303 AAESLFTLLDSPPEKD---TGTRAIERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLI 378
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1154 ERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEPILFDCSIAENIAYGDnSRVVSQEEIVRAAKEANIHAFIESLPN 1233
Cdd:TIGR02203  379 PRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGR-TEQADRAEIERALAAAYAQDFVDKLPL 457
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1234 KYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLI 1313
Cdd:TIGR02203  458 GLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRI 537
                          570       580       590
                   ....*....|....*....|....*....|....
gi 1149123047 1314 VVFQNGRVKEHGTHQQLLAQKGIYFSMVSVQAGT 1347
Cdd:TIGR02203  538 VVMDDGRIVERGTHNELLARNGLYAQLHNMQFRE 571
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
1105-1337 3.10e-104

ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213218 [Multi-domain]  Cd Length: 234  Bit Score: 330.35  E-value: 3.10e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1105 VTFGEVVFNYPTRPDiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLG 1184
Cdd:cd03251      1 VEFKNVTFRYPGDGP-PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1185 IVSQEPILFDCSIAENIAYGDnsRVVSQEEIVRAAKEANIHAFIESLPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQP 1264
Cdd:cd03251     80 LVSQDVFLFNDTVAENIAYGR--PGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDP 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1149123047 1265 HILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQKGIY 1337
Cdd:cd03251    158 PILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVY 230
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
462-699 2.06e-103

ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213220 [Multi-domain]  Cd Length: 236  Bit Score: 328.04  E-value: 2.06e-103
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSRKevKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIG 541
Cdd:cd03253      1 IEFENVTFAYDPGR--PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  542 VVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKI 621
Cdd:cd03253     79 VVPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPI 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1149123047  622 LLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELMKEKGIYFKLVTMQ 699
Cdd:cd03253    159 LLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
1102-1345 1.63e-101

ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444078 [Multi-domain]  Cd Length: 605  Bit Score: 336.79  E-value: 1.63e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1102 EGNVTFGEVVFNYptRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRA 1181
Cdd:COG5265    355 GGEVRFENVSFGY--DPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRA 432
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1182 HLGIVSQEPILFDCSIAENIAYGDNSrvVSQEEIVRAAKEANIHAFIESLPNKYSTKVGDKGTQLSGGQKQRIAIARALV 1261
Cdd:COG5265    433 AIGIVPQDTVLFNDTIAYNIAYGRPD--ASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLL 510
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1262 RQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQKGIYFSMV 1341
Cdd:COG5265    511 KNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMW 590

                   ....
gi 1149123047 1342 SVQA 1345
Cdd:COG5265    591 ARQQ 594
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
460-690 1.48e-100

ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213221 [Multi-domain]  Cd Length: 229  Bit Score: 319.94  E-value: 1.48e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  460 GNLEFRNVHFSYpsRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREI 539
Cdd:cd03254      1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  540 IGVVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNP 619
Cdd:cd03254     79 IGVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDP 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1149123047  620 KILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELMKEKG 690
Cdd:cd03254    159 KILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
209-690 2.57e-100

ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444012 [Multi-domain]  Cd Length: 563  Bit Score: 332.11  E-value: 2.57e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  209 AAGRQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQSMATFFTGFIVGFTRGWKLTLVI 288
Cdd:COG4988     85 AAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPQLFLAALVPLLILVAVFPLDWLSGLIL 164
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  289 LAISPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKRIGIKKAITANIS 368
Cdd:COG4988    165 LVTAPLIPLFMILVGKGAAKASRRQWRALARLSGHFLDRLRGLTTLKLFGRAKAEAERIAEASEDFRKRTMKVLRVAFLS 244
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  369 IGAAFLLIYASYALAFWYGTTLVLSGEYSIGQVLTV------FFSVL--IGAFsvgqaspsieaF---ANARGAAYEIFK 437
Cdd:COG4988    245 SAVLEFFASLSIALVAVYIGFRLLGGSLTLFAALFVlllapeFFLPLrdLGSF-----------YharANGIAAAEKIFA 313
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  438 IIDNKPSIdsySKSGHKPDNIKGN--LEFRNVHFSYPSRKEVkiLKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYD 515
Cdd:COG4988    314 LLDAPEPA---APAGTAPLPAAGPpsIELEDVSFSYPGGRPA--LDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLP 388
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  516 PTEGMVSVDGQDIRTINVRFLREIIGVVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPHKFDTLVG 595
Cdd:COG4988    389 PYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALPDGLDTPLG 468
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  596 ERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGV 675
Cdd:COG4988    469 EGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGR 548
                          490
                   ....*....|....*
gi 1149123047  676 IVEKGNHDELMKEKG 690
Cdd:COG4988    549 IVEQGTHEELLAKNG 563
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
363-699 1.39e-99

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 330.77  E-value: 1.39e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  363 ITANISIGAAFLLiyasyalafwyGTTLVLSGEYSIGQVLTV--FFSVLIGAFSvgqaspSIEAFAN----ARGAAYEIF 436
Cdd:PRK13657   248 AASTITMLAILVL-----------GAALVQKGQLRVGEVVAFvgFATLLIGRLD------QVVAFINqvfmAAPKLEEFF 310
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  437 KIIDNKPSIDSYSKSGhKPDNIKGNLEFRNVHFSYPSRKEVkiLKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDP 516
Cdd:PRK13657   311 EVEDAVPDVRDPPGAI-DLGRVKGAVEFDDVSFSYDNSRQG--VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDP 387
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  517 TEGMVSVDGQDIRTINVRFLREIIGVVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPHKFDTLVGE 596
Cdd:PRK13657   388 QSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGE 467
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  597 RGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVI 676
Cdd:PRK13657   468 RGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRV 547
                          330       340
                   ....*....|....*....|...
gi 1149123047  677 VEKGNHDELMKEKGIYFKLVTMQ 699
Cdd:PRK13657   548 VESGSFDELVARGGRFAALLRAQ 570
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
1105-1344 1.58e-99

ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213220 [Multi-domain]  Cd Length: 236  Bit Score: 317.25  E-value: 1.58e-99
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1105 VTFGEVVFNYPtrPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLG 1184
Cdd:cd03253      1 IEFENVTFAYD--PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1185 IVSQEPILFDCSIAENIAYGDNSrvVSQEEIVRAAKEANIHAFIESLPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQP 1264
Cdd:cd03253     79 VVPQDTVLFNDTIGYNIRYGRPD--ATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNP 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1265 HILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQKGIYFSMVSVQ 1344
Cdd:cd03253    157 PILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
1103-1335 9.69e-96

ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213221 [Multi-domain]  Cd Length: 229  Bit Score: 306.46  E-value: 9.69e-96
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1103 GNVTFGEVVFNYptRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAH 1182
Cdd:cd03254      1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1183 LGIVSQEPILFDCSIAENIAYGDNSrvVSQEEIVRAAKEANIHAFIESLPNKYSTKVGDKGTQLSGGQKQRIAIARALVR 1262
Cdd:cd03254     79 IGVVLQDTFLFSGTIMENIRLGRPN--ATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLR 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1149123047 1263 QPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQKG 1335
Cdd:cd03254    157 DPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
824-1346 2.80e-94

lipid A ABC transporter ATP-binding protein/permease MsbA;


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 315.81  E-value: 2.80e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  824 LFSLLFLAlGIISFITFFLQGFTFGKageiLTKRLRYMVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIGSRL 903
Cdd:PRK11176    71 VIGLMILR-GITSFISSYCISWVSGK----VVMTMRRRLFGHMMGMPVSFFD--KQSTGTLLSRITYDSEQVASSSSGAL 143
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  904 AVITQNIANLGTGIIISFIYGWQLTLLLLAIVPIIAIA-GVVE-------------MKMLSG---QALKDKKELEGSGKI 966
Cdd:PRK11176   144 ITVVREGASIIGLFIMMFYYSWQLSLILIVIAPIVSIAiRVVSkrfrnisknmqntMGQVTTsaeQMLKGHKEVLIFGGQ 223
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  967 ATEaIENFRTVVSLTQEQKFEHMYAQSLQVPyrnslrkahIFGITFSFTQAMMYFsyagcfrfgaylvahkLMSFEDVLL 1046
Cdd:PRK11176   224 EVE-TKRFDKVSNRMRQQGMKMVSASSISDP---------IIQLIASLALAFVLY----------------AASFPSVMD 277
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1047 VFSA----VVFGAM--------AVGQVSS-FAPDYAKAKISAAHIIMIIEKtplidsySTEGLMPNTLEGNVTFGEVVFN 1113
Cdd:PRK11176   278 TLTAgtitVVFSSMialmrplkSLTNVNAqFQRGMAACQTLFAILDLEQEK-------DEGKRVIERAKGDIEFRNVTFT 350
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1114 YPTRpDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEPILF 1193
Cdd:PRK11176   351 YPGK-EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLF 429
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1194 DCSIAENIAYGDNSRVvSQEEIVRAAKEANIHAFIESLPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEAT 1273
Cdd:PRK11176   430 NDTIANNIAYARTEQY-SREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEAT 508
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1149123047 1274 SALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQKGIYFSMVSVQAG 1346
Cdd:PRK11176   509 SALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQLHKMQFG 581
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
209-695 4.01e-90

ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444011 [Multi-domain]  Cd Length: 569  Bit Score: 303.61  E-value: 4.01e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  209 AAGRQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVskinegigDKIGMFF-QSMATFFTGFIVGFTrgwkLTLV 287
Cdd:COG4987     82 ATLRLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADV--------DALDNLYlRVLLPLLVALLVILA----AVAF 149
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  288 ILAISPVLGLS-------AAVWAKILSSFTDK---ELLAYAKAGAVAE--EVLAAIRTVIAFGGQKKELERYN---KNLE 352
Cdd:COG4987    150 LAFFSPALALVlalglllAGLLLPLLAARLGRragRRLAAARAALRARltDLLQGAAELAAYGALDRALARLDaaeARLA 229
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  353 EAKRigiKKAITANISIGAAFLLIYASYALAFWYGTTLVLSGEYSIGQVLTVFFSVLiGAFSVgqASPSIEAFAN---AR 429
Cdd:COG4987    230 AAQR---RLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPLLALLVLAAL-ALFEA--LAPLPAAAQHlgrVR 303
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  430 GAAYEIFKIIDNKPSIDSYSKSGHKPDNikGNLEFRNVHFSYPSRKEvKILKGLNLKVQSGQTVALVGNSGCGKSTTVQL 509
Cdd:COG4987    304 AAARRLNELLDAPPAVTEPAEPAPAPGG--PSLELEDVSFRYPGAGR-PVLDGLSLTLPPGERVAIVGPSGSGKSTLLAL 380
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  510 MQRLYDPTEGMVSVDGQDIRTINVRFLREIIGVVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPHK 589
Cdd:COG4987    381 LLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDG 460
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  590 FDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIA 669
Cdd:COG4987    461 LDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRIL 540
                          490       500
                   ....*....|....*....|....*.
gi 1149123047  670 GFDDGVIVEKGNHDELMKEKGIYFKL 695
Cdd:COG4987    541 VLEDGRIVEQGTHEELLAQNGRYRQL 566
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
1096-1321 7.68e-90

ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.


Pssm-ID: 213215 [Multi-domain]  Cd Length: 226  Bit Score: 290.14  E-value: 7.68e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1096 LMPNTLEGNVTFGEVVFNYPTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLN 1175
Cdd:cd03248      3 LAPDHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYE 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1176 VQWLRAHLGIVSQEPILFDCSIAENIAYGDNSrvVSQEEIVRAAKEANIHAFIESLPNKYSTKVGDKGTQLSGGQKQRIA 1255
Cdd:cd03248     83 HKYLHSKVSLVGQEPVLFARSLQDNIAYGLQS--CSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVA 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1149123047 1256 IARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRV 1321
Cdd:cd03248    161 IARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
type_I_sec_HlyB TIGR01846
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ...
220-700 1.88e-89

type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 273831 [Multi-domain]  Cd Length: 694  Bit Score: 305.90  E-value: 1.88e-89
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  220 QFFHAIMRQEIGWFDVHDVGELNTRLTDdVSKINEGIGDKIGMFFQSMATFFTGFIVGFTRGWKLTLVILAISPVLGLSA 299
Cdd:TIGR01846  217 RLYRHLLGLPLGYFESRRVGDTVARVRE-LEQIRNFLTGSALTVVLDLLFVVVFLAVMFFYSPTLTGVVIGSLVCYALLS 295
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  300 AVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKRIGIKKAITANISIGAAFLLIYAS 379
Cdd:TIGR01846  296 VFVGPILRKRVEDKFERSAAATSFLVESVTGIETIKATATEPQFQNRWDRQLAAYVAASFRVTNLGNIAGQAIELIQKLT 375
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  380 YALAFWYGTTLVLSGEYSIGQVltVFFSVLIGAFS--VGQASPSIEAFANARGAAYEIFKIIdNKPSiDSYSKSGHKPDN 457
Cdd:TIGR01846  376 FAILLWFGAHLVIGGALSPGQL--VAFNMLAGRVTqpVLRLAQLWQDFQQTGIALERLGDIL-NSPT-EPRSAGLAALPE 451
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  458 IKGNLEFRNVHFSY-PSRKEVkiLKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFL 536
Cdd:TIGR01846  452 LRGAITFENIRFRYaPDSPEV--LSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWL 529
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  537 REIIGVVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALV 616
Cdd:TIGR01846  530 RRQMGVVLQENVLFSRSIRDNIALCNPGAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALV 609
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  617 RNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELMKEKGIYFKLV 696
Cdd:TIGR01846  610 GNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYARLW 689

                   ....
gi 1149123047  697 TMQT 700
Cdd:TIGR01846  690 QQQS 693
ABC_6TM_Pgp_ABCB1_D2_like cd18578
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ...
114-445 5.58e-88

Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.


Pssm-ID: 350022 [Multi-domain]  Cd Length: 317  Bit Score: 288.58  E-value: 5.58e-88
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  114 NWLDKLYMVVGTLAAIIHGAGLPLMMLVFGEMTDIFANAGNLEdlmsnitnrsdindtgffmnLEEDMTRYAYYYSGIGA 193
Cdd:cd18578      4 NKPEWPLLLLGLIGAIIAGAVFPVFAILFSKLISVFSLPDDDE--------------------LRSEANFWALMFLVLAI 63
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  194 GVLVAAYIQVSFWCLAAGRQIHKIRKQFFHAIMRQEIGWFD--VHDVGELNTRLTDDVSKINEGIGDKIGMFFQSMATFF 271
Cdd:cd18578     64 VAGIAYFLQGYLFGIAGERLTRRLRKLAFRAILRQDIAWFDdpENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLV 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  272 TGFIVGFTRGWKLTLVILAISPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNL 351
Cdd:cd18578    144 AGLIIAFVYGWKLALVGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEAL 223
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  352 EEAKRIGIKKAITANISIGAAFLLIYASYALAFWYGTTLVLSGEYSIGQVLTVFFSVLIGAFSVGQASPSIEAFANARGA 431
Cdd:cd18578    224 EEPLKKGLRRALISGLGFGLSQSLTFFAYALAFWYGGRLVANGEYTFEQFFIVFMALIFGAQSAGQAFSFAPDIAKAKAA 303
                          330
                   ....*....|....
gi 1149123047  432 AYEIFKIIDNKPSI 445
Cdd:cd18578    304 AARIFRLLDRKPEI 317
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
769-1335 1.20e-86

ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444012 [Multi-domain]  Cd Length: 563  Bit Score: 293.59  E-value: 1.20e-86
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  769 RIMKLNLTEWPYFVVGVFCAIINGGLQPAFAIIFSKII-GVFTRIDDPetkrqnSNLFSLLFLALGII---SFITFFLQG 844
Cdd:COG4988      7 RLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLaGLIIGGAPL------SALLPLLGLLLAVLllrALLAWLRER 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  845 FTFgKAGEILTKRLRYMVFRSMLRQDVSWFDDPKntTGALTTRLANDAAQVKGAIG-----SRLAVITQnianLGTGIII 919
Cdd:COG4988     81 AAF-RAAARVKRRLRRRLLEKLLALGPAWLRGKS--TGELATLLTEGVEALDGYFArylpqLFLAALVP----LLILVAV 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  920 SFIYgWQLTLLLLAIVPII----AIAGV----------VEMKMLSGQ---ALK----------DKKELEgsgKIATEAiE 972
Cdd:COG4988    154 FPLD-WLSGLILLVTAPLIplfmILVGKgaakasrrqwRALARLSGHfldRLRglttlklfgrAKAEAE---RIAEAS-E 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  973 NFRTvvsltqeqkfehmyaQSLQVpyrnsLRKAhiFGITFsftqAMMYFSYagcfrFGAYLVAhklmsfedVLLVFSAV- 1051
Cdd:COG4988    229 DFRK---------------RTMKV-----LRVA--FLSSA----VLEFFAS-----LSIALVA--------VYIGFRLLg 269
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1052 ----VFGAMAV-----------GQVSSFapdY-AKAK-ISAAHIIMIIEKTPLIDSYSTEGLMPNTLEGNVTFGEVVFNY 1114
Cdd:COG4988    270 gsltLFAALFVlllapefflplRDLGSF---YhARANgIAAAEKIFALLDAPEPAAPAGTAPLPAAGPPSIELEDVSFSY 346
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1115 PTRPdiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEPILFD 1194
Cdd:COG4988    347 PGGR--PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFA 424
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1195 CSIAENIAYGDnsRVVSQEEIVRAAKEANIHAFIESLPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATS 1274
Cdd:COG4988    425 GTIRENLRLGR--PDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTA 502
                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1149123047 1275 ALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQKG 1335
Cdd:COG4988    503 HLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
ABC_membrane pfam00664
ABC transporter transmembrane region; This family represents a unit of six transmembrane ...
121-413 2.95e-84

ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.


Pssm-ID: 459896 [Multi-domain]  Cd Length: 274  Bit Score: 276.45  E-value: 2.95e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  121 MVVGTLAAIIHGAGLPLMMLVFGEMTDIFanagnledlmsnitnrSDINDTGFFmnleeDMTRYAYYYSGIGAGVLVAAY 200
Cdd:pfam00664    1 LILAILLAILSGAISPAFPLVLGRILDVL----------------LPDGDPETQ-----ALNVYSLALLLLGLAQFILSF 59
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  201 IQVSFWCLAAGRQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQSMATFFTGFIVGFTR 280
Cdd:pfam00664   60 LQSYLLNHTGERLSRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYY 139
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  281 GWKLTLVILAISPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKRIGIK 360
Cdd:pfam00664  140 GWKLTLVLLAVLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIK 219
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1149123047  361 KAITANISIGAAFLLIYASYALAFWYGTTLVLSGEYSIGQ--VLTVFFSVLIGAF 413
Cdd:pfam00664  220 KAVANGLSFGITQFIGYLSYALALWFGAYLVISGELSVGDlvAFLSLFAQLFGPL 274
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
462-699 5.17e-84

ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.


Pssm-ID: 213219 [Multi-domain]  Cd Length: 237  Bit Score: 274.36  E-value: 5.17e-84
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIG 541
Cdd:cd03252      1 ITFEHVRFRYKP-DGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVG 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  542 VVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKI 621
Cdd:cd03252     80 VVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRI 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1149123047  622 LLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELMKEKGIYFKLVTMQ 699
Cdd:cd03252    160 LIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
ABC_6TM_Pgp_ABCB1_D1_like cd18577
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ...
781-1078 2.94e-83

Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.


Pssm-ID: 350021 [Multi-domain]  Cd Length: 300  Bit Score: 274.74  E-value: 2.94e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  781 FVVGVFCAIINGGLQPAFAIIFSKIIGVFTRI----DDPETKRQNSNLFSLLFLALGIISFITFFLQGFTFGKAGEILTK 856
Cdd:cd18577      1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFTDFgsgeSSPDEFLDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQAR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  857 RLRYMVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIGSRLAVITQNIANLGTGIIISFIYGWQLTLLLLAIVP 936
Cdd:cd18577     81 RIRKRYLKALLRQDIAWFD--KNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLP 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  937 IIAIAGVVEMKMLSGQALKDKKELEGSGKIATEAIENFRTVVSLTQEQKFEHMYAQSLQVPYRNSLRKAHIFGITFSFTQ 1016
Cdd:cd18577    159 LIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLF 238
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1149123047 1017 AMMYFSYAGCFRFGAYLVAHKLMSFEDVLLVFSAVVFGAMAVGQVSSFAPDYAKAKISAAHI 1078
Cdd:cd18577    239 FIIFAMYALAFWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
455-676 1.86e-82

ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.


Pssm-ID: 213215 [Multi-domain]  Cd Length: 226  Bit Score: 269.34  E-value: 1.86e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  455 PDNIKGNLEFRNVHFSYPSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVR 534
Cdd:cd03248      5 PDHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHK 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  535 FLREIIGVVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARA 614
Cdd:cd03248     85 YLHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARA 164
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1149123047  615 LVRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVI 676
Cdd:cd03248    165 LIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
910-1335 3.70e-81

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 279.15  E-value: 3.70e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  910 IANLGTGIIISFIYGWQLTLLLLAIVPI-IAIAGVVEMKMLSGQALKDKKELEGSGKiATEAIENFRTVVSLTQ---EQK 985
Cdd:PRK13657   141 LVALVVLLPLALFMNWRLSLVLVVLGIVyTLITTLVMRKTKDGQAAVEEHYHDLFAH-VSDAIGNVSVVQSYNRieaETQ 219
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  986 FEHMYAQSL---QVPYRNSLrkAHIFGIT-FSFTQAMMyfsyaGCFRFGAYLVAHKLMSFEDVLlvfSAVVFGAMAVG-- 1059
Cdd:PRK13657   220 ALRDIADNLlaaQMPVLSWW--ALASVLNrAASTITML-----AILVLGAALVQKGQLRVGEVV---AFVGFATLLIGrl 289
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1060 -QVSSFAPDYAKAKISAAHIIMIIEKTPliDSYSTEGLM-PNTLEGNVTFGEVVFNYPTRPdiPVLQGLSLEVKKGQTLA 1137
Cdd:PRK13657   290 dQVVAFINQVFMAAPKLEEFFEVEDAVP--DVRDPPGAIdLGRVKGAVEFDDVSFSYDNSR--QGVEDVSFEAKPGQTVA 365
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1138 LVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEPILFDCSIAENIAYGDNSrvVSQEEIVR 1217
Cdd:PRK13657   366 IVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPD--ATDEEMRA 443
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1218 AAKEANIHAFIESLPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTC 1297
Cdd:PRK13657   444 AAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTT 523
                          410       420       430
                   ....*....|....*....|....*....|....*...
gi 1149123047 1298 IVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQKG 1335
Cdd:PRK13657   524 FIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGG 561
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
854-1342 4.57e-81

ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444011 [Multi-domain]  Cd Length: 569  Bit Score: 278.19  E-value: 4.57e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  854 LTKRLRYMVFRSMLRQDVSWFDDPKntTGALTTRLANDAAQVKGAIgsrLAVITQNIANLGTGIIISFIYGWQLTLLLLA 933
Cdd:COG4987     86 LLADLRVRLYRRLEPLAPAGLARLR--SGDLLNRLVADVDALDNLY---LRVLLPLLVALLVILAAVAFLAFFSPALALV 160
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  934 IVPIIAIAGVVeMKMLSGQALK--DKKELEGSGKIATEAIENFRTVVSLT---QEQKFEHMYAQSLQVPYRNSLRKAHIF 1008
Cdd:COG4987    161 LALGLLLAGLL-LPLLAARLGRraGRRLAAARAALRARLTDLLQGAAELAaygALDRALARLDAAEARLAAAQRRLARLS 239
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1009 GITFSFTQAMMYFSYAGCFRFGAYLVAHKLMSfeDVLLVfsAVVFGAMA----VGQVSSFAPDYAKAKISAAHIIMIIEK 1084
Cdd:COG4987    240 ALAQALLQLAAGLAVVAVLWLAAPLVAAGALS--GPLLA--LLVLAALAlfeaLAPLPAAAQHLGRVRAAARRLNELLDA 315
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1085 TPLIDSYSTEGLMPNTLEgnVTFGEVVFNYPTRPDiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKV 1164
Cdd:COG4987    316 PPAVTEPAEPAPAPGGPS--LELEDVSFRYPGAGR-PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSI 392
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1165 LLDGKEIKRLNVQWLRAHLGIVSQEPILFDCSIAENIAYGDNSrvVSQEEIVRAAKEANIHAFIESLPNKYSTKVGDKGT 1244
Cdd:COG4987    393 TLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPD--ATDEELWAALERVGLGDWLAALPDGLDTWLGEGGR 470
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1245 QLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEH 1324
Cdd:COG4987    471 RLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQ 550
                          490
                   ....*....|....*...
gi 1149123047 1325 GTHQQLLAQKGIYFSMVS 1342
Cdd:COG4987    551 GTHEELLAQNGRYRQLYQ 568
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
1105-1344 4.68e-80

ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.


Pssm-ID: 213219 [Multi-domain]  Cd Length: 237  Bit Score: 263.19  E-value: 4.68e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1105 VTFGEVVFNYptRPDIP-VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHL 1183
Cdd:cd03252      1 ITFEHVRFRY--KPDGPvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1184 GIVSQEPILFDCSIAENIAYGDNSrvVSQEEIVRAAKEANIHAFIESLPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQ 1263
Cdd:cd03252     79 GVVLQENVLFNRSIRDNIALADPG--MSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHN 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1264 PHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQKGIYFSMVSV 1343
Cdd:cd03252    157 PRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQL 236

                   .
gi 1149123047 1344 Q 1344
Cdd:cd03252    237 Q 237
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
462-674 5.81e-80

ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213195 [Multi-domain]  Cd Length: 171  Bit Score: 260.01  E-value: 5.81e-80
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSRkEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIG 541
Cdd:cd03228      1 IEFKNVSFSYPGR-PKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  542 VVSQEPVLFATTIAENIrygrenvtmdeiekavkeanaydfimklphkfdtlvgergaqLSGGQKQRIAIARALVRNPKI 621
Cdd:cd03228     80 YVPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPI 117
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1149123047  622 LLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDG 674
Cdd:cd03228    118 LILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
chvA TIGR01192
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ...
387-696 5.36e-78

glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 130260 [Multi-domain]  Cd Length: 585  Bit Score: 269.84  E-value: 5.36e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  387 GTTLVLSGEYSIGQVLTV--FFSVLIGAFSvgQASPSIEAFANARGAAYEIFKIIDNKPSIDSYSKSGHKPdNIKGNLEF 464
Cdd:TIGR01192  261 GTVLVIKGELSVGEVIAFigFANLLIGRLD--QMSGFITQIFEARAKLEDFFDLEDSVFQREEPADAPELP-NVKGAVEF 337
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  465 RNVHFSYPSRKEVkiLKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIGVVS 544
Cdd:TIGR01192  338 RHITFEFANSSQG--VFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESLRKSIATVF 415
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  545 QEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLL 624
Cdd:TIGR01192  416 QDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIARAILKNAPILVL 495
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1149123047  625 DEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELMKEKGIYFKLV 696
Cdd:TIGR01192  496 DEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQKDGRFYKLL 567
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
1105-1320 1.68e-77

ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213195 [Multi-domain]  Cd Length: 171  Bit Score: 253.07  E-value: 1.68e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1105 VTFGEVVFNYPTRPDiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLG 1184
Cdd:cd03228      1 IEFKNVSFSYPGRPK-PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1185 IVSQEPILFDCSIAENIaygdnsrvvsqeeivraakeanihafieslpnkystkvgdkgtqLSGGQKQRIAIARALVRQP 1264
Cdd:cd03228     80 YVPQDPFLFSGTIRENI--------------------------------------------LSGGQRQRIAIARALLRDP 115
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1149123047 1265 HILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGR 1320
Cdd:cd03228    116 PILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
type_I_sec_HlyB TIGR01846
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ...
1049-1346 4.85e-76

type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 273831 [Multi-domain]  Cd Length: 694  Bit Score: 267.38  E-value: 4.85e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1049 SAVVFGAMAVGQVSSF--------AP---------DYAKAKISAAHIIMIIEkTPLIDSYSTEGLMPNtLEGNVTFGEVV 1111
Cdd:TIGR01846  385 HLVIGGALSPGQLVAFnmlagrvtQPvlrlaqlwqDFQQTGIALERLGDILN-SPTEPRSAGLAALPE-LRGAITFENIR 462
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1112 FNYptRPDIP-VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEP 1190
Cdd:TIGR01846  463 FRY--APDSPeVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQEN 540
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1191 ILFDCSIAENIAYGDNSrvVSQEEIVRAAKEANIHAFIESLPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLD 1270
Cdd:TIGR01846  541 VLFSRSIRDNIALCNPG--APFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFD 618
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1149123047 1271 EATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQKGIYFSMVSVQAG 1346
Cdd:TIGR01846  619 EATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYARLWQQQSG 694
NHLM_micro_ABC1 TIGR03796
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ...
764-1337 7.51e-76

NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]


Pssm-ID: 274788 [Multi-domain]  Cd Length: 710  Bit Score: 267.19  E-value: 7.51e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  764 PVSFWRIMKLNLTEWP----YFVVGVFCAIINGGLQPAFAIIFskiigvftrIDDPETKRQNSNLFSLL---FLALGIIS 836
Cdd:TIGR03796  138 KPSLLRALWRRLRGSRgallYLLLAGLLLVLPGLVIPAFSQIF---------VDEILVQGRQDWLRPLLlgmGLTALLQG 208
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  837 FITFfLQGFTFGKAGEILTKRLRYMVFRSMLRQDVSWFDdpKNTTGALTTRLANdAAQVKGAIGSRLAVITQNIANLGTG 916
Cdd:TIGR03796  209 VLTW-LQLYYLRRLEIKLAVGMSARFLWHILRLPVRFFA--QRHAGDIASRVQL-NDQVAEFLSGQLATTALDAVMLVFY 284
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  917 IIISFIYGWQLTLLLLAIVPIIAIAGVVEMKMLSGQALKDKKELEGSGKIATEAIENFRTVVSLTQEQKFEHMYA--QSL 994
Cdd:TIGR03796  285 ALLMLLYDPVLTLIGIAFAAINVLALQLVSRRRVDANRRLQQDAGKLTGVAISGLQSIETLKASGLESDFFSRWAgyQAK 364
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  995 QVPYRNSL-RKAHIFGItfsFTQAMMYFSYAGCFRFGAYLVAHKLMS------FEDVLLVFSAVVFGAMAVGQ-VSSFAP 1066
Cdd:TIGR03796  365 LLNAQQELgVLTQILGV---LPTLLTSLNSALILVVGGLRVMEGQLTigmlvaFQSLMSSFLEPVNNLVGFGGtLQELEG 441
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1067 DYAKAKISAAHIIMIIEKTPLIDSYSTEglMPNTLEGNVTFGEVVFNYpTRPDIPVLQGLSLEVKKGQTLALVGSSGCGK 1146
Cdd:TIGR03796  442 DLNRLDDVLRNPVDPLLEEPEGSAATSE--PPRRLSGYVELRNITFGY-SPLEPPLIENFSLTLQPGQRVALVGGSGSGK 518
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1147 STVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEPILFDCSIAENIAYGDNSrvVSQEEIVRAAKEANIHA 1226
Cdd:TIGR03796  519 STIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLWDPT--IPDADLVRACKDAAIHD 596
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1227 FIESLPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALdkAREGRTCIVIAHRLST 1306
Cdd:TIGR03796  597 VITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNL--RRRGCTCIIVAHRLST 674
                          570       580       590
                   ....*....|....*....|....*....|.
gi 1149123047 1307 IQNADLIVVFQNGRVKEHGTHQQLLAQKGIY 1337
Cdd:TIGR03796  675 IRDCDEIIVLERGKVVQRGTHEELWAVGGAY 705
NHLM_micro_ABC2 TIGR03797
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ...
782-1344 2.62e-73

NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]


Pssm-ID: 274789 [Multi-domain]  Cd Length: 686  Bit Score: 259.12  E-value: 2.62e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  782 VVGVFCAIInGGLQP-AFAIIFSKIIgvftriddPETKRQnsnLFSLLFLALGIISFITF---FLQGFTFGKAGEILTKR 857
Cdd:TIGR03797  143 AMGLLGTLL-GMLVPiATGILIGTAI--------PDADRS---LLVQIALALLAAAVGAAafqLAQSLAVLRLETRMDAS 210
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  858 LRYMVFRSMLRQDVSWFDdpKNTTGALTTRlANDAAQVKGAIGSRL--AVITQNIANLGTGIIisFIYGWQLTL--LLLA 933
Cdd:TIGR03797  211 LQAAVWDRLLRLPVSFFR--QYSTGDLASR-AMGISQIRRILSGSTltTLLSGIFALLNLGLM--FYYSWKLALvaVALA 285
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  934 IVpIIAIAGVVEMKMLSgqalKDKKELEGSGKIATEAIENFRTVVSL----TQEQKF---EHMYAQSLQVpyrnSLRKAH 1006
Cdd:TIGR03797  286 LV-AIAVTLVLGLLQVR----KERRLLELSGKISGLTVQLINGISKLrvagAENRAFarwAKLFSRQRKL----ELSAQR 356
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1007 IFGITFSFTQAMMYFSYAGCFRFGAYLVAHKLMSFEDVLLVFSAVVFGAMAVGQVSSFAPDYAKAKISAAHIIMIIEKTP 1086
Cdd:TIGR03797  357 IENLLTVFNAVLPVLTSAALFAAAISLLGGAGLSLGSFLAFNTAFGSFSGAVTQLSNTLISILAVIPLWERAKPILEALP 436
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1087 LIDSYSTEglmPNTLEGNVTFGEVVFNYptRPDIP-VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVL 1165
Cdd:TIGR03797  437 EVDEAKTD---PGKLSGAIEVDRVTFRY--RPDGPlILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVF 511
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1166 LDGKEIKRLNVQWLRAHLGIVSQEPILFDCSIAENIAYGDnsrVVSQEEIVRAAKEANIHAFIESLPNKYSTKVGDKGTQ 1245
Cdd:TIGR03797  512 YDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGA---PLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGT 588
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1246 LSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRtcIVIAHRLSTIQNADLIVVFQNGRVKEHG 1325
Cdd:TIGR03797  589 LSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERLKVTR--IVIAHRLSTIRNADRIYVLDAGRVVQQG 666
                          570
                   ....*....|....*....
gi 1149123047 1326 THQQLLAQKGIYFSMVSVQ 1344
Cdd:TIGR03797  667 TYDELMAREGLFAQLARRQ 685
ABC_membrane pfam00664
ABC transporter transmembrane region; This family represents a unit of six transmembrane ...
781-1056 7.97e-73

ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.


Pssm-ID: 459896 [Multi-domain]  Cd Length: 274  Bit Score: 244.09  E-value: 7.97e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  781 FVVGVFCAIINGGLQPAFAIIFSKIIGVFTRIDDPETkrQNSNLFSLLFLALGIISFITFFLQGFTFGKAGEILTKRLRY 860
Cdd:pfam00664    1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPET--QALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRR 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  861 MVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIGSRLAVITQNIANLGTGIIISFIYGWQLTLLLLAIVPIIAI 940
Cdd:pfam00664   79 KLFKKILRQPMSFFD--TNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYIL 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  941 AGVVEMKMLSGQALKDKKELEGSGKIATEAIENFRTVVSLTQEQKFEHMYAQSLQVPYRNSLRKAHIFGITFSFTQAMMY 1020
Cdd:pfam00664  157 VSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGY 236
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1149123047 1021 FSYAGCFRFGAYLVAHKLMSFED--VLLVFSAVVFGAM 1056
Cdd:pfam00664  237 LSYALALWFGAYLVISGELSVGDlvAFLSLFAQLFGPL 274
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
465-1340 6.72e-71

multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]


Pssm-ID: 188098 [Multi-domain]  Cd Length: 1522  Bit Score: 262.19  E-value: 6.72e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  465 RNVHFSYpSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQdirtinvrflreiIGVVS 544
Cdd:TIGR00957  640 HNATFTW-ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-------------VAYVP 705
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  545 QEPVLFATTIAENIRYGREnvTMDEIEKAVKEANAY--DFIMkLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKIL 622
Cdd:TIGR00957  706 QQAWIQNDSLRENILFGKA--LNEKYYQQVLEACALlpDLEI-LPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIY 782
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  623 LLDEATSALDTEseaVVQVALDKA------RKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELMKEKGIYFK-L 695
Cdd:TIGR00957  783 LFDDPLSAVDAH---VGKHIFEHVigpegvLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEfL 859
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  696 VTMQTAGNEVELEN--AADESKSEIDALEMSSNDSRSSLIRKRSTRR---SVRGSQAQDRKLSTKEALDESIPPVSFWRI 770
Cdd:TIGR00957  860 RTYAPDEQQGHLEDswTALVSGEGKEAKLIENGMLVTDVVGKQLQRQlsaSSSDSGDQSRHHGSSAELQKAEAKEETWKL 939
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  771 MKLNLTE---------WPYF-VVGVFCAIINGGL---QPAFAIIFSKIIGVFTriDDP--ETKRQNSNLFSLLFLALGII 835
Cdd:TIGR00957  940 MEADKAQtgqvelsvyWDYMkAIGLFITFLSIFLfvcNHVSALASNYWLSLWT--DDPmvNGTQNNTSLRLSVYGALGIL 1017
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  836 SFITFFLQGFTFGKAGEILTKRLRYMVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIGSRLAVITQNIAN-LG 914
Cdd:TIGR00957 1018 QGFAVFGYSMAVSIGGIQASRVLHQDLLHNKLRSPMSFFE--RTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNvIG 1095
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  915 TGIIISFIygwqlTLLLLAIVPIIAIAGVVEMKMLSGQAlKDKKELEGSGKIA-----TEAIENFRTVVSLTQEQKFEHM 989
Cdd:TIGR00957 1096 ALIVILLA-----TPIAAVIIPPLGLLYFFVQRFYVASS-RQLKRLESVSRSPvyshfNETLLGVSVIRAFEEQERFIHQ 1169
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  990 yaQSLQVpyrNSLRKAhifgitfsftqammYFSYAGCFRF---GAYLVAHKLMSFEDVLLVFSAVVFGAMAVG------- 1059
Cdd:TIGR00957 1170 --SDLKV---DENQKA--------------YYPSIVANRWlavRLECVGNCIVLFAALFAVISRHSLSAGLVGlsvsysl 1230
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1060 QVSSFAPDYAKAKISAAHIIMIIEKtplIDSYS-TEGLMPNTLEGNVT------FGEVVF-NYPTR--PDIP-VLQGLSL 1128
Cdd:TIGR00957 1231 QVTFYLNWLVRMSSEMETNIVAVER---LKEYSeTEKEAPWQIQETAPpsgwppRGRVEFrNYCLRyrEDLDlVLRHINV 1307
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1129 EVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEPILFDCSIAENIaygDNSR 1208
Cdd:TIGR00957 1308 TIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNL---DPFS 1384
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1209 VVSQEEIVRAAKEANIHAFIESLPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEAL 1288
Cdd:TIGR00957 1385 QYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTI 1464
                          890       900       910       920       930
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1149123047 1289 DKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQKGIYFSM 1340
Cdd:TIGR00957 1465 RTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSM 1516
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
460-680 4.24e-70

ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.


Pssm-ID: 213212 [Multi-domain]  Cd Length: 220  Bit Score: 234.02  E-value: 4.24e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  460 GNLEFRNVHFSYPSrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREI 539
Cdd:cd03245      1 GRIEFRNVSFSYPN-QEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  540 IGVVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNP 619
Cdd:cd03245     80 IGYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDP 159
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1149123047  620 KILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKG 680
Cdd:cd03245    160 PILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
174-698 8.89e-68

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 251.87  E-value: 8.89e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  174 FMNLEEDMTRYAYYYSGIGAGVLVAAYIQvSFWCLAAGRQIHK-IRKQFFHAIMRQEIGWFD--VHDVGELNTRLTDDVS 250
Cdd:PTZ00265   858 FANLEANSNKYSLYILVIAIAMFISETLK-NYYNNVIGEKVEKtMKRRLFENILYQEISFFDqdKHAPGLLSAHINRDVH 936
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  251 KINEGIGDKIGMFFQSMATFFTGFIVGF----------TRGWKLTLVILAISPVLGLSAAVWAK-------ILSSFTDKE 313
Cdd:PTZ00265   937 LLKTGLVNNIVIFTHFIVLFLVSMVMSFyfcpivaavlTGTYFIFMRVFAIRARLTANKDVEKKeinqpgtVFAYNSDDE 1016
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  314 LlaYAKAGAVAEEVLAAIRTVIAFGgqkkeLERYNKNLEEA----KRIGIKKAITAN-----ISIGAAFLLiyasYALAF 384
Cdd:PTZ00265  1017 I--FKDPSFLIQEAFYNMNTVIIYG-----LEDYFCNLIEKaidySNKGQKRKTLVNsmlwgFSQSAQLFI----NSFAY 1085
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  385 WYGTTLVLSGEYSIGQVLTVFFSVLIGAFSVGQASPSIEAFANARGAAYEIFKIIDNKPSIDSYSKSGHKPDN---IKGN 461
Cdd:PTZ00265  1086 WFGSFLIRRGTILVDDFMKSLFTFLFTGSYAGKLMSLKGDSENAKLSFEKYYPLIIRKSNIDVRDNGGIRIKNkndIKGK 1165
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYD-------------------------- 515
Cdd:PTZ00265  1166 IEIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqdyqgd 1245
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  516 ----------------------------PTEGMVSVDGQDIRTINVRFLREIIGVVSQEPVLFATTIAENIRYGRENVTM 567
Cdd:PTZ00265  1246 eeqnvgmknvnefsltkeggsgedstvfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATR 1325
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  568 DEIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVAL---- 643
Cdd:PTZ00265  1326 EDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIvdik 1405
                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1149123047  644 DKARKgrTTIVIAHRLSTVRNADVIAGFDD----GVIVE-KGNHDELMK-EKGIYFKLVTM 698
Cdd:PTZ00265  1406 DKADK--TIITIAHRIASIKRSDKIVVFNNpdrtGSFVQaHGTHEELLSvQDGVYKKYVKL 1464
NHLM_micro_ABC2 TIGR03797
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ...
231-699 1.60e-66

NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]


Pssm-ID: 274789 [Multi-domain]  Cd Length: 686  Bit Score: 239.09  E-value: 1.60e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  231 GWFDVHDVGELNTRlTDDVSKINEGIGDK-IGMFFQSMATFFTgFIVGFTRGWKLTLVILAISPVLGLSAAVWAKILssf 309
Cdd:TIGR03797  225 SFFRQYSTGDLASR-AMGISQIRRILSGStLTTLLSGIFALLN-LGLMFYYSWKLALVAVALALVAIAVTLVLGLLQ--- 299
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  310 TDKELLAYAKAGAVAEEVLAAIRTVIAF---GGQKKELERYNKNLEEAKRIGIKKAITANI--SIGAAFLLIyASYALaF 384
Cdd:TIGR03797  300 VRKERRLLELSGKISGLTVQLINGISKLrvaGAENRAFARWAKLFSRQRKLELSAQRIENLltVFNAVLPVL-TSAAL-F 377
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  385 WYGTTLVLSGEYSIGQVLTvfFSVLIGAF--SVGQASPSIEAfANARGAAYEIFK-IIDNKPSIDSYSKsghKPDNIKGN 461
Cdd:TIGR03797  378 AAAISLLGGAGLSLGSFLA--FNTAFGSFsgAVTQLSNTLIS-ILAVIPLWERAKpILEALPEVDEAKT---DPGKLSGA 451
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSRKEVkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIG 541
Cdd:TIGR03797  452 IEVDRVTFRYRPDGPL-ILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLG 530
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  542 VVSQEPVLFATTIAENIrYGRENVTMDEIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKI 621
Cdd:TIGR03797  531 VVLQNGRLMSGSIFENI-AGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRI 609
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1149123047  622 LLLDEATSALDTESEAVVQVALDKARKGRttIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELMKEKGIYFKLVTMQ 699
Cdd:TIGR03797  610 LLFDEATSALDNRTQAIVSESLERLKVTR--IVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGLFAQLARRQ 685
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
191-715 3.36e-66

SmdA family multidrug ABC transporter permease/ATP-binding protein;


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 235.38  E-value: 3.36e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  191 IGAGVLVAA--YIQVSFWCL----AAGRQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFF 264
Cdd:PRK10789    39 IGTMVLIAVvvYLLRYVWRVllfgASYQLAVELREDFYRQLSRQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLV 118
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  265 QSMATFFTGFIVGFTR-GWKLTLVILAISPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKE 343
Cdd:PRK10789   119 DSLVMGCAVLIVMSTQiSWQLTLLALLPMPVMAIMIKRYGDQLHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQ 198
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  344 LERY--------NKNLEEAkRIGIKKAITANISIGAAFLLiyasyalAFWYGTTLVLSGEYSIGQvLTVFFSVLigafsv 415
Cdd:PRK10789   199 SALFaadaedtgKKNMRVA-RIDARFDPTIYIAIGMANLL-------AIGGGSWMVVNGSLTLGQ-LTSFVMYL------ 263
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  416 GQASPSIEAFA---N--ARG-AAY-EIFKIIDNKPSIdsysKSGHKP-DNIKGNLEFRNVHFSYPsRKEVKILKGLNLKV 487
Cdd:PRK10789   264 GLMIWPMLALAwmfNivERGsAAYsRIRAMLAEAPVV----KDGSEPvPEGRGELDVNIRQFTYP-QTDHPALENVNFTL 338
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  488 QSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIGVVSQEPVLFATTIAENIRYGRENVTM 567
Cdd:PRK10789   339 KPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDATQ 418
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  568 DEIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKAR 647
Cdd:PRK10789   419 QEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWG 498
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1149123047  648 KGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELMKEKGIYFKLVTMQtagnevELENAADESK 715
Cdd:PRK10789   499 EGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMYRYQ------QLEAALDDAP 560
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
1103-1321 9.47e-66

ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.


Pssm-ID: 213212 [Multi-domain]  Cd Length: 220  Bit Score: 221.69  E-value: 9.47e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1103 GNVTFGEVVFNYPTRPdIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAH 1182
Cdd:cd03245      1 GRIEFRNVSFSYPNQE-IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1183 LGIVSQEPILFDCSIAENIAYGDnsRVVSQEEIVRAAKEANIHAFIESLPNKYSTKVGDKGTQLSGGQKQRIAIARALVR 1262
Cdd:cd03245     80 IGYVPQDVTLFYGTLRDNITLGA--PLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLN 157
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1149123047 1263 QPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRV 1321
Cdd:cd03245    158 DPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
424-668 2.16e-65

thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD


Pssm-ID: 274323 [Multi-domain]  Cd Length: 529  Bit Score: 231.79  E-value: 2.16e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  424 AFANARGAAYEIFKIIDNKPSIDSYSKSghKPDNIKGNLEFRNVHFSYPSRKEVkiLKGLNLKVQSGQTVALVGNSGCGK 503
Cdd:TIGR02857  286 ARADGVAAAEALFAVLDAAPRPLAGKAP--VTAAPASSLEFSGVSVAYPGRRPA--LRPVSFTVPPGERVALVGPSGAGK 361
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  504 STTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIGVVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYDFI 583
Cdd:TIGR02857  362 STLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFV 441
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  584 MKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVR 663
Cdd:TIGR02857  442 AALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAA 521

                   ....*
gi 1149123047  664 NADVI 668
Cdd:TIGR02857  522 LADRI 526
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
460-681 1.17e-64

ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.


Pssm-ID: 213211 [Multi-domain]  Cd Length: 221  Bit Score: 218.52  E-value: 1.17e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  460 GNLEFRNVHFSYPSRKEVkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREI 539
Cdd:cd03244      1 GDIEFKNVSLRYRPNLPP-VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSR 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  540 IGVVSQEPVLFATTIAENI----RYgrenvTMDEIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARAL 615
Cdd:cd03244     80 ISIIPQDPVLFSGTIRSNLdpfgEY-----SDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARAL 154
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1149123047  616 VRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGN 681
Cdd:cd03244    155 LRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
1102-1333 5.25e-64

ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 443660 [Multi-domain]  Cd Length: 563  Bit Score: 228.48  E-value: 5.25e-64
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1102 EGNVTFGEVVFNYPTRpDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRA 1181
Cdd:COG4618    328 KGRLSVENLTVVPPGS-KRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGR 406
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1182 HLGIVSQEPILFDCSIAENIA-YGDnsrvVSQEEIVRAAKEANIHAFIESLPNKYSTKVGDKGTQLSGGQKQRIAIARAL 1260
Cdd:COG4618    407 HIGYLPQDVELFDGTIAENIArFGD----ADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARAL 482
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1149123047 1261 VRQPHILLLDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQ 1333
Cdd:COG4618    483 YGDPRLVVLDEPNSNLDDEGEAALAAAIRALKArGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
827-1344 3.73e-63

SmdA family multidrug ABC transporter permease/ATP-binding protein;


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 226.13  E-value: 3.73e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  827 LLFLALgIISFITFFLQGFTFGkAGEILTKRLRYMVFRSMLRQDVSWFddPKNTTGALTTRLANDAAQVKGAIGSR-LAV 905
Cdd:PRK10789    42 MVLIAV-VVYLLRYVWRVLLFG-ASYQLAVELREDFYRQLSRQHPEFY--LRHRTGDLMARATNDVDRVVFAAGEGvLTL 117
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  906 ITQNIANLGTGIIISFIYGWQLTLLLLAIVPIIAIA-----GVVEMKMLSGQA----LKDKkelegsgkiATEAIENFRT 976
Cdd:PRK10789   118 VDSLVMGCAVLIVMSTQISWQLTLLALLPMPVMAIMikrygDQLHERFKLAQAafssLNDR---------TQESLTSIRM 188
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  977 VVSLTQEQKFEHMYAQSLQVPYRNSLRKAHI---FGITFSFTQAMMYFSYAGCfrfGAYLVAHklmsfedvllvfsavvf 1053
Cdd:PRK10789   189 IKAFGLEDRQSALFAADAEDTGKKNMRVARIdarFDPTIYIAIGMANLLAIGG---GSWMVVN----------------- 248
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1054 GAMAVGQVSSFA--------PDYAKA-------KISAAH--IIMIIEKTPLIDSySTEGLM--PNTLEGNVTfgevVFNY 1114
Cdd:PRK10789   249 GSLTLGQLTSFVmylglmiwPMLALAwmfniveRGSAAYsrIRAMLAEAPVVKD-GSEPVPegRGELDVNIR----QFTY 323
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1115 PTRpDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEPILFD 1194
Cdd:PRK10789   324 PQT-DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFS 402
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1195 CSIAENIAYGDNSrvVSQEEIVRAAKEANIHAFIESLPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATS 1274
Cdd:PRK10789   403 DTVANNIALGRPD--ATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALS 480
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1275 ALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQKGIYFSMVSVQ 1344
Cdd:PRK10789   481 AVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMYRYQ 550
PLN03232 PLN03232
ABC transporter C family member; Provisional
462-1341 1.93e-62

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 234.87  E-value: 1.93e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEgMVSVDgqdirtinvrfLREIIG 541
Cdd:PLN03232   615 ISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAE-TSSVV-----------IRGSVA 682
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  542 VVSQEPVLFATTIAENIRYGRENvtmdEIEKAVKeanAYDfIMKLPHKFD-------TLVGERGAQLSGGQKQRIAIARA 614
Cdd:PLN03232   683 YVPQVSWIFNATVRENILFGSDF----ESERYWR---AID-VTALQHDLDllpgrdlTEIGERGVNISGGQKQRVSMARA 754
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  615 LVRNPKILLLDEATSALDTE-SEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELMKEKGIYF 693
Cdd:PLN03232   755 VYSNSDIYIFDDPLSALDAHvAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFK 834
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  694 KLvtMQTAG--NEVELENAADESKSEIDA-LEMSSNDSRSSLIRKRSTRRSVrgsqaqdrkLSTKEALDESIppVSFWRI 770
Cdd:PLN03232   835 KL--MENAGkmDATQEVNTNDENILKLGPtVTIDVSERNLGSTKQGKRGRSV---------LVKQEERETGI--ISWNVL 901
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  771 MKLNLTEWPYFVVGVF--CAIinggLQPAFAIIFSKIIGVFTRIDDPETKRQNSNLFSLLFLALGIISFItfFLQGFTFG 848
Cdd:PLN03232   902 MRYNKAVGGLWVVMILlvCYL----TTEVLRVSSSTWLSIWTDQSTPKSYSPGFYIVVYALLGFGQVAVT--FTNSFWLI 975
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  849 KAGEILTKRLRYMVFRSMLRQDVSWFDdpKNTTGALTTRLANDaaqvkgaIGSrlavITQNIANLGTGIIISFiygWQL- 927
Cdd:PLN03232   976 SSSLHAAKRLHDAMLNSILRAPMLFFH--TNPTGRVINRFSKD-------IGD----IDRNVANLMNMFMNQL---WQLl 1039
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  928 -TLLLLAIVPIIAIAGVVEMKMLSGQAL-------KDKKELEGSGKIAT-----EAIENFRTVVSLTQEQKFEHMYAQSL 994
Cdd:PLN03232  1040 sTFALIGTVSTISLWAIMPLLILFYAAYlyyqstsREVRRLDSVTRSPIyaqfgEALNGLSSIRAYKAYDRMAKINGKSM 1119
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  995 QVPYRNSLRKAHIFG---ITFSFTQAMMYFSYA--GCFRFGAYLVAHKLMSFEDVLLVFSAVVFGAMA--VGQVSSFAPD 1067
Cdd:PLN03232  1120 DNNIRFTLANTSSNRwltIRLETLGGVMIWLTAtfAVLRNGNAENQAGFASTMGLLLSYTLNITTLLSgvLRQASKAENS 1199
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1068 YAKAKISAAHIIMIIEKTPLIDSYSTEGLMPntLEGNVTFGEVVFNYptRPDIP-VLQGLSLEVKKGQTLALVGSSGCGK 1146
Cdd:PLN03232  1200 LNSVERVGNYIDLPSEATAIIENNRPVSGWP--SRGSIKFEDVHLRY--RPGLPpVLHGLSFFVSPSEKVGVVGRTGAGK 1275
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1147 STVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEPILFDCSIAENIaygDNSRVVSQEEIVRAAKEANIHA 1226
Cdd:PLN03232  1276 SSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNI---DPFSEHNDADLWEALERAHIKD 1352
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1227 FIESLPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLST 1306
Cdd:PLN03232  1353 VIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNT 1432
                          890       900       910
                   ....*....|....*....|....*....|....*.
gi 1149123047 1307 IQNADLIVVFQNGRVKEHGTHQQLLAQKG-IYFSMV 1341
Cdd:PLN03232  1433 IIDCDKILVLSSGQVLEYDSPQELLSRDTsAFFRMV 1468
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
1103-1326 4.38e-61

ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.


Pssm-ID: 213211 [Multi-domain]  Cd Length: 221  Bit Score: 208.50  E-value: 4.38e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1103 GNVTFGEVVFNYptRPDI-PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRA 1181
Cdd:cd03244      1 GDIEFKNVSLRY--RPNLpPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1182 HLGIVSQEPILFDCSIAENIaygDNSRVVSQEEIVRAAKEANIHAFIESLPNKYSTKVGDKGTQLSGGQKQRIAIARALV 1261
Cdd:cd03244     79 RISIIPQDPVLFSGTIRSNL---DPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALL 155
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1149123047 1262 RQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGT 1326
Cdd:cd03244    156 RKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
286-688 8.80e-61

ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 443660 [Multi-domain]  Cd Length: 563  Bit Score: 219.23  E-value: 8.80e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  286 LVILAISPVLGLSAAVWAKILSSFT------DKELL-----AYAKAGAVAEEVLAAIRTVIAFG----GQKKELERYNKN 350
Cdd:COG4618    148 AVLFLFHPLLGLLALVGALVLVALAllnerlTRKPLkeaneAAIRANAFAEAALRNAEVIEAMGmlpaLRRRWQRANARA 227
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  351 LEEAKRIGIKKAITANISIGAAFLLIYASYALAFWygttLVLSGEYSIGqvltVFF--SVLIG-AFS-VGQASPSIEAFA 426
Cdd:COG4618    228 LALQARASDRAGGFSALSKFLRLLLQSAVLGLGAY----LVIQGEITPG----AMIaaSILMGrALApIEQAIGGWKQFV 299
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  427 NARGAAYEIFKIIDNKPSIDSYSKSGhKPdniKGNLEFRNVHFSYPSRKEVkILKGLNLKVQSGQTVALVGNSGCGKSTT 506
Cdd:COG4618    300 SARQAYRRLNELLAAVPAEPERMPLP-RP---KGRLSVENLTVVPPGSKRP-ILRGVSFSLEPGEVLGVIGPSGSGKSTL 374
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  507 VQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIGVVSQEPVLFATTIAENI-RYGreNVTMDEIEKAVKEANAYDFIMK 585
Cdd:COG4618    375 ARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIaRFG--DADPEKVVAAAKLAGVHEMILR 452
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  586 LPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARK-GRTTIVIAHRLSTVRN 664
Cdd:COG4618    453 LPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKArGATVVVITHRPSLLAA 532
                          410       420
                   ....*....|....*....|....
gi 1149123047  665 ADVIAGFDDGVIVEKGNHDELMKE 688
Cdd:COG4618    533 VDKLLVLRDGRVQAFGPRDEVLAR 556
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
829-1344 1.29e-60

SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 219.59  E-value: 1.29e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  829 FLALGIISFITFFLQGFTFGKAGEILTKRLRYMVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIGSRLAVITQ 908
Cdd:PRK10790    71 YVGLQLLAAGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSAFD--TQPVGQLISRVTNDTEVIRDLYVTVVATVLR 148
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  909 NIANLGTGIIISFIYGWQLTLLLLAIVPIIAIAGVVEMKMLSGQALKDKKELEGSGKIATEAIENFRTVVSLTQEQKF-E 987
Cdd:PRK10790   149 SAALIGAMLVAMFSLDWRMALVAIMIFPAVLVVMVIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQARFgE 228
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  988 HMYAQSlqvpyrnslrKAHifgitfsftqammYFSYAGCFRFGAYLVAHKLMSFE-----DVLLVFSAVVFGAMAVGQVS 1062
Cdd:PRK10790   229 RMGEAS----------RSH-------------YMARMQTLRLDGFLLRPLLSLFSalilcGLLMLFGFSASGTIEVGVLY 285
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1063 SFapdyakakISaaHIIMIIEktPLIDSYSTEGLMPNTL-------------------------EGNVTFGEVVFNYptR 1117
Cdd:PRK10790   286 AF--------IS--YLGRLNE--PLIELTTQQSMLQQAVvagervfelmdgprqqygnddrplqSGRIDIDNVSFAY--R 351
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1118 PDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEPILFDCSI 1197
Cdd:PRK10790   352 DDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTF 431
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1198 AENIAYGdnsRVVSQEEIVRAAKEANIHAFIESLPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALD 1277
Cdd:PRK10790   432 LANVTLG---RDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANID 508
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1149123047 1278 TESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQKGIYFSMVSVQ 1344
Cdd:PRK10790   509 SGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQLQ 575
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
197-697 5.21e-60

ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]


Pssm-ID: 130261 [Multi-domain]  Cd Length: 708  Bit Score: 220.38  E-value: 5.21e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  197 VAAYIQVSFWCLAAGRQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDdVSKINEGIGDKIGMFFQSMATFFT-GFI 275
Cdd:TIGR01193  211 ILSYIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGEIVSRFTD-ASSIIDALASTILSLFLDMWILVIvGLF 289
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  276 VGFtRGWKLTLVILAISPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGqkkELERYNK------ 349
Cdd:TIGR01193  290 LVR-QNMLLFLLSLLSIPVYAVIIILFKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTS---EAERYSKidsefg 365
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  350 -NLEEAKRIGIKKAITANISIGAAFLLIyasyALAFWYGTTLVLSGEYSIGQVLTvfFSVLIGAF-----SVGQASPSIE 423
Cdd:TIGR01193  366 dYLNKSFKYQKADQGQQAIKAVTKLILN----VVILWTGAYLVMRGKLTLGQLIT--FNALLSYFltpleNIINLQPKLQ 439
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  424 AFANARGAAYEIFKIidnkPSIDSYSKSGHKPDNIKGNLEFRNVHFSYPSRKEvkILKGLNLKVQSGQTVALVGNSGCGK 503
Cdd:TIGR01193  440 AARVANNRLNEVYLV----DSEFINKKKRTELNNLNGDIVINDVSYSYGYGSN--ILSDISLTIKMNSKTTIVGMSGSGK 513
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  504 STTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIGVVSQEPVLFATTIAENIRYG-RENVTMDEIEKAVKEANAYDF 582
Cdd:TIGR01193  514 STLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGaKENVSQDEIWAACEIAEIKDD 593
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  583 IMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKArKGRTTIVIAHRLSTV 662
Cdd:TIGR01193  594 IENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNL-QDKTIIFVAHRLSVA 672
                          490       500       510
                   ....*....|....*....|....*....|....*
gi 1149123047  663 RNADVIAGFDDGVIVEKGNHDELMKEKGIYFKLVT 697
Cdd:TIGR01193  673 KQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLIH 707
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
1060-1315 2.84e-59

thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD


Pssm-ID: 274323 [Multi-domain]  Cd Length: 529  Bit Score: 213.69  E-value: 2.84e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1060 QVSSFAPDYAKAKISAAHIIMIIEKTPLIDSYSTEGLMPNTLEgnVTFGEVVFNYPTRPdiPVLQGLSLEVKKGQTLALV 1139
Cdd:TIGR02857  279 QLGAQYHARADGVAAAEALFAVLDAAPRPLAGKAPVTAAPASS--LEFSGVSVAYPGRR--PALRPVSFTVPPGERVALV 354
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1140 GSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEPILFDCSIAENIAYGDnsRVVSQEEIVRAA 1219
Cdd:TIGR02857  355 GPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLAR--PDASDAEIREAL 432
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1220 KEANIHAFIESLPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIV 1299
Cdd:TIGR02857  433 ERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLL 512
                          250
                   ....*....|....*.
gi 1149123047 1300 IAHRLSTIQNADLIVV 1315
Cdd:TIGR02857  513 VTHRLALAALADRIVV 528
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
196-716 1.73e-58

SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 213.04  E-value: 1.73e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  196 LVAA---YIQVSFWCLAAGRQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQSMATFFT 272
Cdd:PRK10790    76 LLAAglhYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDLYVTVVATVLRSAALIGA 155
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  273 GFIVGFTRGWKLTLVILAISPVLGLSAAVWAKiLSSFTDKELLAY-AKAGAVAEEVLAAIrTVIAfggQKKELERYNKNL 351
Cdd:PRK10790   156 MLVAMFSLDWRMALVAIMIFPAVLVVMVIYQR-YSTPIVRRVRAYlADINDGFNEVINGM-SVIQ---QFRQQARFGERM 230
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  352 EEAKRIGIKKAITA----------NISIGAAFLLIyasyALAFWYGttlvLSGEYSIG-QVLTVFFSVLiGAFSvgqaSP 420
Cdd:PRK10790   231 GEASRSHYMARMQTlrldgfllrpLLSLFSALILC----GLLMLFG----FSASGTIEvGVLYAFISYL-GRLN----EP 297
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  421 SIE------AFANARGAAYEIFKIIDNkpsidsySKSGHKPDNI---KGNLEFRNVHFSYpsRKEVKILKGLNLKVQSGQ 491
Cdd:PRK10790   298 LIElttqqsMLQQAVVAGERVFELMDG-------PRQQYGNDDRplqSGRIDIDNVSFAY--RDDNLVLQNINLSVPSRG 368
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  492 TVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIGVVSQEPVLFATTIAENIRYGReNVTMDEIE 571
Cdd:PRK10790   369 FVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGR-DISEEQVW 447
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  572 KAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARKGRT 651
Cdd:PRK10790   448 QALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTT 527
                          490       500       510       520       530       540
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1149123047  652 TIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELMKEKGIYFKLVTMQTAGNEVELENAADESKS 716
Cdd:PRK10790   528 LVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQLQLAGEELAASVREEESLS 592
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
1051-1340 2.02e-58

cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 212.38  E-value: 2.02e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1051 VVFGAMA--------------VGQVSSfapdyakakiSAAHIIMIIEKTPLIDSYSTEGLMPNtlEGNVTFGEVVFNYPT 1116
Cdd:PRK11160   283 FVFAALAafealmpvagafqhLGQVIA----------SARRINEITEQKPEVTFPTTSTAAAD--QVSLTLNNVSFTYPD 350
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1117 RPDiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEPILFDCS 1196
Cdd:PRK11160   351 QPQ-PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSAT 429
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1197 IAENIAYGDNSrvVSQEEIVRAAKEANIHAFIESlPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSAL 1276
Cdd:PRK11160   430 LRDNLLLAAPN--ASDEALIEVLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGL 506
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1149123047 1277 DTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQKGIYFSM 1340
Cdd:PRK11160   507 DAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQL 570
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
288-659 3.00e-58

thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.


Pssm-ID: 274331 [Multi-domain]  Cd Length: 530  Bit Score: 210.68  E-value: 3.00e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  288 ILAISPVLGLSAAVWAKILSSFTDKELLAYAKaGAVAEEVLAAIR---TVIAFGGQKKELERYNKNLEEAKRIGIKKAIT 364
Cdd:TIGR02868  158 ILAAGLLLAGFVAPLVSLRAARAAEQALARLR-GELAAQLTDALDgaaELVASGALPAALAQVEEADRELTRAERRAAAA 236
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  365 ANISIGAAFLLIYASYALAFWYGTTLVLSGEYSiGQVLTVFFSVLIGAF-SVGQASPSIEAFANARGAAYEIFKIIDNKP 443
Cdd:TIGR02868  237 TALGAALTLLAAGLAVLGALWAGGPAVADGRLA-PVTLAVLVLLPLAAFeAFAALPAAAQQLTRVRAAAERIVEVLDAAG 315
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  444 SIDSYSKSGHKPDNIKG-NLEFRNVHFSYPSRKEVkiLKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVS 522
Cdd:TIGR02868  316 PVAEGSAPAAGAVGLGKpTLELRDLSAGYPGAPPV--LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVT 393
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  523 VDGQDIRTINVRFLREIIGVVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLS 602
Cdd:TIGR02868  394 LDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLS 473
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1149123047  603 GGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRL 659
Cdd:TIGR02868  474 GGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
PLN03130 PLN03130
ABC transporter C family member; Provisional
465-1341 3.95e-58

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 221.54  E-value: 3.95e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  465 RNVHFSYPSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVdgqdirtinvrfLREIIGVVS 544
Cdd:PLN03130   618 KNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV------------IRGTVAYVP 685
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  545 QEPVLFATTIAENIRYGREnVTMDEIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLL 624
Cdd:PLN03130   686 QVSWIFNATVRDNILFGSP-FDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIF 764
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  625 DEATSALDTE-SEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELMKEKGIYFKLvtMQTAGn 703
Cdd:PLN03130   765 DDPLSALDAHvGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKL--MENAG- 841
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  704 evELENAADESKSEIDalemsSNDSRSSLIRKRSTRRSVRGSQAQDRK-----LSTKEALDESIppVSFWRIMKLNLTEW 778
Cdd:PLN03130   842 --KMEEYVEENGEEED-----DQTSSKPVANGNANNLKKDSSSKKKSKegksvLIKQEERETGV--VSWKVLERYKNALG 912
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  779 PYFVVGV--FCAIinggLQPAFAIIFSKIIGVFTriDDPETKRQNSNLFSLLFLALGIISFITFFLQGFTFGKAGEILTK 856
Cdd:PLN03130   913 GAWVVMIlfLCYV----LTEVFRVSSSTWLSEWT--DQGTPKTHGPLFYNLIYALLSFGQVLVTLLNSYWLIMSSLYAAK 986
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  857 RLRYMVFRSMLRQDVSWFDdpKNTTGALTTRLANDAaqvkGAIGSRLAVITQNIAN-----LGTGIIISFIYgwqlTLLL 931
Cdd:PLN03130   987 RLHDAMLGSILRAPMSFFH--TNPLGRIINRFAKDL----GDIDRNVAVFVNMFLGqifqlLSTFVLIGIVS----TISL 1056
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  932 LAIVPI-IAIAGVVEMKMLSGQALKDKKELEGSGKIAT--EAIENFRTVVSLTQEQKFEHMYAQSLQVPYRNSL---RKA 1005
Cdd:PLN03130  1057 WAIMPLlVLFYGAYLYYQSTAREVKRLDSITRSPVYAQfgEALNGLSTIRAYKAYDRMAEINGRSMDNNIRFTLvnmSSN 1136
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1006 HIFGITFSFTQAMMYFsYAGCFRFGAYLVAHKLMSFED---VLLVFSAVVFGAM-AVGQVSSFAPDYAKAKISAAHIIMI 1081
Cdd:PLN03130  1137 RWLAIRLETLGGLMIW-LTASFAVMQNGRAENQAAFAStmgLLLSYALNITSLLtAVLRLASLAENSLNAVERVGTYIDL 1215
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1082 IEKTPL-IDSYSTEGLMPNTleGNVTFGEVVFNYptRPDIP-VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDP 1159
Cdd:PLN03130  1216 PSEAPLvIENNRPPPGWPSS--GSIKFEDVVLRY--RPELPpVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVEL 1291
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1160 LAGKVLLDGKEIKRLNVQWLRAHLGIVSQEPILFDCSIAENIaygDNSRVVSQEEIVRAAKEANIHAFIESLPNKYSTKV 1239
Cdd:PLN03130  1292 ERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNL---DPFNEHNDADLWESLERAHLKDVIRRNSLGLDAEV 1368
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1240 GDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKarEGRTC--IVIAHRLSTIQNADLIVVFQ 1317
Cdd:PLN03130  1369 SEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIRE--EFKSCtmLIIAHRLNTIIDCDRILVLD 1446
                          890       900
                   ....*....|....*....|....*
gi 1149123047 1318 NGRVKEHGTHQQLLAQKGIYFS-MV 1341
Cdd:PLN03130  1447 AGRVVEFDTPENLLSNEGSAFSkMV 1471
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
431-695 1.34e-55

cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 204.29  E-value: 1.34e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  431 AAYEIFKIIDNKPSIDSYSKSGHKPDniKGNLEFRNVHFSYPSRkEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLM 510
Cdd:PRK11160   310 SARRINEITEQKPEVTFPTTSTAAAD--QVSLTLNNVSFTYPDQ-PQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLL 386
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  511 QRLYDPTEGMVSVDGQDIRTINVRFLREIIGVVSQEPVLFATTIAENIRYGRENVTmDEIEKAVKEANAYDFIMKLPHKF 590
Cdd:PRK11160   387 TRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNAS-DEALIEVLQQVGLEKLLEDDKGL 465
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  591 DTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAG 670
Cdd:PRK11160   466 NAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICV 545
                          250       260
                   ....*....|....*....|....*
gi 1149123047  671 FDDGVIVEKGNHDELMKEKGIYFKL 695
Cdd:PRK11160   546 MDNGQIIEQGTHQELLAQQGRYYQL 570
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
785-1343 2.07e-55

ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]


Pssm-ID: 130261 [Multi-domain]  Cd Length: 708  Bit Score: 206.51  E-value: 2.07e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  785 VFCAIINGGLQPAFAIIFSKIIGVFTriddPETKRQNSNLFSLLFLALGIISFITFFLQGFTFGKAGEILTKRLRYMVFR 864
Cdd:TIGR01193  162 VIAAIIVTLISIAGSYYLQKIIDTYI----PHKMMGTLGIISIGLIIAYIIQQILSYIQIFLLNVLGQRLSIDIILSYIK 237
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  865 SMLRQDVSWFDDPKntTGALTTRLAnDAAQVKGAIGSrlaVITQNIANLGTGIIISFIYGWQ---LTLLLLAIVPIIAIA 941
Cdd:TIGR01193  238 HLFELPMSFFSTRR--TGEIVSRFT-DASSIIDALAS---TILSLFLDMWILVIVGLFLVRQnmlLFLLSLLSIPVYAVI 311
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  942 GVVEMKMLSGQalkDKKELEGSGKIATEAIENF---RTVVSLTQE----QKFEHMYAQSLQVPYRNS----LRKAHIFGI 1010
Cdd:TIGR01193  312 IILFKRTFNKL---NHDAMQANAVLNSSIIEDLngiETIKSLTSEaerySKIDSEFGDYLNKSFKYQkadqGQQAIKAVT 388
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1011 TFSFTQAMMYFsyagcfrfGAYLVAHKLMSFEDvLLVFSAVV-FGAMAVGQVSSFAPDYAKAKISAAHIimiiEKTPLID 1089
Cdd:TIGR01193  389 KLILNVVILWT--------GAYLVMRGKLTLGQ-LITFNALLsYFLTPLENIINLQPKLQAARVANNRL----NEVYLVD 455
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1090 SYSTEGLMP---NTLEGNVTFGEVVFNYPTRPdiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLL 1166
Cdd:TIGR01193  456 SEFINKKKRtelNNLNGDIVINDVSYSYGYGS--NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILL 533
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1167 DGKEIKRLNVQWLRAHLGIVSQEPILFDCSIAENIAYGdNSRVVSQEEIVRAAKEANIHAFIESLPNKYSTKVGDKGTQL 1246
Cdd:TIGR01193  534 NGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLG-AKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSI 612
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1247 SGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREgRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGT 1326
Cdd:TIGR01193  613 SGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQD-KTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGS 691
                          570
                   ....*....|....*..
gi 1149123047 1327 HQQLLAQKGIYFSMVSV 1343
Cdd:TIGR01193  692 HDELLDRNGFYASLIHN 708
type_I_sec_PrtD TIGR01842
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ...
387-688 1.27e-53

type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 200134 [Multi-domain]  Cd Length: 544  Bit Score: 197.57  E-value: 1.27e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  387 GTTLVLSGEYSIGqvltvffSVLIGAFSVGQASPSIE-------AFANARGAAYEIFKIIDNKPSIDSYSKSghkPdNIK 459
Cdd:TIGR01842  246 GAYLAIDGEITPG-------MMIAGSILVGRALAPIDgaiggwkQFSGARQAYKRLNELLANYPSRDPAMPL---P-EPE 314
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  460 GNLEFRNVHFSYPSRKEVkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREI 539
Cdd:TIGR01842  315 GHLSVENVTIVPPGGKKP-TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKH 393
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  540 IGVVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNP 619
Cdd:TIGR01842  394 IGYLPQDVELFPGTVAENIARFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDP 473
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  620 KILLLDEATSALDTESEAVVQVALDKARK-GRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELMKE 688
Cdd:TIGR01842  474 KLVVLDEPNSNLDEEGEQALANAIKALKArGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
424-692 1.44e-52

cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 195.45  E-value: 1.44e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  424 AFANARGAAYEIFKIIDnkpSIDSYSKSGHKPDNIKGNLEFRNVHFSYPSRKEVKILKGLNLKVQSGQTVALVGNSGCGK 503
Cdd:PRK11174   313 AKAQAVGAAESLVTFLE---TPLAHPQQGEKELASNDPVTIEAEDLEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGK 389
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  504 STtvqLMQRL--YDPTEGMVSVDGQDIRTINVRFLREIIGVVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYD 581
Cdd:PRK11174   390 TS---LLNALlgFLPYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSE 466
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  582 FIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLST 661
Cdd:PRK11174   467 FLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLED 546
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1149123047  662 VRNADVIAGFDDGVIVEKGNHDELMKEKGIY 692
Cdd:PRK11174   547 LAQWDQIWVMQDGQIVQQGDYAELSQAGGLF 577
type_I_sec_PrtD TIGR01842
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ...
1102-1333 1.54e-52

type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 200134 [Multi-domain]  Cd Length: 544  Bit Score: 194.49  E-value: 1.54e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1102 EGNVTFGEVVFnYPTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRA 1181
Cdd:TIGR01842  314 EGHLSVENVTI-VPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGK 392
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1182 HLGIVSQEPILFDCSIAENIA-YGDNsrvVSQEEIVRAAKEANIHAFIESLPNKYSTKVGDKGTQLSGGQKQRIAIARAL 1260
Cdd:TIGR01842  393 HIGYLPQDVELFPGTVAENIArFGEN---ADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARAL 469
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1149123047 1261 VRQPHILLLDEATSALDTESEKVVQEALDKAR-EGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQ 1333
Cdd:TIGR01842  470 YGDPKLVVLDEPNSNLDEEGEQALANAIKALKaRGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
462-689 2.87e-52

Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];


Pssm-ID: 440739 [Multi-domain]  Cd Length: 230  Bit Score: 183.30  E-value: 2.87e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPsrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIG 541
Cdd:COG1122      1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  542 VVSQEPV--LFATTIAENIRYGREN--VTMDEIEKAVKEA----NAYDFIMKLPHkfdtlvgergaQLSGGQKQRIAIAR 613
Cdd:COG1122     79 LVFQNPDdqLFAPTVEEDVAFGPENlgLPREEIRERVEEAlelvGLEHLADRPPH-----------ELSGGQKQRVAIAG 147
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1149123047  614 ALVRNPKILLLDEATSALDTESEAVVQVALDK-ARKGRTTIVIAHRLSTV-RNADVIAGFDDGVIVEKGNHDELMKEK 689
Cdd:COG1122    148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREVFSDY 225
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
1069-1340 5.51e-52

cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 193.91  E-value: 5.51e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1069 AKAK-ISAAHIIMIIEKTPLIDSYSTEGLM----PNTLEGNvtfGEVVFNyptrPDIPVLQG-LSLEVKKGQTLALVGSS 1142
Cdd:PRK11174   313 AKAQaVGAAESLVTFLETPLAHPQQGEKELasndPVTIEAE---DLEILS----PDGKTLAGpLNFTLPAGQRIALVGPS 385
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1143 GCGKSTVVQLLERFYdPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEPILFDCSIAENIAYGDNSrvVSQEEIVRAAKEA 1222
Cdd:PRK11174   386 GAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPD--ASDEQLQQALENA 462
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1223 NIHAFIESLPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAH 1302
Cdd:PRK11174   463 WVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTH 542
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1149123047 1303 RLSTIQNADLIVVFQNGRVKEHGTHQQLLAQKGIYFSM 1340
Cdd:PRK11174   543 QLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATL 580
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
462-686 2.15e-51

ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440740 [Multi-domain]  Cd Length: 514  Bit Score: 190.11  E-value: 2.15e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSRK--EVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREI 539
Cdd:COG1123    261 LEVRNLSKRYPVRGkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLREL 340
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  540 ---IGVVSQEPV--LFAT-TIAENIRYGREN---VTMDEIEKAVKEANA-----YDFIMKLPHkfdtlvgergaQLSGGQ 605
Cdd:COG1123    341 rrrVQMVFQDPYssLNPRmTVGDIIAEPLRLhglLSRAERRERVAELLErvglpPDLADRYPH-----------ELSGGQ 409
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  606 KQRIAIARALVRNPKILLLDEATSALDTESEAVVqvaLD-----KARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEK 679
Cdd:COG1123    410 RQRVAIARALALEPKLLILDEPTSALDVSVQAQI---LNllrdlQRELGLTYLFISHDLAVVRYiADRVAVMYDGRIVED 486

                   ....*..
gi 1149123047  680 GNHDELM 686
Cdd:COG1123    487 GPTEEVF 493
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
463-674 1.90e-50

First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.


Pssm-ID: 213192 [Multi-domain]  Cd Length: 211  Bit Score: 177.66  E-value: 1.90e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  463 EFRNVHFSYPSRKEvKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIGV 542
Cdd:cd03225      1 ELKNLSFSYPDGAR-PALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  543 VSQEP--VLFATTIAENIRYGREN--VTMDEIEKAVKEANAydfIMKLPHKFDTLVgergAQLSGGQKQRIAIARALVRN 618
Cdd:cd03225     80 VFQNPddQFFGPTVEEEVAFGLENlgLPEEEIEERVEEALE---LVGLEGLRDRSP----FTLSGGQKQRVAIAGVLAMD 152
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1149123047  619 PKILLLDEATSALDTESEAVVQVALDK-ARKGRTTIVIAHRLSTVRN-ADVIAGFDDG 674
Cdd:cd03225    153 PDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLElADRVIVLEDG 210
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
462-685 7.36e-50

ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).


Pssm-ID: 213227 [Multi-domain]  Cd Length: 227  Bit Score: 176.60  E-value: 7.36e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYpsrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYD-----PTEGMVSVDGQDIRTINVRF- 535
Cdd:cd03260      1 IELRDLNVYY---GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDVl 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  536 -LREIIGVVSQEPVLFATTIAENIRYG------RENVTMDEI-EKAVKEANAYDFIMKLPHkfdtlvgerGAQLSGGQKQ 607
Cdd:cd03260     78 eLRRRVGMVFQKPNPFPGSIYDNVAYGlrlhgiKLKEELDERvEEALRKAALWDEVKDRLH---------ALGLSGGQQQ 148
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1149123047  608 RIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTV-RNADVIAGFDDGVIVEKGNHDEL 685
Cdd:cd03260    149 RLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAaRVADRTAFLLNGRLVEFGPTEQI 227
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
462-676 3.90e-49

ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.


Pssm-ID: 213213 [Multi-domain]  Cd Length: 173  Bit Score: 172.40  E-value: 3.90e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSRKEVkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIG 541
Cdd:cd03246      1 LEVENVSFRYPGAEPP-VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVG 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  542 VVSQEPVLFATTIAENIrygrenvtmdeiekavkeanaydfimklphkfdtlvgergaqLSGGQKQRIAIARALVRNPKI 621
Cdd:cd03246     80 YLPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRI 117
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1149123047  622 LLLDEATSALDTESEAVVQVALDKARK-GRTTIVIAHRLSTVRNADVIAGFDDGVI 676
Cdd:cd03246    118 LVLDEPNSHLDVEGERALNQAIAALKAaGATRIVIAHRPETLASADRILVLEDGRV 173
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
1110-1321 1.10e-47

ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.


Pssm-ID: 213213 [Multi-domain]  Cd Length: 173  Bit Score: 168.16  E-value: 1.10e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1110 VVFNYP-TRPdiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQ 1188
Cdd:cd03246      6 VSFRYPgAEP--PVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQ 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1189 EPILFDCSIAENIaygdnsrvvsqeeivraakeanihafieslpnkystkvgdkgtqLSGGQKQRIAIARALVRQPHILL 1268
Cdd:cd03246     84 DDELFSGSIAENI--------------------------------------------LSGGQRQRLGLARALYGNPRILV 119
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1149123047 1269 LDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIVVFQNGRV 1321
Cdd:cd03246    120 LDEPNSHLDVEGERALNQAIAALKAaGATRIVIAHRPETLASADRILVLEDGRV 173
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
1110-1334 1.47e-47

Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];


Pssm-ID: 440739 [Multi-domain]  Cd Length: 230  Bit Score: 169.82  E-value: 1.47e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1110 VVFNYPtrPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQE 1189
Cdd:COG1122      6 LSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLVFQN 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1190 PI--LFDCSIAENIAYGDNSRVVSQEEIVRAAKEA----NIHAFIESLPNkystkvgdkgtQLSGGQKQRIAIARALVRQ 1263
Cdd:COG1122     84 PDdqLFAPTVEEDVAFGPENLGLPREEIRERVEEAlelvGLEHLADRPPH-----------ELSGGQKQRVAIAGVLAME 152
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1149123047 1264 PHILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTI-QNADLIVVFQNGRVKEHGTHQQLLAQK 1334
Cdd:COG1122    153 PEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREVFSDY 225
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
1119-1330 3.18e-47

ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).


Pssm-ID: 213227 [Multi-domain]  Cd Length: 227  Bit Score: 168.90  E-value: 3.18e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1119 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD-----PLAGKVLLDGKEI--KRLNVQWLRAHLGIVSQEPI 1191
Cdd:cd03260     12 DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIydLDVDVLELRRRVGMVFQKPN 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1192 LFDCSIAENIAYGDNSRVVSQ----EEIVRAA-KEANIHAfieslpnkystKVGDK--GTQLSGGQKQRIAIARALVRQP 1264
Cdd:cd03260     92 PFPGSIYDNVAYGLRLHGIKLkeelDERVEEAlRKAALWD-----------EVKDRlhALGLSGGQQQRLCLARALANEP 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1149123047 1265 HILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQL 1330
Cdd:cd03260    161 EVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
ABC_6TM_TAP_ABCB8_10_like cd18557
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ...
179-435 4.14e-47

Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.


Pssm-ID: 350001 [Multi-domain]  Cd Length: 289  Bit Score: 170.82  E-value: 4.14e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  179 EDMTRYAYYYSGIGAGVLVAAYIQVSFWCLAAGRQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGD 258
Cdd:cd18557     33 DVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTD 112
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  259 KIGMFFQSMATFFTGFIVGFTRGWKLTLVILAISPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFG 338
Cdd:cd18557    113 NLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFS 192
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  339 GQKKELERYNKNLEEAKRIGIKKAITANISIGAAFLLIYASYALAFWYGTTLVLSGEYSIGQVLT-VFFSVLIgAFSVGQ 417
Cdd:cd18557    193 AEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWYGGYLVLSGQLTVGELTSfILYTIMV-ASSVGG 271
                          250
                   ....*....|....*...
gi 1149123047  418 ASPSIEAFANARGAAYEI 435
Cdd:cd18557    272 LSSLLADIMKALGASERV 289
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
462-657 9.40e-47

ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 166.92  E-value: 9.40e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIG 541
Cdd:COG4619      1 LELEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVA 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  542 VVSQEPVLFATTIAENI----RYGRENVTMDEIEKAVKEANaydfimkLPHKF-DTLVGErgaqLSGGQKQRIAIARALV 616
Cdd:COG4619     78 YVPQEPALWGGTVRDNLpfpfQLRERKFDRERALELLERLG-------LPPDIlDKPVER----LSGGERQRLALIRALL 146
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1149123047  617 RNPKILLLDEATSALDTESEAVVQVALDK--ARKGRTTIVIAH 657
Cdd:COG4619    147 LQPDVLLLDEPTSALDPENTRRVEELLREylAEEGRAVLWVSH 189
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
480-629 1.19e-46

ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.


Pssm-ID: 394964 [Multi-domain]  Cd Length: 150  Bit Score: 164.36  E-value: 1.19e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  480 LKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIGVVSQEPVLF-ATTIAENI 558
Cdd:pfam00005    1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENL 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1149123047  559 RYGREnvtMDEIEKAVKEANAYDFI--MKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATS 629
Cdd:pfam00005   81 RLGLL---LKGLSKREKDARAEEALekLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
462-685 1.24e-46

ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213225 [Multi-domain]  Cd Length: 233  Bit Score: 167.37  E-value: 1.24e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSR-KEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREI- 539
Cdd:cd03258      2 IELKNVSKVFGDTgGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKAr 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  540 --IGVVSQEPVLFAT-TIAENIRYGRE--NVTMDEIEKAVKEANAydfIMKLPHKFDTlvgeRGAQLSGGQKQRIAIARA 614
Cdd:cd03258     82 rrIGMIFQHFNLLSSrTVFENVALPLEiaGVPKAEIEERVLELLE---LVGLEDKADA----YPAQLSGGQKQRVGIARA 154
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1149123047  615 LVRNPKILLLDEATSALDTES-EAVVQVALDKARKGRTTIV-IAHRLSTVRN-ADVIAGFDDGVIVEKGNHDEL 685
Cdd:cd03258    155 LANNPKVLLCDEATSALDPETtQSILALLRDINRELGLTIVlITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEV 228
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
1110-1333 4.26e-46

ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440740 [Multi-domain]  Cd Length: 514  Bit Score: 174.32  E-value: 4.26e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1110 VVFNYPTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLN---VQWLRAHLGIV 1186
Cdd:COG1123    268 KRYPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLRELRRRVQMV 347
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1187 SQEPIL-FDC--SIAENIAYG-DNSRVVSQEEIVRAAKEAnIHA------FIESLPNkystkvgdkgtQLSGGQKQRIAI 1256
Cdd:COG1123    348 FQDPYSsLNPrmTVGDIIAEPlRLHGLLSRAERRERVAEL-LERvglppdLADRYPH-----------ELSGGQRQRVAI 415
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1257 ARALVRQPHILLLDEATSALDTESEKVVQEALD--KAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLLAQ 1333
Cdd:COG1123    416 ARALALEPKLLILDEPTSALDVSVQAQILNLLRdlQRELGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTEEVFAN 495
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
462-680 4.28e-46

ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.


Pssm-ID: 213224 [Multi-domain]  Cd Length: 228  Bit Score: 165.76  E-value: 4.28e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSRK-EVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREI- 539
Cdd:cd03257      2 LEVKNLSVSFPTGGgSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIRr 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  540 --IGVVSQEPVL-------FATTIAENIRYGRENVTMDEIEKAVKEA-----NAYDFIMKLPHkfdtlvgergaQLSGGQ 605
Cdd:cd03257     82 keIQMVFQDPMSslnprmtIGEQIAEPLRIHGKLSKKEARKEAVLLLlvgvgLPEEVLNRYPH-----------ELSGGQ 150
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1149123047  606 KQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARK--GRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKG 680
Cdd:cd03257    151 RQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
462-681 8.46e-46

ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 168.72  E-value: 8.46e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSRK-EVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREI- 539
Cdd:COG1135      2 IELENLSKTFPTKGgPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAAr 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  540 --IGVVSQEPVLFAT-TIAENIRYGRE--NVTMDEIEKAVKE----------ANAYdfimklPhkfdtlvgergAQLSGG 604
Cdd:COG1135     82 rkIGMIFQHFNLLSSrTVAENVALPLEiaGVPKAEIRKRVAEllelvglsdkADAY------P-----------SQLSGG 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  605 QKQRIAIARALVRNPKILLLDEATSALDTES-EAVVQVaLDKARK--GRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKG 680
Cdd:COG1135    145 QKQRVGIARALANNPKVLLCDEATSALDPETtRSILDL-LKDINRelGLTIVLITHEMDVVRRiCDRVAVLENGRIVEQG 223

                   .
gi 1149123047  681 N 681
Cdd:COG1135    224 P 224
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
1110-1320 3.66e-45

First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.


Pssm-ID: 213192 [Multi-domain]  Cd Length: 211  Bit Score: 162.25  E-value: 3.66e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1110 VVFNYPTRpDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQE 1189
Cdd:cd03225      5 LSFSYPDG-ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVFQN 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1190 P--ILFDCSIAENIAYGDNSRVVSQEEIVRAAKEA----NIHAFIESLPNkystkvgdkgtQLSGGQKQRIAIARALVRQ 1263
Cdd:cd03225     84 PddQFFGPTVEEEVAFGLENLGLPEEEIEERVEEAlelvGLEGLRDRSPF-----------TLSGGQKQRVAIAGVLAMD 152
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1149123047 1264 PHILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVFQNGR 1320
Cdd:cd03225    153 PDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
ECF_ATPase_1 TIGR04520
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
462-691 5.49e-45

energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]


Pssm-ID: 275313 [Multi-domain]  Cd Length: 268  Bit Score: 163.76  E-value: 5.49e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSRkEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTI-NVRFLREII 540
Cdd:TIGR04520    1 IEVENVSFSYPES-EKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEeNLWEIRKKV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  541 GVVSQEP--VLFATTIAENIRYGREN--VTMDEIEKAVKEA----NAYDFIMKLPHKfdtlvgergaqLSGGQKQRIAIA 612
Cdd:TIGR04520   80 GMVFQNPdnQFVGATVEDDVAFGLENlgVPREEMRKRVDEAlklvGMEDFRDREPHL-----------LSGGQKQRVAIA 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  613 RALVRNPKILLLDEATSALDTES-EAVVQVALD-KARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKG------NHDE 684
Cdd:TIGR04520  149 GVLAMRPDIIILDEATSMLDPKGrKEVLETIRKlNKEEGITVISITHDMEEAVLADRVIVMNKGKIVAEGtpreifSQVE 228

                   ....*..
gi 1149123047  685 LMKEKGI 691
Cdd:TIGR04520  229 LLKEIGL 235
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
462-678 1.14e-44

ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 161.36  E-value: 1.14e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSRK-EVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTIN----VRFL 536
Cdd:COG1136      5 LELRNLTKSYGTGEgEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSerelARLR 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  537 REIIGVVSQEPVLFAT-TIAENIRYGRE--NVTMDEIEKAVKEANAYdfiMKLPHKFDTLVgergAQLSGGQKQRIAIAR 613
Cdd:COG1136     85 RRHIGFVFQFFNLLPElTALENVALPLLlaGVSRKERRERARELLER---VGLGDRLDHRP----SQLSGGQQQRVAIAR 157
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1149123047  614 ALVRNPKILLLDEATSALDTE-SEAVVQVALDKARKGRTTIVIA-HRLSTVRNADVIAGFDDGVIVE 678
Cdd:COG1136    158 ALVNRPKLILADEPTGNLDSKtGEEVLELLRELNRELGTTIVMVtHDPELAARADRVIRLRDGRIVS 224
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
1121-1321 1.31e-44

ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 160.75  E-value: 1.31e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1121 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEPILFDCSIAEN 1200
Cdd:COG4619     14 PILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVPQEPALWGGTVRDN 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1201 IA--YGDNSRVVSQEEIVRAAKEANihafiesLPNKYSTKvgdKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDT 1278
Cdd:COG4619     94 LPfpFQLRERKFDRERALELLERLG-------LPPDILDK---PVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDP 163
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1149123047 1279 ESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVFQNGRV 1321
Cdd:COG4619    164 ENTRRVEELLREylAEEGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
462-687 1.63e-44

ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440744 [Multi-domain]  Cd Length: 241  Bit Score: 161.69  E-value: 1.63e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREI-- 539
Cdd:COG1127      6 IEVRNLTKSFGDRV---VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELrr 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  540 -IGVVSQEPVLF-ATTIAENIRYG-RENVTM--DEIEKAVkeanaydfIMKLphkfdTLVGERGA------QLSGGQKQR 608
Cdd:COG1127     83 rIGMLFQGGALFdSLTVFENVAFPlREHTDLseAEIRELV--------LEKL-----ELVGLPGAadkmpsELSGGMRKR 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  609 IAIARALVRNPKILLLDEATSALD--TeSEAVVQVALD-KARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKGNHDE 684
Cdd:COG1127    150 VALARALALDPEILLYDEPTAGLDpiT-SAVIDELIRElRDELGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEE 228

                   ...
gi 1149123047  685 LMK 687
Cdd:COG1127    229 LLA 231
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
462-676 1.88e-44

ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.


Pssm-ID: 213222 [Multi-domain]  Cd Length: 218  Bit Score: 160.73  E-value: 1.88e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSRKE-VKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTIN----VRFL 536
Cdd:cd03255      1 IELKNLSKTYGGGGEkVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSekelAAFR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  537 REIIGVVSQEPVLFAT-TIAENIRYGrenVTMDEIEKAVKEANAYDFI--MKLPHKFDTLVgergAQLSGGQKQRIAIAR 613
Cdd:cd03255     81 RRHIGFVFQSFNLLPDlTALENVELP---LLLAGVPKKERRERAEELLerVGLGDRLNHYP----SELSGGQQQRVAIAR 153
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1149123047  614 ALVRNPKILLLDEATSALDTE-SEAVVQVALDKARKGRTTIVIA-HRLSTVRNADVIAGFDDGVI 676
Cdd:cd03255    154 ALANDPKIILADEPTGNLDSEtGKEVMELLRELNKEAGTTIVVVtHDPELAEYADRIIELRDGKI 218
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
1044-1304 1.97e-44

thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.


Pssm-ID: 274331 [Multi-domain]  Cd Length: 530  Bit Score: 169.85  E-value: 1.97e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1044 VLLVFSAvvFGAMAVgqVSSFAPDYAKAKISAAHIIMIIEKTPLIDSYSTEGLMPNTLEG-NVTFGEVVFNYPTRPdiPV 1122
Cdd:TIGR02868  277 VLLPLAA--FEAFAA--LPAAAQQLTRVRAAAERIVEVLDAAGPVAEGSAPAAGAVGLGKpTLELRDLSAGYPGAP--PV 350
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1123 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEPILFDCSIAEN-- 1200
Cdd:TIGR02868  351 LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENlr 430
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1201 IAYGDnsrvVSQEEIVRAAKEANIHAFIESLPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTES 1280
Cdd:TIGR02868  431 LARPD----ATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAET 506
                          250       260
                   ....*....|....*....|....
gi 1149123047 1281 EKVVQEALDKAREGRTCIVIAHRL 1304
Cdd:TIGR02868  507 ADELLEDLLAALSGRTVVLITHHL 530
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
462-685 2.74e-44

ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 160.93  E-value: 2.74e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYpsrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDI--RTINVRFLREI 539
Cdd:COG1126      2 IEIENLHKSF---GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKLRRK 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  540 IGVVSQEPVLFA-TTIAENIRYGRENVT-MDEiEKAVKEANAYDFIMKLPHKFDtlvgERGAQLSGGQKQRIAIARALVR 617
Cdd:COG1126     79 VGMVFQQFNLFPhLTVLENVTLAPIKVKkMSK-AEAEERAMELLERVGLADKAD----AYPAQLSGGQQQRVAIARALAM 153
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1149123047  618 NPKILLLDEATSALDTE--SEaVVQVALDKARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKGNHDEL 685
Cdd:COG1126    154 EPKVMLFDEPTSALDPElvGE-VLDVMRDLAKEGMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGPPEEF 223
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
462-687 3.75e-44

ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213228 [Multi-domain]  Cd Length: 235  Bit Score: 160.36  E-value: 3.75e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREI-- 539
Cdd:cd03261      1 IELRGLTKSFGGRT---VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLrr 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  540 -IGVVSQEPVLF-ATTIAENIRYG-RENVTMDE--IEKAVKeanaydfiMKLphkfdTLVGERG------AQLSGGQKQR 608
Cdd:cd03261     78 rMGMLFQSGALFdSLTVFENVAFPlREHTRLSEeeIREIVL--------EKL-----EAVGLRGaedlypAELSGGMKKR 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  609 IAIARALVRNPKILLLDEATSALD-TESEAVVQVALD-KARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKGNHDEL 685
Cdd:cd03261    145 VALARALALDPELLLYDEPTAGLDpIASGVIDDLIRSlKKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEEL 224

                   ..
gi 1149123047  686 MK 687
Cdd:cd03261    225 RA 226
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
1106-1326 4.00e-44

ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.


Pssm-ID: 213269 [Multi-domain]  Cd Length: 207  Bit Score: 159.11  E-value: 4.00e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1106 TFGEV-VFNYPTR--PDIP-VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRA 1181
Cdd:cd03369      3 EHGEIeVENLSVRyaPDLPpVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1182 HLGIVSQEPILFDCSIAENIaygDNSRVVSQEEIVRAakeanihafieslpnkysTKVGDKGTQLSGGQKQRIAIARALV 1261
Cdd:cd03369     83 SLTIIPQDPTLFSGTIRSNL---DPFDEYSDEEIYGA------------------LRVSEGGLNLSQGQRQLLCLARALL 141
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1149123047 1262 RQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGT 1326
Cdd:cd03369    142 KRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
462-686 5.47e-44

ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440740 [Multi-domain]  Cd Length: 514  Bit Score: 168.16  E-value: 5.47e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSRkEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPT---EGMVSVDGQDIRTINVRFLRE 538
Cdd:COG1123      5 LEVRDLSVRYPGG-DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGR 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  539 IIGVVSQEP--VLFATTIAENIRYGREN--VTMDEIEKAVKEANAydfIMKLPHKFDtlvgERGAQLSGGQKQRIAIARA 614
Cdd:COG1123     84 RIGMVFQDPmtQLNPVTVGDQIAEALENlgLSRAEARARVLELLE---AVGLERRLD----RYPHQLSGGQRQRVAIAMA 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1149123047  615 LVRNPKILLLDEATSALDTESEAVVQVALDKARK--GRTTIVIAHRLSTV-RNADVIAGFDDGVIVEKGNHDELM 686
Cdd:COG1123    157 LALDPDLLIADEPTTALDVTTQAEILDLLRELQRerGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEIL 231
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
462-688 6.33e-44

ABC-type multidrug transport system, ATPase component [Defense mechanisms];


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 159.84  E-value: 6.33e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYpsrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRfLREIIG 541
Cdd:COG1131      1 IEVRGLTKRY---GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAE-VRRRIG 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  542 VVSQEPVLFAT-TIAENIRYGRE--NVTMDEIEKAVKEANAydfIMKLPHKFDTLVGergaQLSGGQKQRIAIARALVRN 618
Cdd:COG1131     77 YVPQEPALYPDlTVRENLRFFARlyGLPRKEARERIDELLE---LFGLTDAADRKVG----TLSGGMKQRLGLALALLHD 149
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1149123047  619 PKILLLDEATSALDTES-EAVVQVALDKARKGRTTIVIAHRLSTV-RNADVIAGFDDGVIVEKGNHDELMKE 688
Cdd:COG1131    150 PELLILDEPTSGLDPEArRELWELLRELAAEGKTVLLSTHYLEEAeRLCDRVAIIDKGRIVADGTPDELKAR 221
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
460-680 1.16e-43

ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.


Pssm-ID: 213269 [Multi-domain]  Cd Length: 207  Bit Score: 157.96  E-value: 1.16e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  460 GNLEFRNVHFSYPSRKEvKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREI 539
Cdd:cd03369      5 GEIEVENLSVRYAPDLP-PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSS 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  540 IGVVSQEPVLFATTIAENI-RYGREnvTMDEIEKAVKeanaydfimklphkfdtlVGERGAQLSGGQKQRIAIARALVRN 618
Cdd:cd03369     84 LTIIPQDPTLFSGTIRSNLdPFDEY--SDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLKR 143
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1149123047  619 PKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKG 680
Cdd:cd03369    144 PRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYD 205
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
1105-1325 1.27e-43

ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.


Pssm-ID: 213214 [Multi-domain]  Cd Length: 178  Bit Score: 156.70  E-value: 1.27e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1105 VTFGEVVFNYPTRpDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQwLRAHLG 1184
Cdd:cd03247      1 LSINNVSFSYPEQ-EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-LSSLIS 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1185 IVSQEPILFDCSIAENIaygdnsrvvsqeeivraakeanihafieslpnkystkvgdkGTQLSGGQKQRIAIARALVRQP 1264
Cdd:cd03247     79 VLNQRPYLFDTTLRNNL-----------------------------------------GRRFSGGERQRLALARILLQDA 117
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1149123047 1265 HILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHG 1325
Cdd:cd03247    118 PIVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
462-680 3.19e-43

ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.


Pssm-ID: 213214 [Multi-domain]  Cd Length: 178  Bit Score: 155.55  E-value: 3.19e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINvRFLREIIG 541
Cdd:cd03247      1 LSINNVSFSYPE-QEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLIS 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  542 VVSQEPVLFATTIAENIrygrenvtmdeiekavkeanaydfimklphkfdtlvgerGAQLSGGQKQRIAIARALVRNPKI 621
Cdd:cd03247     79 VLNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPI 119
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1149123047  622 LLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKG 680
Cdd:cd03247    120 VLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
462-657 3.76e-43

ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213260 [Multi-domain]  Cd Length: 220  Bit Score: 156.86  E-value: 3.76e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSRK-EVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRflreiI 540
Cdd:cd03293      1 LEVRNVSKTYGGGGgAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD-----R 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  541 GVVSQEPVLFA-TTIAENIRYGRE--NVTMDEIEKAVKEANA----YDFIMKLPHkfdtlvgergaQLSGGQKQRIAIAR 613
Cdd:cd03293     76 GYVFQQDALLPwLTVLDNVALGLElqGVPKAEARERAEELLElvglSGFENAYPH-----------QLSGGMRQRVALAR 144
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1149123047  614 ALVRNPKILLLDEATSALDTESEAVVQVALDK--ARKGRTTIVIAH 657
Cdd:cd03293    145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDiwRETGKTVLLVTH 190
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
1116-1325 4.55e-43

ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213226 [Multi-domain]  Cd Length: 213  Bit Score: 156.53  E-value: 4.55e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1116 TRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQwlRAHLGIVSQEPILFD- 1194
Cdd:cd03259      9 TYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMVFQDYALFPh 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1195 CSIAENIAYGDNSRVVSQEEIVRAAKEANIHAFIESLPNKYSTkvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEATS 1274
Cdd:cd03259     87 LTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPH-------ELSGGQQQRVALARALAREPSLLLLDEPLS 159
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1149123047 1275 ALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVFQNGRVKEHG 1325
Cdd:cd03259    160 ALDAKLREELREELKElqRELGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
ABC_6TM_AtABCB27_like cd18780
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ...
124-418 6.66e-43

Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.


Pssm-ID: 350053 [Multi-domain]  Cd Length: 295  Bit Score: 158.95  E-value: 6.66e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  124 GTLAAIIHGAGLPLMMLVFGEMTDIfanagnledlmsnITNRSDINDTGffmnLEEDMTRYAYYYSGIGAGVLVAAYIQV 203
Cdd:cd18780      1 GTIALLVSSGTNLALPYFFGQVIDA-------------VTNHSGSGGEE----ALRALNQAVLILLGVVLIGSIATFLRS 63
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  204 SFWCLAAGRQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQSMATFFTGFIVGFTRGWK 283
Cdd:cd18780     64 WLFTLAGERVVARLRKRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWK 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  284 LTLVILAISPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKRIGIKKAI 363
Cdd:cd18780    144 LTLVMLSVVPPLSIGAVIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLAR 223
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1149123047  364 TANISIGAAFLLIYASYALAFWYGTTLVLSGEYSIGQvLTVFfsvLIGAFSVGQA 418
Cdd:cd18780    224 ASGGFNGFMGAAAQLAIVLVLWYGGRLVIDGELTTGL-LTSF---LLYTLTVAMS 274
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
462-657 7.38e-43

ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 157.56  E-value: 7.38e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSRK-EVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRflreiI 540
Cdd:COG1116      8 LELRGVSKRFPTGGgGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD-----R 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  541 GVVSQEPVLFA-TTIAENIRYGRENVTMDEiEKAVKEANAY-------DFIMKLPHkfdtlvgergaQLSGGQKQRIAIA 612
Cdd:COG1116     83 GVVFQEPALLPwLTVLDNVALGLELRGVPK-AERRERARELlelvglaGFEDAYPH-----------QLSGGMRQRVAIA 150
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1149123047  613 RALVRNPKILLLDEATSALDTESEAVVQVALDK--ARKGRTTIVIAH 657
Cdd:COG1116    151 RALANDPEVLLMDEPFGALDALTRERLQDELLRlwQETGKTVLFVTH 197
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
462-687 8.97e-43

ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];


Pssm-ID: 440741 [Multi-domain]  Cd Length: 248  Bit Score: 156.89  E-value: 8.97e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSR-KEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREII 540
Cdd:COG1124      2 LEVRNLSVSYGQGgRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  541 GVVSQEP---------VlfATTIAENIRYGRENVTMDEIEKAVKEAN-AYDFIMKLPHkfdtlvgergaQLSGGQKQRIA 610
Cdd:COG1124     82 QMVFQDPyaslhprhtV--DRILAEPLRIHGLPDREERIAELLEQVGlPPSFLDRYPH-----------QLSGGQRQRVA 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  611 IARALVRNPKILLLDEATSALDteseAVVQVA-LD-----KARKGRTTIVIAHRLSTV-RNADVIAGFDDGVIVEKGNHD 683
Cdd:COG1124    149 IARALILEPELLLLDEPTSALD----VSVQAEiLNllkdlREERGLTYLFVSHDLAVVaHLCDRVAVMQNGRIVEELTVA 224

                   ....
gi 1149123047  684 ELMK 687
Cdd:COG1124    225 DLLA 228
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
462-680 3.20e-42

ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213226 [Multi-domain]  Cd Length: 213  Bit Score: 153.83  E-value: 3.20e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYpsrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRflREIIG 541
Cdd:cd03259      1 LELKGLSKTY---GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIG 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  542 VVSQEPVLFAT-TIAENIRYGRENVTM--DEIEKAVKEANAydfIMKLPHkfdtLVGERGAQLSGGQKQRIAIARALVRN 618
Cdd:cd03259     76 MVFQDYALFPHlTVAENIAFGLKLRGVpkAEIRARVRELLE---LVGLEG----LLNRYPHELSGGQQQRVALARALARE 148
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1149123047  619 PKILLLDEATSALDTESEAVVQVALDKARK--GRTTIVIAHRLS-TVRNADVIAGFDDGVIVEKG 680
Cdd:cd03259    149 PSLLLLDEPLSALDAKLREELREELKELQRelGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
1110-1323 3.33e-42

ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 154.43  E-value: 3.33e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1110 VVFNYPT-RPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQL---LERfydPLAGKVLLDGKEIKRLN----VQWLRA 1181
Cdd:COG1136     10 LTKSYGTgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNIlggLDR---PTSGEVLIDGQDISSLSerelARLRRR 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1182 HLGIVSQEPILFDC-SIAENIA----YGDNSRVVSQEEIVRAAKEANIHAFIESLPNkystkvgdkgtQLSGGQKQRIAI 1256
Cdd:COG1136     87 HIGFVFQFFNLLPElTALENVAlpllLAGVSRKERRERARELLERVGLGDRLDHRPS-----------QLSGGQQQRVAI 155
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1149123047 1257 ARALVRQPHILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQNADLIVVFQNGRVKE 1323
Cdd:COG1136    156 ARALVNRPKLILADEPTGNLDSKTGEEVLELLRElnRELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
1114-1325 4.23e-42

ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.


Pssm-ID: 213224 [Multi-domain]  Cd Length: 228  Bit Score: 154.20  E-value: 4.23e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1114 YPTRPD-IPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWL---RAHLGIVSQE 1189
Cdd:cd03257     11 FPTGGGsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirRKEIQMVFQD 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1190 PI-----LFdcSIAENIA-----YGDNSRvvsQEEIVRAAKEANIH-----AFIESLPNkystkvgdkgtQLSGGQKQRI 1254
Cdd:cd03257     91 PMsslnpRM--TIGEQIAeplriHGKLSK---KEARKEAVLLLLVGvglpeEVLNRYPH-----------ELSGGQRQRV 154
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1149123047 1255 AIARALVRQPHILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHG 1325
Cdd:cd03257    155 AIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
462-686 5.61e-42

ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213262 [Multi-domain]  Cd Length: 242  Bit Score: 154.38  E-value: 5.61e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSRKevKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIG 541
Cdd:cd03295      1 IEFENVTKRYGGGK--KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  542 VVSQEPVLFA-TTIAENI-------RYGREnvtmdEIEKAVKEANAydfIMKLPHKfdTLVGERGAQLSGGQKQRIAIAR 613
Cdd:cd03295     79 YVIQQIGLFPhMTVEENIalvpkllKWPKE-----KIRERADELLA---LVGLDPA--EFADRYPHELSGGQQQRVGVAR 148
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1149123047  614 ALVRNPKILLLDEATSALDTESEAVVQVALDKARK--GRTTIVIAHRL-STVRNADVIAGFDDGVIVEKGNHDELM 686
Cdd:cd03295    149 ALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEIL 224
ABC_6TM_TAP cd18572
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ...
179-403 8.03e-42

Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.


Pssm-ID: 350016 [Multi-domain]  Cd Length: 289  Bit Score: 155.39  E-value: 8.03e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  179 EDMTRYAYYYSGIGAGVLVAAYIQVsfWCLA-AGRQIHK-IRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGI 256
Cdd:cd18572     33 EAFYRAVLLLLLLSVLSGLFSGLRG--GCFSyAGTRLVRrLRRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPL 110
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  257 GDKIGMFFQSMATFFTGFIVGFTRGWKLTLVILAISPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIA 336
Cdd:cd18572    111 STNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRYYRKLSKEIQDALAEANQVAEEALSNIRTVRS 190
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1149123047  337 FGGQKKELERYNKNLEEAKRIGIKKAITANISIGAAFLLIYASYALAFWYGTTLVLSGEYSIGQVLT 403
Cdd:cd18572    191 FATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFYGGHLVLSGRMSAGQLVT 257
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
1105-1323 8.72e-42

ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213260 [Multi-domain]  Cd Length: 220  Bit Score: 153.01  E-value: 8.72e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1105 VTFGEVVFNYPT-RPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNvqwlrAHL 1183
Cdd:cd03293      1 LEVRNVSKTYGGgGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG-----PDR 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1184 GIVSQEPILFD-CSIAENIAYGDNSRVVSqeeivRAAKEANIHAFIEslpnkystKVGDKGT------QLSGGQKQRIAI 1256
Cdd:cd03293     76 GYVFQQDALLPwLTVLDNVALGLELQGVP-----KAEARERAEELLE--------LVGLSGFenayphQLSGGMRQRVAL 142
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1149123047 1257 ARALVRQPHILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVFQN--GRVKE 1323
Cdd:cd03293    143 ARALAVDPDVLLLDEPFSALDALTREQLQEELLDiwRETGKTVLLVTHDIDeAVFLADRVVVLSArpGRIVA 214
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
1119-1326 1.09e-41

ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 157.18  E-value: 1.09e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1119 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQwlRAHLGIVSQEPILF-DCSI 1197
Cdd:COG3842     17 DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE--KRNVGMVFQDYALFpHLTV 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1198 AENIAYGDNSRVVSQEEIVRAAKEA----NIHAFIESLPNkystkvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEAT 1273
Cdd:COG3842     95 AENVAFGLRMRGVPKAEIRARVAELlelvGLEGLADRYPH-----------QLSGGQQQRVALARALAPEPRVLLLDEPL 163
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1149123047 1274 SALDTESEKVVQEALDK--AREGRTCIVIAHRLS---TIqnADLIVVFQNGRVKEHGT 1326
Cdd:COG3842    164 SALDAKLREEMREELRRlqRELGITFIYVTHDQEealAL--ADRIAVMNDGRIEQVGT 219
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
1123-1274 1.23e-41

ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.


Pssm-ID: 394964 [Multi-domain]  Cd Length: 150  Bit Score: 149.72  E-value: 1.23e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1123 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEPILF-DCSIAENI 1201
Cdd:pfam00005    1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENL 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1149123047 1202 AYGDNSrvvsqEEIVRAAKEANIHAFIE--SLPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATS 1274
Cdd:pfam00005   81 RLGLLL-----KGLSKREKDARAEEALEklGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
462-674 2.41e-41

ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213196 [Multi-domain]  Cd Length: 178  Bit Score: 150.03  E-value: 2.41e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYpsrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRT--INVRFLREI 539
Cdd:cd03229      1 LELKNVSKRY---GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDleDELPPLRRR 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  540 IGVVSQEPVLFAT-TIAENIRYGrenvtmdeiekavkeanaydfimklphkfdtlvgergaqLSGGQKQRIAIARALVRN 618
Cdd:cd03229     78 IGMVFQDFALFPHlTVLENIALG---------------------------------------LSGGQQQRVALARALAMD 118
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1149123047  619 PKILLLDEATSALDTESEAVVQVALD--KARKGRTTIVIAHRLSTVRN-ADVIAGFDDG 674
Cdd:cd03229    119 PDVLLLDEPTSALDPITRREVRALLKslQAQLGITVVLVTHDLDEAARlADRVVVLRDG 177
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
462-688 2.76e-41

ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];


Pssm-ID: 440213 [Multi-domain]  Cd Length: 320  Bit Score: 154.83  E-value: 2.76e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSRK-EVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDP---TEGMVSVDGQDIRTINVRFLR 537
Cdd:COG0444      2 LEVRNLKVYFPTRRgVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELR 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  538 EI----IGVVSQEPvlFA---------TTIAENIRYgRENVTMDEIEKAVKEA-------NAYDFIMKLPHkfdtlvger 597
Cdd:COG0444     82 KIrgreIQMIFQDP--MTslnpvmtvgDQIAEPLRI-HGGLSKAEARERAIELlervglpDPERRLDRYPH--------- 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  598 gaQLSGGQKQRIAIARALVRNPKILLLDEATSALDteseAVVQVA-LD-----KARKGRTTIVIAHRLSTVRN-ADVIA- 669
Cdd:COG0444    150 --ELSGGMRQRVMIARALALEPKLLIADEPTTALD----VTIQAQiLNllkdlQRELGLAILFITHDLGVVAEiADRVAv 223
                          250       260
                   ....*....|....*....|.
gi 1149123047  670 --GfddGVIVEKGNHDELMKE 688
Cdd:COG0444    224 myA---GRIVEEGPVEELFEN 241
PLN03232 PLN03232
ABC transporter C family member; Provisional
184-715 3.17e-41

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 166.30  E-value: 3.17e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  184 YAYYYSGIGAGvLVAAYIQVSFW----CLAAGRQIHKirkQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDK 259
Cdd:PLN03232   952 YIVVYALLGFG-QVAVTFTNSFWlissSLHAAKRLHD---AMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANL 1027
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  260 IGMFFQSMATFFTGFIVgftRGWKLTLVILAISPVLGLSAAVW---------AKILSSFTDKELlaYAKAGavaeEVLAA 330
Cdd:PLN03232  1028 MNMFMNQLWQLLSTFAL---IGTVSTISLWAIMPLLILFYAAYlyyqstsreVRRLDSVTRSPI--YAQFG----EALNG 1098
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  331 IRTVIAFGGQKKELERYNKNLEEAKRIGIKkAITAN-------ISIGAAFLLIYASYALaFWYGTT-----------LVL 392
Cdd:PLN03232  1099 LSSIRAYKAYDRMAKINGKSMDNNIRFTLA-NTSSNrwltirlETLGGVMIWLTATFAV-LRNGNAenqagfastmgLLL 1176
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  393 SGEYSIGQVLTvffSVLIGAFSVGQASPSIEAFANARGAAYEIFKIIDNKPSIDSYSKSGhkpdnikgNLEFRNVHFSYp 472
Cdd:PLN03232  1177 SYTLNITTLLS---GVLRQASKAENSLNSVERVGNYIDLPSEATAIIENNRPVSGWPSRG--------SIKFEDVHLRY- 1244
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  473 sRKEVK-ILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIGVVSQEPVLFA 551
Cdd:PLN03232  1245 -RPGLPpVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFS 1323
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  552 TTIAENIRYGRENVTMDeIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSAL 631
Cdd:PLN03232  1324 GTVRFNIDPFSEHNDAD-LWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASV 1402
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  632 DTESEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELM-KEKGIYFKLVTMQTAGNEVELENA 710
Cdd:PLN03232  1403 DVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLsRDTSAFFRMVHSTGPANAQYLSNL 1482

                   ....*
gi 1149123047  711 ADESK 715
Cdd:PLN03232  1483 VFERR 1487
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
1114-1332 3.61e-41

ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];


Pssm-ID: 440741 [Multi-domain]  Cd Length: 248  Bit Score: 152.26  E-value: 3.61e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1114 YPTRP-DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEPIL 1192
Cdd:COG1124     11 YGQGGrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVFQDPYA 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1193 -------FDCSIAE--NIAYGDNSrvvsQEEIVRAAKEANIH-AFIESLPNkystkvgdkgtQLSGGQKQRIAIARALVR 1262
Cdd:COG1124     91 slhprhtVDRILAEplRIHGLPDR----EERIAELLEQVGLPpSFLDRYPH-----------QLSGGQRQRVAIARALIL 155
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1149123047 1263 QPHILLLDEATSALDTesekVVQ-EALD-----KAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLLA 1332
Cdd:COG1124    156 EPELLLLDEPTSALDV----SVQaEILNllkdlREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLA 228
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
462-676 4.82e-41

ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.


Pssm-ID: 213229 [Multi-domain]  Cd Length: 213  Bit Score: 150.76  E-value: 4.82e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYpsrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDI--RTINVRFLREI 539
Cdd:cd03262      1 IEIKNLHKSF---GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQK 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  540 IGVVSQEPVLFA-TTIAENIRYGRENVT-MDEIEKavkEANAYDFIMK--LPHKFDtlvgERGAQLSGGQKQRIAIARAL 615
Cdd:cd03262     78 VGMVFQQFNLFPhLTVLENITLAPIKVKgMSKAEA---EERALELLEKvgLADKAD----AYPAQLSGGQQQRVAIARAL 150
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1149123047  616 VRNPKILLLDEATSALDTE-SEAVVQVALDKARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVI 676
Cdd:cd03262    151 AMNPKVMLFDEPTSALDPElVGEVLDVMKDLAEEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
ABC_6TM_exporters cd07346
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ...
121-435 5.55e-41

Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349983 [Multi-domain]  Cd Length: 292  Bit Score: 153.09  E-value: 5.55e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  121 MVVGTLAAIIHGAGLPLMMLVFGEMTDIFANAGNLEDLmsnitnrsdindtgffmnleedmtryaYYYSGIGAGVLVAA- 199
Cdd:cd07346      1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLL---------------------------LWIALLLLLLALLRa 53
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  200 ---YIQVSFWCLAAGRQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQSMATFFTGFIV 276
Cdd:cd07346     54 llsYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVI 133
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  277 GFTRGWKLTLVILAISPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKR 356
Cdd:cd07346    134 LFYLNWKLTLVALLLLPLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRD 213
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  357 IGIKKAITANISIGAAFLLIYASYALAFWYGTTLVLSGEYSIGQvLTVFFSVLIGAFS-VGQASPSIEAFANARGAAYEI 435
Cdd:cd07346    214 ANLRAARLSALFSPLIGLLTALGTALVLLYGGYLVLQGSLTIGE-LVAFLAYLGMLFGpIQRLANLYNQLQQALASLERI 292
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
1119-1333 1.07e-40

ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 150.53  E-value: 1.07e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1119 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTV---VQLLERfydPLAGKVLLDGKEI--KRLNVQWLRAHLGIVSQEPILF 1193
Cdd:COG1126     13 DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLlrcINLLEE---PDSGTITVDGEDLtdSKKDINKLRRKVGMVFQQFNLF 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1194 -DCSIAENIAYGdnSRVV---SQEEIVRAAKEanihafieslpnkYSTKVG--DKG----TQLSGGQKQRIAIARALVRQ 1263
Cdd:COG1126     90 pHLTVLENVTLA--PIKVkkmSKAEAEERAME-------------LLERVGlaDKAdaypAQLSGGQQQRVAIARALAME 154
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1149123047 1264 PHILLLDEATSALDTEsekVVQEALD--K--AREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLLAQ 1333
Cdd:COG1126    155 PKVMLFDEPTSALDPE---LVGEVLDvmRdlAKEGMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGPPEEFFEN 226
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
1110-1333 1.79e-40

ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440740 [Multi-domain]  Cd Length: 514  Bit Score: 157.76  E-value: 1.79e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1110 VVFNYPTRpDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDP---LAGKVLLDGKEIKRLNVQWLRAHLGIV 1186
Cdd:COG1123     10 LSVRYPGG-DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLDGRDLLELSEALRGRRIGMV 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1187 SQEPI--LFDCSIAENIAYGDNSRVVSQEEIVRAAKEANIHAFIESLPNKYSTkvgdkgtQLSGGQKQRIAIARALVRQP 1264
Cdd:COG1123     89 FQDPMtqLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPH-------QLSGGQRQRVAIAMALALDP 161
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1149123047 1265 HILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTI-QNADLIVVFQNGRVKEHGTHQQLLAQ 1333
Cdd:COG1123    162 DLLIADEPTTALDVTTQAEILDLLRElqRERGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILAA 233
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
462-678 1.89e-40

Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 149.05  E-value: 1.89e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPsrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTIN---VRFLRE 538
Cdd:COG2884      2 IRFENVSKRYP--GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrreIPYLRR 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  539 IIGVVSQE-PVLFATTIAENIRY-----GRENvtmDEIEKAVKEAnaydfIMK--LPHKFDTLVgergAQLSGGQKQRIA 610
Cdd:COG2884     80 RIGVVFQDfRLLPDRTVYENVALplrvtGKSR---KEIRRRVREV-----LDLvgLSDKAKALP----HELSGGEQQRVA 147
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1149123047  611 IARALVRNPKILLLDEATSALDTE-SEAVVQVaLDKARKGRTTIVIA-HRLSTVRNAD--VIAgFDDGVIVE 678
Cdd:COG2884    148 IARALVNRPELLLADEPTGNLDPEtSWEIMEL-LEEINRRGTTVLIAtHDLELVDRMPkrVLE-LEDGRLVR 217
ABC_6TM_exporters cd07346
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ...
781-1078 1.99e-40

Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349983 [Multi-domain]  Cd Length: 292  Bit Score: 151.55  E-value: 1.99e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  781 FVVGVFCAIINGGLQPAFAIIFSKIIGVFTriddPETKRQNSNLFSLLFLALGIISFITFFLQGFTFGKAGEILTKRLRY 860
Cdd:cd07346      1 LLLALLLLLLATALGLALPLLTKLLIDDVI----PAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRR 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  861 MVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIGSRLAVITQNIANLGTGIIISFIYGWQLTLLLLAIVPIIAI 940
Cdd:cd07346     77 DLFRHLQRLSLSFFD--RNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVL 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  941 AGVVEMKMLSGQALKDKKELEGSGKIATEAIENFRTVVSLTQEQKFEHMYAQSLQVPYRNSLRKAHIFGITFSFTQAMMY 1020
Cdd:cd07346    155 ILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTA 234
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1149123047 1021 FSYAGCFRFGAYLVAHKLMSFEDVLLVFSAVVFGAMAVGQVSSFAPDYAKAKISAAHI 1078
Cdd:cd07346    235 LGTALVLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
1104-1331 2.62e-40

ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];


Pssm-ID: 440737 [Multi-domain]  Cd Length: 254  Bit Score: 149.81  E-value: 2.62e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1104 NVTFGevvfnYPTRPdipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHL 1183
Cdd:COG1120      6 NLSVG-----YGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1184 GIVSQEPIL-FDCSIAENIAYG-----DNSRVVSQE--EIVRAA-KEANIHAFIE-SLpnkystkvgdkgTQLSGGQKQR 1253
Cdd:COG1120     78 AYVPQEPPApFGLTVRELVALGryphlGLFGRPSAEdrEAVEEAlERTGLEHLADrPV------------DELSGGERQR 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1254 IAIARALVRQPHILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVFQNGRVKEHGTHQQL 1330
Cdd:COG1120    146 VLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRlaRERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEV 225

                   .
gi 1149123047 1331 L 1331
Cdd:COG1120    226 L 226
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
462-688 3.08e-40

ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];


Pssm-ID: 440737 [Multi-domain]  Cd Length: 254  Bit Score: 149.81  E-value: 3.08e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIG 541
Cdd:COG1120      2 LEAENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  542 VVSQEPVL-FATTIAENIRYGR---------ENVTMDEI-EKAVKEANAYDFIMKLphkFDTlvgergaqLSGGQKQRIA 610
Cdd:COG1120     79 YVPQEPPApFGLTVRELVALGRyphlglfgrPSAEDREAvEEALERTGLEHLADRP---VDE--------LSGGERQRVL 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  611 IARALVRNPKILLLDEATSALDteseavV--QVA-LD-----KARKGRTTIVIAHRLS-TVRNADVIAGFDDGVIVEKGN 681
Cdd:COG1120    148 IARALAQEPPLLLLDEPTSHLD------LahQLEvLEllrrlARERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGP 221

                   ....*..
gi 1149123047  682 HDELMKE 688
Cdd:COG1120    222 PEEVLTP 228
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
463-674 4.63e-40

ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213179 [Multi-domain]  Cd Length: 157  Bit Score: 145.47  E-value: 4.63e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  463 EFRNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIGV 542
Cdd:cd00267      1 EIENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  543 VSQepvlfattiaenirygrenvtmdeiekavkeanaydfimklphkfdtlvgergaqLSGGQKQRIAIARALVRNPKIL 622
Cdd:cd00267     78 VPQ-------------------------------------------------------LSGGQRQRVALARALLLNPDLL 102
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1149123047  623 LLDEATSALDTES-EAVVQVALDKARKGRTTIVIAHRLSTVRNA-DVIAGFDDG 674
Cdd:cd00267    103 LLDEPTSGLDPASrERLLELLRELAEEGRTVIIVTHDPELAELAaDRVIVLKDG 156
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
462-680 7.13e-40

ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 151.79  E-value: 7.13e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYpsrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDI--RTINVRFlrei 539
Cdd:COG3842      6 LELENVSKRY---GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVtgLPPEKRN---- 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  540 IGVVSQEPVLFA-TTIAENIRYG--RENVTMDEIEKAVKEANAydfIMKLPHKFDTLVgergAQLSGGQKQRIAIARALV 616
Cdd:COG3842     79 VGMVFQDYALFPhLTVAENVAFGlrMRGVPKAEIRARVAELLE---LVGLEGLADRYP----HQLSGGQQQRVALARALA 151
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1149123047  617 RNPKILLLDEATSALDTESEAVVQVALDK--ARKGRTTIVIAHRLS---TVrnADVIAGFDDGVIVEKG 680
Cdd:COG3842    152 PEPRVLLLDEPLSALDAKLREEMREELRRlqRELGITFIYVTHDQEealAL--ADRIAVMNDGRIEQVG 218
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
1110-1323 8.46e-40

ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 148.70  E-value: 8.46e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1110 VVFNYPTRP-DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLnvqwlRAHLGIVSQ 1188
Cdd:COG1116     13 VSKRFPTGGgGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGP-----GPDRGVVFQ 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1189 EPILFD-CSIAENIAYGDNSRVVSQEEIVRAAKEA----NIHAFIESLPNkystkvgdkgtQLSGGQKQRIAIARALVRQ 1263
Cdd:COG1116     88 EPALLPwLTVLDNVALGLELRGVPKAERRERARELlelvGLAGFEDAYPH-----------QLSGGMRQRVAIARALAND 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1264 PHILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAH------RLstiqnADLIVVFQN--GRVKE 1323
Cdd:COG1116    157 PEVLLMDEPFGALDALTRERLQDELLRlwQETGKTVLFVTHdvdeavFL-----ADRVVVLSArpGRIVE 221
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
190-695 2.55e-39

multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]


Pssm-ID: 188098 [Multi-domain]  Cd Length: 1522  Bit Score: 160.11  E-value: 2.55e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  190 GIGAGVLVAAY-IQVSFWCLAAGRQIHKirkQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQSMA 268
Cdd:TIGR00957 1015 GILQGFAVFGYsMAVSIGGIQASRVLHQ---DLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLF 1091
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  269 TFFTGFIVGFTRGWKLTLVILAISPVLGLSAAVWAKilSSFTDKELLAYAKAGAVAE--EVLAAIRTVIAFGGQKKELER 346
Cdd:TIGR00957 1092 NVIGALIVILLATPIAAVIIPPLGLLYFFVQRFYVA--SSRQLKRLESVSRSPVYSHfnETLLGVSVIRAFEEQERFIHQ 1169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  347 YNKNLEEAKRiGIKKAITAN--ISIGAAFL-----LIYASYALAFWYGTTLVLSGeysigqvLTVFFSVLIGAFSVGQAS 419
Cdd:TIGR00957 1170 SDLKVDENQK-AYYPSIVANrwLAVRLECVgncivLFAALFAVISRHSLSAGLVG-------LSVSYSLQVTFYLNWLVR 1241
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  420 PSIEAFANArgAAYEIFKIIDNKPSIDSYSKSGHKPDNI---KGNLEFRNVHFSYpsRKEVK-ILKGLNLKVQSGQTVAL 495
Cdd:TIGR00957 1242 MSSEMETNI--VAVERLKEYSETEKEAPWQIQETAPPSGwppRGRVEFRNYCLRY--REDLDlVLRHINVTIHGGEKVGI 1317
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  496 VGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIGVVSQEPVLFATTIAENI----RYGRENVTMdeie 571
Cdd:TIGR00957 1318 VGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLdpfsQYSDEEVWW---- 1393
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  572 kAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARKGRT 651
Cdd:TIGR00957 1394 -ALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCT 1472
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....
gi 1149123047  652 TIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELMKEKGIYFKL 695
Cdd:TIGR00957 1473 VLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSM 1516
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
1116-1333 3.86e-39

ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213225 [Multi-domain]  Cd Length: 233  Bit Score: 145.80  E-value: 3.86e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1116 TRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQ---LLERfydPLAGKVLLDGKEIKRLN---VQWLRAHLGIVSQE 1189
Cdd:cd03258     14 TGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRcinGLER---PTSGSVLVDGTDLTLLSgkeLRKARRRIGMIFQH 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1190 PILFDC-SIAENIAYgdnsrvvsQEEIVRAAKeANIHAFIESLPN--KYSTKVGDKGTQLSGGQKQRIAIARALVRQPHI 1266
Cdd:cd03258     91 FNLLSSrTVFENVAL--------PLEIAGVPK-AEIEERVLELLElvGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1267 LLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLLAQ 1333
Cdd:cd03258    162 LLCDEATSALDPETTQSILALLRDinRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVFAN 231
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
469-1342 8.81e-39

cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]


Pssm-ID: 273530 [Multi-domain]  Cd Length: 1490  Bit Score: 158.54  E-value: 8.81e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  469 FSYPSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQdirtinvrflreiIGVVSQEPV 548
Cdd:TIGR01271  431 FSNFSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQTSW 497
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  549 LFATTIAENIRYGrenVTMDEIE--KAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDE 626
Cdd:TIGR01271  498 IMPGTIKDNIIFG---LSYDEYRytSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDS 574
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  627 ATSALD--TESEaVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELMKEKGIY------------ 692
Cdd:TIGR01271  575 PFTHLDvvTEKE-IFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFsslllgleafdn 653
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  693 -------------------------------------------------------------FKLV--TMQTAgNEVELEN 709
Cdd:TIGR01271  654 fsaerrnsiltetlrrvsidgdstvfsgpetikqsfkqpppefaekrkqsiilnpiasarkFSFVqmGPQKA-QATTIED 732
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  710 AADE--------------------------------SKSEIDALEMSSNDSRSSLIRKR---STRRSVRGSQAQD----- 749
Cdd:TIGR01271  733 AVREpserkfslvpedeqgeeslprgnqyhhglqhqAQRRQSVLQLMTHSNRGENRREQlqtSFRKKSSITQQNElasel 812
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  750 ----RKLSTKEALD------------------ESIPPVSFWR------IMKLNLTEWPYFVVGVFCAIINGGLQPAFaII 801
Cdd:TIGR01271  813 diysRRLSKDSVYEiseeineedlkecfaderENVFETTTWNtylryiTTNRNLVFVLIFCLVIFLAEVAASLLGLW-LI 891
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  802 FSKIIGVFTRIDDPETKRQNSNLFSLL-------------------FLALGiisfitfFLQGFTFGKAGEILTKRLRYMV 862
Cdd:TIGR01271  892 TDNPSAPNYVDQQHANASSPDVQKPVIitptsayyifyiyvgtadsVLALG-------FFRGLPLVHTLLTVSKRLHEQM 964
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  863 FRSMLRQDVSWFDDPKntTGALTTRLANDAAQVKGAIGSRLAVITQ-NIANLGTGIIISFIYGWqltlLLLAIVPIIAIA 941
Cdd:TIGR01271  965 LHSVLQAPMAVLNTMK--AGRILNRFTKDMAIIDDMLPLTLFDFIQlTLIVLGAIFVVSVLQPY----IFIAAIPVAVIF 1038
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  942 GVVEMKML-SGQALKdKKELEGSGKIATEAIENFR---TVVSLTQEQKFEHMYAQSLQVPYRN-----------SLRKAH 1006
Cdd:TIGR01271 1039 IMLRAYFLrTSQQLK-QLESEARSPIFSHLITSLKglwTIRAFGRQSYFETLFHKALNLHTANwflylstlrwfQMRIDI 1117
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1007 IFGITFSftqAMMYFSYA----GCFRFGAYL-VAHKLMSFEDVLLVFSAVVFGAM-AVGQVSSF---APDYAKAKISAAH 1077
Cdd:TIGR01271 1118 IFVFFFI---AVTFIAIGtnqdGEGEVGIILtLAMNILSTLQWAVNSSIDVDGLMrSVSRVFKFidlPQEEPRPSGGGGK 1194
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1078 I----IMIIEKTPLIDSYSTEGLMpntlegnvTFGEVVFNYpTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL 1153
Cdd:TIGR01271 1195 YqlstVLVIENPHAQKCWPSGGQM--------DVQGLTAKY-TEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSAL 1265
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1154 ERFYDPlAGKVLLDGKEIKRLNVQWLRAHLGIVSQEPILFDCSIAENIaygDNSRVVSQEEIVRAAKEANIHAFIESLPN 1233
Cdd:TIGR01271 1266 LRLLST-EGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNL---DPYEQWSDEEIWKVAEEVGLKSVIEQFPD 1341
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1234 KYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLI 1313
Cdd:TIGR01271 1342 KLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQF 1421
                         1050      1060
                   ....*....|....*....|....*....
gi 1149123047 1314 VVFQNGRVKEHGTHQQLLAQKGIYFSMVS 1342
Cdd:TIGR01271 1422 LVIEGSSVKQYDSIQKLLNETSLFKQAMS 1450
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
463-680 1.96e-38

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 147.25  E-value: 1.96e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  463 EFRNVHFSYP-SRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREI-- 539
Cdd:PRK11153     3 ELKNISKVFPqGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKArr 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  540 -IGVVSQEPVLFAT-TIAENIRYGRE--NVTMDEIEKAVKE----------ANAYdfimklPhkfdtlvgergAQLSGGQ 605
Cdd:PRK11153    83 qIGMIFQHFNLLSSrTVFDNVALPLElaGTPKAEIKARVTEllelvglsdkADRY------P-----------AQLSGGQ 145
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1149123047  606 KQRIAIARALVRNPKILLLDEATSALDTE-SEAVVQVALDKARKGRTTIV-IAHRLSTVRN-ADVIAGFDDGVIVEKG 680
Cdd:PRK11153   146 KQRVAIARALASNPKVLLCDEATSALDPAtTRSILELLKDINRELGLTIVlITHEMDVVKRiCDRVAVIDAGRLVEQG 223
PTZ00243 PTZ00243
ABC transporter; Provisional
478-1341 1.97e-38

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 157.25  E-value: 1.97e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  478 KILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVsvdgqdirtinvrFLREIIGVVSQEPVLFATTIAEN 557
Cdd:PTZ00243   674 VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-------------WAERSIAYVPQQAWIMNATVRGN 740
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  558 IRYGRENVTMDeIEKAVK----EANaydfIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDT 633
Cdd:PTZ00243   741 ILFFDEEDAAR-LADAVRvsqlEAD----LAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDA 815
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  634 E-SEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELMkEKGIYFKLvTMQTAGNEVELENAAD 712
Cdd:PTZ00243   816 HvGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFM-RTSLYATL-AAELKENKDSKEGDAD 893
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  713 ESKSEIDALE--MSSNDSRSSLIRKRSTRRSVRGSQAQDRKLSTKEALDESIPPvsfWRimklnlTEWPYFVvgvFCaii 790
Cdd:PTZ00243   894 AEVAEVDAAPggAVDHEPPVAKQEGNAEGGDGAALDAAAGRLMTREEKASGSVP---WS------TYVAYLR---FC--- 958
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  791 nGGLQPAFAIIFSKIIGVFTRID----------DPETKRQNSNLFSLLFLA-LGIISFITFFLQGFTFGKAGeilTKRLR 859
Cdd:PTZ00243   959 -GGLHAAGFVLATFAVTELVTVSsgvwlsmwstRSFKLSAATYLYVYLGIVlLGTFSVPLRFFLSYEAMRRG---SRNMH 1034
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  860 YMVFRSMLRQDVSWFDdpknTT--GALTTRLANDAaqvkGAIGSRLAVITQNIANLGTGIIIS-FIYGWQLTLLLLAIVP 936
Cdd:PTZ00243  1035 RDLLRSVSRGTMSFFD----TTplGRILNRFSRDI----DILDNTLPMSYLYLLQCLFSICSSiLVTSASQPFVLVALVP 1106
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  937 ------------------IIAIAGVVEMKMLS--GQALKDKKELEGSGK---IATEAIENFRTVVSLTQEQKFEHMYAqS 993
Cdd:PTZ00243  1107 cgylyyrlmqfynsanreIRRIKSVAKSPVFTllEEALQGSATITAYGKahlVMQEALRRLDVVYSCSYLENVANRWL-G 1185
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  994 LQVPY---------------RNSLRKAH--IFGITFSFTQAMMYFSYAGCFRFGAYLVAHKLMSFEDVLLVFSAVVFGAM 1056
Cdd:PTZ00243  1186 VRVEFlsnivvtvialigviGTMLRATSqeIGLVSLSLTMAMQTTATLNWLVRQVATVEADMNSVERLLYYTDEVPHEDM 1265
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1057 AvgQVSSFAPDYAKAKISAAHIImiieKTPLIDSYSTEGLMPNTLE-GNVTFGEVVFNYptRPDIP-VLQGLSLEVKKGQ 1134
Cdd:PTZ00243  1266 P--ELDEEVDALERRTGMAADVT----GTVVIEPASPTSAAPHPVQaGSLVFEGVQMRY--REGLPlVLRGVSFRIAPRE 1337
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1135 TLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEPILFDCSIAENIaygDNSRVVSQEE 1214
Cdd:PTZ00243  1338 KVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNV---DPFLEASSAE 1414
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1215 IVRAAKEANIHAFIESLPNKYSTKVGDKGTQLSGGQKQRIAIARALV-RQPHILLLDEATSALDTESEKVVQEALDKARE 1293
Cdd:PTZ00243  1415 VWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLkKGSGFILMDEATANIDPALDRQIQATVMSAFS 1494
                          890       900       910       920
                   ....*....|....*....|....*....|....*....|....*....
gi 1149123047 1294 GRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQL-LAQKGIYFSMV 1341
Cdd:PTZ00243  1495 AYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELvMNRQSIFHSMV 1543
ECF_ATPase_1 TIGR04520
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
1110-1334 2.05e-38

energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]


Pssm-ID: 275313 [Multi-domain]  Cd Length: 268  Bit Score: 144.88  E-value: 2.05e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1110 VVFNYPtRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIK-RLNVQWLRAHLGIVSQ 1188
Cdd:TIGR04520    6 VSFSYP-ESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLdEENLWEIRKKVGMVFQ 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1189 EPilfD----CSIAEN-IAYGDNSRVVSQEEIVR----AAKEANIHAFIESLPNKystkvgdkgtqLSGGQKQRIAIARA 1259
Cdd:TIGR04520   85 NP---DnqfvGATVEDdVAFGLENLGVPREEMRKrvdeALKLVGMEDFRDREPHL-----------LSGGQKQRVAIAGV 150
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1149123047 1260 LVRQPHILLLDEATSALDTESEKVVQEALDKAR--EGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQK 1334
Cdd:TIGR04520  151 LAMRPDIIILDEATSMLDPKGRKEVLETIRKLNkeEGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPREIFSQV 227
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
462-685 2.24e-38

ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 144.41  E-value: 2.24e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYpsrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYD--P---TEGMVSVDGQDI--RTINVR 534
Cdd:COG1117     12 IEVRNLNVYY---GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPgarVEGEILLDGEDIydPDVDVV 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  535 FLREIIGVVSQEPVLFATTIAENIRYG------RENVTMDEI-EKAVKEANAYDFImklphKfDTLvGERGAQLSGGQKQ 607
Cdd:COG1117     89 ELRRRVGMVFQKPNPFPKSIYDNVAYGlrlhgiKSKSELDEIvEESLRKAALWDEV-----K-DRL-KKSALGLSGGQQQ 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  608 RIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARKgRTTIVI-------AHRLStvrnaDVIAGFDDGVIVEKG 680
Cdd:COG1117    162 RLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKK-DYTIVIvthnmqqAARVS-----DYTAFFYLGELVEFG 235

                   ....*
gi 1149123047  681 NHDEL 685
Cdd:COG1117    236 PTEQI 240
ABCC_SUR2 cd03288
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...
1121-1341 2.55e-38

ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.


Pssm-ID: 213255 [Multi-domain]  Cd Length: 257  Bit Score: 144.28  E-value: 2.55e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1121 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEPILFDCSIAEN 1200
Cdd:cd03288     35 PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFN 114
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1201 IaygDNSRVVSQEEIVRAAKEANIHAFIESLPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTES 1280
Cdd:cd03288    115 L---DPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMAT 191
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1149123047 1281 EKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQK-GIYFSMV 1341
Cdd:cd03288    192 ENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEdGVFASLV 253
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
1116-1320 3.47e-38

ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213196 [Multi-domain]  Cd Length: 178  Bit Score: 141.17  E-value: 3.47e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1116 TRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLN--VQWLRAHLGIVSQEPILF 1193
Cdd:cd03229      9 RYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRRIGMVFQDFALF 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1194 -DCSIAENIAYGdnsrvvsqeeivraakeanihafieslpnkystkvgdkgtqLSGGQKQRIAIARALVRQPHILLLDEA 1272
Cdd:cd03229     89 pHLTVLENIALG-----------------------------------------LSGGQQQRVALARALAMDPDVLLLDEP 127
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1149123047 1273 TSALDTESEKVVQEALD--KAREGRTCIVIAHRLSTIQN-ADLIVVFQNGR 1320
Cdd:cd03229    128 TSALDPITRREVRALLKslQAQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
1119-1333 3.67e-38

ABC-type multidrug transport system, ATPase component [Defense mechanisms];


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 143.28  E-value: 3.67e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1119 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWlRAHLGIVSQEPILF-DCSI 1197
Cdd:COG1131     12 DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEV-RRRIGYVPQEPALYpDLTV 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1198 AENIAYGDNSRVVSQEEIVRAAKEAnIHAFieSLPNKYSTKVGdkgtQLSGGQKQRIAIARALVRQPHILLLDEATSALD 1277
Cdd:COG1131     91 RENLRFFARLYGLPRKEARERIDEL-LELF--GLTDAADRKVG----TLSGGMKQRLGLALALLHDPELLILDEPTSGLD 163
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1149123047 1278 TESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLLAQ 1333
Cdd:COG1131    164 PEARRELWELLRElAAEGKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELKAR 221
ABC_6TM_ABCB10_like cd18573
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ...
179-419 3.91e-38

Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.


Pssm-ID: 350017 [Multi-domain]  Cd Length: 294  Bit Score: 144.96  E-value: 3.91e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  179 EDMTRYAYYYSGIGAGVLV----AAYIQVSFWCLAAGRQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINE 254
Cdd:cd18573     34 EIFGLSLKTFALALLGVFVvgaaANFGRVYLLRIAGERIVARLRKRLFKSILRQDAAFFDKNKTGELVSRLSSDTSVVGK 113
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  255 GIGDKIGMFFQSMATFFTGFIVGFTRGWKLTLVILAISPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTV 334
Cdd:cd18573    114 SLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRYVRKLSKQVQDALADATKVAEERLSNIRTV 193
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  335 IAFGGQKKELERYNKNLEEAKRIGIKKAITANISIGAAFLLIYASYALAFWYGTTLVLSGEYSIGQvLTVF--FSVLIGA 412
Cdd:cd18573    194 RAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLLSVLYYGGSLVASGELTVGD-LTSFlmYAVYVGS 272

                   ....*..
gi 1149123047  413 fSVGQAS 419
Cdd:cd18573    273 -SVSGLS 278
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
462-690 4.30e-38

ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];


Pssm-ID: 443618 [Multi-domain]  Cd Length: 243  Bit Score: 143.07  E-value: 4.30e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYpsrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIiG 541
Cdd:COG4555      2 IEVENLSKKY---GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQI-G 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  542 VVSQEPVLFAT-TIAENIRYGRE--NVTMDEIEKAVKEanaYDFIMKLPHKFDTLVGErgaqLSGGQKQRIAIARALVRN 618
Cdd:COG4555     78 VLPDERGLYDRlTVRENIRYFAElyGLFDEELKKRIEE---LIELLGLEEFLDRRVGE----LSTGMKKKVALARALVHD 150
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1149123047  619 PKILLLDEATSALDTES-EAVVQVALDKARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKGNHDELMKEKG 690
Cdd:COG4555    151 PKVLLLDEPTNGLDVMArRLLREILRALKKEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
462-676 5.95e-38

ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213197 [Multi-domain]  Cd Length: 173  Bit Score: 140.23  E-value: 5.95e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTiNVRFLREIIG 541
Cdd:cd03230      1 IEVRNLSKRYGKKT---ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIG 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  542 VVSQEPVLFAT-TIAENIRYgrenvtmdeiekavkeanaydfimklphkfdtlvgergaqlSGGQKQRIAIARALVRNPK 620
Cdd:cd03230     77 YLPEEPSLYENlTVRENLKL-----------------------------------------SGGMKQRLALAQALLHDPE 115
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1149123047  621 ILLLDEATSALDTES-EAVVQVALDKARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVI 676
Cdd:cd03230    116 LLILDEPTSGLDPESrREFWELLRELKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
1119-1330 7.36e-38

ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 142.87  E-value: 7.36e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1119 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD--PLA---GKVLLDGKEI--KRLNVQWLRAHLGIVSQEPI 1191
Cdd:COG1117     23 DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPGArveGEILLDGEDIydPDVDVVELRRRVGMVFQKPN 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1192 LFDCSIAENIAYG-----DNSRVVsQEEIVRAA-KEANihafiesLPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQPH 1265
Cdd:COG1117    103 PFPKSIYDNVAYGlrlhgIKSKSE-LDEIVEESlRKAA-------LWDEVKDRLKKSALGLSGGQQQRLCIARALAVEPE 174
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1149123047 1266 ILLLDEATSALDTESEKVVQEALDKAREgRTCIVI-------AHRLStiqnaDLIVVFQNGRVKEHGTHQQL 1330
Cdd:COG1117    175 VLLMDEPTSALDPISTAKIEELILELKK-DYTIVIvthnmqqAARVS-----DYTAFFYLGELVEFGPTEQI 240
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
462-674 1.20e-37

ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.


Pssm-ID: 213217 [Multi-domain]  Cd Length: 204  Bit Score: 140.30  E-value: 1.20e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSRKEV--KILKGLNLKVQSGQTVALVGNSGCGKSTTVQ-LMQRLyDPTEGMVSVDGQdirtinvrflre 538
Cdd:cd03250      1 ISVEDASFTWDSGEQEtsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSaLLGEL-EKLSGSVSVPGS------------ 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  539 iIGVVSQEPVLFATTIAENIRYGREnvtMDEIE-KAVKEANA--YDFIMkLPHKFDTLVGERGAQLSGGQKQRIAIARAL 615
Cdd:cd03250     68 -IAYVSQEPWIQNGTIRENILFGKP---FDEERyEKVIKACAlePDLEI-LPDGDLTEIGEKGINLSGGQKQRISLARAV 142
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1149123047  616 VRNPKILLLDEATSALDTESEAVV--QVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDG 674
Cdd:cd03250    143 YSDADIYLLDDPLSAVDAHVGRHIfeNCILGLLLNNKTRILVTHQLQLLPHADQIVVLDNG 203
ABC_6TM_TAP_ABCB8_10_like cd18557
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ...
784-1076 1.24e-37

Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.


Pssm-ID: 350001 [Multi-domain]  Cd Length: 289  Bit Score: 143.47  E-value: 1.24e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  784 GVFCAIINGGLQPAFAIIFSKIIGVFTRIDDPEtkrqNSNLFSLLFLALGIISFITFFLQGFTFGKAGEILTKRLRYMVF 863
Cdd:cd18557      1 GLLFLLISSAAQLLLPYLIGRLIDTIIKGGDLD----VLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLF 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  864 RSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIGSRLAVITQNIANLGTGIIISFIYGWQLTLLLLAIVPIIAIAGV 943
Cdd:cd18557     77 SSLLRQEIAFFD--KHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASK 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  944 V---EMKMLSGQALkdkKELEGSGKIATEAIENFRTVVSLTQEQKFEHMYAQSLQVPYRNSLRKAHIFGITFSFTQAMMY 1020
Cdd:cd18557    155 IygrYIRKLSKEVQ---DALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIY 231
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1149123047 1021 FSYAGCFRFGAYLVAHK------LMSFedvlLVFSAVVfgAMAVGQVSSFAPDYAKAkISAA 1076
Cdd:cd18557    232 LSLLLVLWYGGYLVLSGqltvgeLTSF----ILYTIMV--ASSVGGLSSLLADIMKA-LGAS 286
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
462-632 1.70e-37

ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 144.83  E-value: 1.70e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYpsrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFlREIiG 541
Cdd:COG3839      4 LELENVSKSY---GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD-RNI-A 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  542 VVSQEPVLF-ATTIAENIRYG--RENVTMDEIEKAVKEANAydfIMKLPHkfdtLVGERGAQLSGGQKQRIAIARALVRN 618
Cdd:COG3839     79 MVFQSYALYpHMTVYENIAFPlkLRKVPKAEIDRRVREAAE---LLGLED----LLDRKPKQLSGGQRQRVALGRALVRE 151
                          170
                   ....*....|....
gi 1149123047  619 PKILLLDEATSALD 632
Cdd:COG3839    152 PKVFLLDEPLSNLD 165
PhnC COG3638
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ...
462-677 1.92e-37

ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 442855 [Multi-domain]  Cd Length: 249  Bit Score: 141.35  E-value: 1.92e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSRKevKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREI-- 539
Cdd:COG3638      3 LELRNLSKRYPGGT--PALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLrr 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  540 -IGVVSQEPVLFA-TTIAENI---RYGREN--------VTMDEIEKAvkeanaYDFIMK--LPHKFDtlvgERGAQLSGG 604
Cdd:COG3638     81 rIGMIFQQFNLVPrLSVLTNVlagRLGRTStwrsllglFPPEDRERA------LEALERvgLADKAY----QRADQLSGG 150
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1149123047  605 QKQRIAIARALVRNPKILLLDEATSALDTE-SEAVVQVALDKAR-KGRTTIVIAHRLSTVRN-ADVIAGFDDGVIV 677
Cdd:COG3638    151 QQQRVAIARALVQEPKLILADEPVASLDPKtARQVMDLLRRIAReDGITVVVNLHQVDLARRyADRIIGLRDGRVV 226
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
463-691 2.24e-37

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 142.05  E-value: 2.24e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  463 EFRNVHFSYPSrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIGV 542
Cdd:PRK13632     9 KVENVSFSYPN-SENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  543 VSQEP--VLFATTIAENIRYGREN--VTMDE----IEKAVKEANAYDFIMKLPHKfdtlvgergaqLSGGQKQRIAIARA 614
Cdd:PRK13632    88 IFQNPdnQFIGATVEDDIAFGLENkkVPPKKmkdiIDDLAKKVGMEDYLDKEPQN-----------LSGGQKQRVAIASV 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1149123047  615 LVRNPKILLLDEATSALDTES-EAVVQVALDKARKG-RTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELMKEKGI 691
Cdd:PRK13632   157 LALNPEIIIFDESTSMLDPKGkREIKKIMVDLRKTRkKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNKEI 235
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
1109-1320 2.27e-37

ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213179 [Multi-domain]  Cd Length: 157  Bit Score: 137.76  E-value: 2.27e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1109 EVVFNYPTRPdipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQ 1188
Cdd:cd00267      4 NLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1189 epilfdcsiaeniaygdnsrvvsqeeivraakeanihafieslpnkystkvgdkgtqLSGGQKQRIAIARALVRQPHILL 1268
Cdd:cd00267     81 ---------------------------------------------------------LSGGQRQRVALARALLLNPDLLL 103
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1149123047 1269 LDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQNA-DLIVVFQNGR 1320
Cdd:cd00267    104 LDEPTSGLDPASRERLLELLRElAEEGRTVIIVTHDPELAELAaDRVIVLKDGK 157
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
1105-1332 2.34e-37

ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213262 [Multi-domain]  Cd Length: 242  Bit Score: 140.90  E-value: 2.34e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1105 VTFGEVVFNYPTRPdiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLG 1184
Cdd:cd03295      1 IEFENVTKRYGGGK--KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1185 IVSQEPILF-DCSIAENIAYGDNSRVVSQEEIVRAAKE--ANIHAFIESLPNKYStkvgdkgTQLSGGQKQRIAIARALV 1261
Cdd:cd03295     79 YVIQQIGLFpHMTVEENIALVPKLLKWPKEKIRERADEllALVGLDPAEFADRYP-------HELSGGQQQRVGVARALA 151
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1149123047 1262 RQPHILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRL-STIQNADLIVVFQNGRVKEHGTHQQLLA 1332
Cdd:cd03295    152 ADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILR 225
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
1114-1326 8.47e-37

ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 142.52  E-value: 8.47e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1114 YPTRP-DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQ---LLERfydPLAGKVLLDGKEIKRLNVQWLRA---HLGIV 1186
Cdd:COG1135     11 FPTKGgPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRcinLLER---PTSGSVLVDGVDLTALSERELRAarrKIGMI 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1187 SQEPILFD-CSIAENIAY-----GdnsrvVSQEEIVRAAKEanihaFIESlpnkystkVG--DKG----TQLSGGQKQRI 1254
Cdd:COG1135     88 FQHFNLLSsRTVAENVALpleiaG-----VPKAEIRKRVAE-----LLEL--------VGlsDKAdaypSQLSGGQKQRV 149
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1149123047 1255 AIARALVRQPHILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGT 1326
Cdd:COG1135    150 GIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRelGLTIVLITHEMDVVRRiCDRVAVLENGRIVEQGP 224
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
1107-1336 8.81e-37

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 140.51  E-value: 8.81e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1107 FGEVVFNYPTRpDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIV 1186
Cdd:PRK13632    10 VENVSFSYPNS-ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGII 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1187 SQEPilfD-----CSIAENIAYGDNSRVVSQEE----IVRAAKEANIHAFIESLPNKystkvgdkgtqLSGGQKQRIAIA 1257
Cdd:PRK13632    89 FQNP---DnqfigATVEDDIAFGLENKKVPPKKmkdiIDDLAKKVGMEDYLDKEPQN-----------LSGGQKQRVAIA 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1258 RALVRQPHILLLDEATSALDTESEKVVQEALDKAREGR--TCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQKG 1335
Cdd:PRK13632   155 SVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNKE 234

                   .
gi 1149123047 1336 I 1336
Cdd:PRK13632   235 I 235
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
1121-1332 1.60e-36

ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440744 [Multi-domain]  Cd Length: 241  Bit Score: 138.57  E-value: 1.60e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1121 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNV---QWLRAHLGIVSQEPILFDC-S 1196
Cdd:COG1127     19 VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEkelYELRRRIGMLFQGGALFDSlT 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1197 IAENIAYG-DNSRVVSQEEIVRAAKEA----NIHAFIESLPNkystkvgdkgtQLSGGQKQRIAIARALVRQPHILLLDE 1271
Cdd:COG1127     99 VFENVAFPlREHTDLSEAEIRELVLEKlelvGLPGAADKMPS-----------ELSGGMRKRVALARALALDPEILLYDE 167
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1149123047 1272 ATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLLA 1332
Cdd:COG1127    168 PTAGLDPITSAVIDELIRELRDelGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLA 231
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
474-688 1.82e-36

ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 443658 [Multi-domain]  Cd Length: 329  Bit Score: 141.41  E-value: 1.82e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  474 RKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREI---IGVVSQEPvlF 550
Cdd:COG4608     28 VGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLrrrMQMVFQDP--Y 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  551 A---------TTIAENIRYgRENVTMDEIEKAVKEA------NAyDFIMKLPHKFdtlvgergaqlSGGQKQRIAIARAL 615
Cdd:COG4608    106 AslnprmtvgDIIAEPLRI-HGLASKAERRERVAELlelvglRP-EHADRYPHEF-----------SGGQRQRIGIARAL 172
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1149123047  616 VRNPKILLLDEATSALDTESEA-VVQVALD-KARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKGNHDELMKE 688
Cdd:COG4608    173 ALNPKLIVCDEPVSALDVSIQAqVLNLLEDlQDELGLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDELYAR 248
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
462-689 1.88e-36

ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213223 [Multi-domain]  Cd Length: 241  Bit Score: 138.47  E-value: 1.88e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSRKevKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREI-- 539
Cdd:cd03256      1 IEVENLSKTYPNGK--KALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLrr 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  540 -IGVVSQEPVLFA-TTIAENIRYGR-----------ENVTMDEIEKAVKEANAYDFimklphkfDTLVGERGAQLSGGQK 606
Cdd:cd03256     79 qIGMIFQQFNLIErLSVLENVLSGRlgrrstwrslfGLFPKEEKQRALAALERVGL--------LDKAYQRADQLSGGQQ 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  607 QRIAIARALVRNPKILLLDEATSALDTE-SEAVVQVALDKAR-KGRTTIVIAHRLSTVR-NADVIAGFDDGVIVEKGNHD 683
Cdd:cd03256    151 QRVAIARALMQQPKLILADEPVASLDPAsSRQVMDLLKRINReEGITVIVSLHQVDLAReYADRIVGLKDGRIVFDGPPA 230

                   ....*.
gi 1149123047  684 ELMKEK 689
Cdd:cd03256    231 ELTDEV 236
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
1105-1320 6.41e-36

ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.


Pssm-ID: 213217 [Multi-domain]  Cd Length: 204  Bit Score: 135.67  E-value: 6.41e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1105 VTFGEVVFNYPTRPDI--PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL--ErfYDPLAGKVLLDGKeikrlnvqwlr 1180
Cdd:cd03250      1 ISVEDASFTWDSGEQEtsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALlgE--LEKLSGSVSVPGS----------- 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1181 ahLGIVSQEPILFDCSIAENIAYG---DNSRVvsqEEIVRAAkeanihAF---IESLPNKYSTKVGDKGTQLSGGQKQRI 1254
Cdd:cd03250     68 --IAYVSQEPWIQNGTIRENILFGkpfDEERY---EKVIKAC------ALepdLEILPDGDLTEIGEKGINLSGGQKQRI 136
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1149123047 1255 AIARALVRQPHILLLDEATSALDTES-----EKVVQEALdkaREGRTCIVIAHRLSTIQNADLIVVFQNGR 1320
Cdd:cd03250    137 SLARAVYSDADIYLLDDPLSAVDAHVgrhifENCILGLL---LNNKTRILVTHQLQLLPHADQIVVLDNGR 204
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
1110-1332 1.23e-35

ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213228 [Multi-domain]  Cd Length: 235  Bit Score: 135.71  E-value: 1.23e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1110 VVFNYPTRPdipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNV---QWLRAHLGIV 1186
Cdd:cd03261      6 LTKSFGGRT---VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEaelYRLRRRMGML 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1187 SQEPILFDC-SIAENIAYG--DNSRvVSQEEIVRAAKE----ANIHAFIESLPnkystkvgdkgTQLSGGQKQRIAIARA 1259
Cdd:cd03261     83 FQSGALFDSlTVFENVAFPlrEHTR-LSEEEIREIVLEkleaVGLRGAEDLYP-----------AELSGGMKKRVALARA 150
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1149123047 1260 LVRQPHILLLDEATSALD-TESEKVVQEALD-KAREGRTCIVIAHRLSTI-QNADLIVVFQNGRVKEHGTHQQLLA 1332
Cdd:cd03261    151 LALDPELLLYDEPTAGLDpIASGVIDDLIRSlKKELGLTSIMVTHDLDTAfAIADRIAVLYDGKIVAEGTPEELRA 226
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
1122-1331 1.25e-35

ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213266 [Multi-domain]  Cd Length: 235  Bit Score: 135.93  E-value: 1.25e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1122 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQwlRAHLGIVSQEPILF-DCSIAEN 1200
Cdd:cd03299     14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFpHMTVYKN 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1201 IAYGDNSRVVSQEEIVRAAKEANIHAFIESLPNKystkvgdKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTES 1280
Cdd:cd03299     92 IAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNR-------KPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRT 164
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1149123047 1281 EKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLL 1331
Cdd:cd03299    165 KEKLREELKKIRKefGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVF 218
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
1127-1333 1.36e-35

ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213261 [Multi-domain]  Cd Length: 269  Bit Score: 137.00  E-value: 1.36e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1127 SLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRA----HLGIVSQEPILF-DCSIAENI 1201
Cdd:cd03294     44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkKISMVFQSFALLpHRTVLENV 123
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1202 AYGDNSRVVSQEEIVRAAKEA----NIHAFIESLPNkystkvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEATSALD 1277
Cdd:cd03294    124 AFGLEVQGVPRAEREERAAEAlelvGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1149123047 1278 TESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVFQNGRVKEHGTHQQLLAQ 1333
Cdd:cd03294    193 PLIRREMQDELLRlqAELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILTN 251
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
1119-1330 1.45e-35

ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213267 [Multi-domain]  Cd Length: 232  Bit Score: 135.44  E-value: 1.45e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1119 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIkrLNVQWLRAHLGIVSQEPILF-DCSI 1197
Cdd:cd03300     12 GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--TNLPPHKRPVNTVFQNYALFpHLTV 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1198 AENIAYGDNSRVVSQEEIVRAAKEANIHAFIESLPNKYSTkvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEATSALD 1277
Cdd:cd03300     90 FENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPS-------QLSGGQQQRVAIARALVNEPKVLLLDEPLGALD 162
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1149123047 1278 TESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVFQNGRVKEHGTHQQL 1330
Cdd:cd03300    163 LKLRKDMQLELKRlqKELGITFVFVTHDQEeALTMSDRIAVMNKGKIQQIGTPEEI 218
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
1119-1335 1.60e-35

ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];


Pssm-ID: 443618 [Multi-domain]  Cd Length: 243  Bit Score: 135.76  E-value: 1.60e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1119 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNvQWLRAHLGIVSQEPILFD-CSI 1197
Cdd:COG4555     13 KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEP-REARRQIGVLPDERGLYDrLTV 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1198 AENIAYGDNSRVVSQEEIVRAAKEAnIHAFIesLPNKYSTKVGDkgtqLSGGQKQRIAIARALVRQPHILLLDEATSALD 1277
Cdd:COG4555     92 RENIRYFAELYGLFDEELKKRIEEL-IELLG--LEEFLDRRVGE----LSTGMKKKVALARALVHDPKVLLLDEPTNGLD 164
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1278 TESEKVVQEALDKAREGRTCIVIA-HRLSTIQN-ADLIVVFQNGRVKEHGTHQQLLAQKG 1335
Cdd:COG4555    165 VMARRLLREILRALKKEGKTVLFSsHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
1110-1321 1.87e-35

ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.


Pssm-ID: 213222 [Multi-domain]  Cd Length: 218  Bit Score: 134.54  E-value: 1.87e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1110 VVFNYPTRPD-IPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWL----RAHLG 1184
Cdd:cd03255      6 LSKTYGGGGEkVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafrRRHIG 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1185 IVSQE----PILfdcSIAENIAYGDNSRVVSQEEIVRAAKEAnihafIES--LPNKYSTKVGdkgtQLSGGQKQRIAIAR 1258
Cdd:cd03255     86 FVFQSfnllPDL---TALENVELPLLLAGVPKKERRERAEEL-----LERvgLGDRLNHYPS----ELSGGQQQRVAIAR 153
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1149123047 1259 ALVRQPHILLLDEATSALDTESEKVVQEAL-DKAREGRTCIVIA-HRLSTIQNADLIVVFQNGRV 1321
Cdd:cd03255    154 ALANDPKIILADEPTGNLDSETGKEVMELLrELNKEAGTTIVVVtHDPELAEYADRIIELRDGKI 218
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
1110-1333 2.00e-35

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 136.68  E-value: 2.00e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1110 VVFNYPTRPDiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQE 1189
Cdd:PRK13635    11 ISFRYPDAAT-YALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGMVFQN 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1190 PilfD-----CSIAENIAYGDNSRVVSQEEIVR----AAKEANIHAFIESLPNKystkvgdkgtqLSGGQKQRIAIARAL 1260
Cdd:PRK13635    90 P---DnqfvgATVQDDVAFGLENIGVPREEMVErvdqALRQVGMEDFLNREPHR-----------LSGGQKQRVAIAGVL 155
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1149123047 1261 VRQPHILLLDEATSALDTESEkvvQEALD-----KAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQ 1333
Cdd:PRK13635   156 ALQPDIIILDEATSMLDPRGR---REVLEtvrqlKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKS 230
PLN03130 PLN03130
ABC transporter C family member; Provisional
187-736 2.35e-35

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 147.58  E-value: 2.35e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  187 YYSGIGAGVlvaAYIQV------SFW----CLAAGRQIHKirkQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGI 256
Cdd:PLN03130   954 FYNLIYALL---SFGQVlvtllnSYWlimsSLYAAKRLHD---AMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNV 1027
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  257 GDKIGMF----FQSMATFFtgfIVGFTRgwklTLVILAISPVLGL---------SAAVWAKILSSFTDKELlaYAKAGav 323
Cdd:PLN03130  1028 AVFVNMFlgqiFQLLSTFV---LIGIVS----TISLWAIMPLLVLfygaylyyqSTAREVKRLDSITRSPV--YAQFG-- 1096
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  324 aeEVLAAIRTVIAFGGQKKELERYNKNLEEAKRIGIkkaitANIS-----------IGAAFLLIYASYAL---------- 382
Cdd:PLN03130  1097 --EALNGLSTIRAYKAYDRMAEINGRSMDNNIRFTL-----VNMSsnrwlairletLGGLMIWLTASFAVmqngraenqa 1169
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  383 AFWYGTTLVLSGEYSIGQVLTvffSVLIGAFSVGQASPSIEAFANARGAAYEIFKIIDNKPSIDSYSKSGhkpdnikgNL 462
Cdd:PLN03130  1170 AFASTMGLLLSYALNITSLLT---AVLRLASLAENSLNAVERVGTYIDLPSEAPLVIENNRPPPGWPSSG--------SI 1238
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  463 EFRNVHFSYpsRKEVK-ILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIG 541
Cdd:PLN03130  1239 KFEDVVLRY--RPELPpVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLG 1316
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  542 VVSQEPVLFATTIAENIRYGRENVTMDEIEkAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKI 621
Cdd:PLN03130  1317 IIPQAPVLFSGTVRFNLDPFNEHNDADLWE-SLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKI 1395
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  622 LLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDEL-MKEKGIYFKLVTMQT 700
Cdd:PLN03130  1396 LVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLlSNEGSAFSKMVQSTG 1475
                          570       580       590
                   ....*....|....*....|....*....|....*.
gi 1149123047  701 AGNEVELENAADESKSEidalEMSSNDSRSSLIRKR 736
Cdd:PLN03130  1476 AANAQYLRSLVFGGDED----RLAREESKALDGQRK 1507
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
484-686 3.75e-35

ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213261 [Multi-domain]  Cd Length: 269  Bit Score: 135.46  E-value: 3.75e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  484 NLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREI----IGVVSQEPVLFA-TTIAENI 558
Cdd:cd03294     44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELrrkkISMVFQSFALLPhRTVLENV 123
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  559 RYGRENVTMDEIEKAVKEANAY------DFIMKLPHkfdtlvgergaQLSGGQKQRIAIARALVRNPKILLLDEATSALD 632
Cdd:cd03294    124 AFGLEVQGVPRAEREERAAEALelvgleGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1149123047  633 TESEAVVQVALDK--ARKGRTTIVIAHRLS-TVRNADVIAGFDDGVIVEKGNHDELM 686
Cdd:cd03294    193 PLIRREMQDELLRlqAELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEIL 249
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
462-686 5.21e-35

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 134.06  E-value: 5.21e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNV--HFSypsrkEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIR--TINVRFLR 537
Cdd:PRK09493     2 IEFKNVskHFG-----PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIR 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  538 EIIGVVSQEPVLFATTIA-ENIRYGRENVtmdeieKAVKEANAYDFIMKLPHKfdtlVG--ERG----AQLSGGQKQRIA 610
Cdd:PRK09493    77 QEAGMVFQQFYLFPHLTAlENVMFGPLRV------RGASKEEAEKQARELLAK----VGlaERAhhypSELSGGQQQRVA 146
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1149123047  611 IARALVRNPKILLLDEATSALDTE-SEAVVQVALDKARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKGNHDELM 686
Cdd:PRK09493   147 IARALAVKPKLMLFDEPTSALDPElRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLI 224
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
1119-1321 6.15e-35

ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.


Pssm-ID: 213229 [Multi-domain]  Cd Length: 213  Bit Score: 133.04  E-value: 6.15e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1119 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEI--KRLNVQWLRAHLGIVSQEPILF-DC 1195
Cdd:cd03262     12 DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKVGMVFQQFNLFpHL 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1196 SIAENIAYGD-NSRVVSQEEIVRAAKEanihafieslpnkYSTKVG--DKGT----QLSGGQKQRIAIARALVRQPHILL 1268
Cdd:cd03262     92 TVLENITLAPiKVKGMSKAEAEERALE-------------LLEKVGlaDKADaypaQLSGGQQQRVAIARALAMNPKVML 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1149123047 1269 LDEATSALDTEsekVVQEALDK----AREGRTCIVIAHRLSTIQN-ADLIVVFQNGRV 1321
Cdd:cd03262    159 FDEPTSALDPE---LVGEVLDVmkdlAEEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
462-656 8.05e-35

Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages


Pssm-ID: 213259 [Multi-domain]  Cd Length: 214  Bit Score: 132.92  E-value: 8.05e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSrkEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDI---RTINVRFLRE 538
Cdd:cd03292      1 IEFINVTKTYPN--GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsdlRGRAIPYLRR 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  539 IIGVVSQEPVLFAT-TIAENIRYGRE--NVTMDEIEKAVKEANAydfIMKLPHKFDTLvgerGAQLSGGQKQRIAIARAL 615
Cdd:cd03292     79 KIGVVFQDFRLLPDrNVYENVAFALEvtGVPPREIRKRVPAALE---LVGLSHKHRAL----PAELSGGEQQRVAIARAI 151
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1149123047  616 VRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIA 656
Cdd:cd03292    152 VNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVA 192
ABC_6TM_ABCB10_like cd18573
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ...
797-1065 1.19e-34

Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.


Pssm-ID: 350017 [Multi-domain]  Cd Length: 294  Bit Score: 134.95  E-value: 1.19e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  797 AFAIIFSKIIGVFT-RIDDPETKRQNSNLFSLLFLALGIISFITFFLQGFTFGKAGEILTKRLRYMVFRSMLRQDVSWFD 875
Cdd:cd18573     14 SVPFAIGKLIDVASkESGDIEIFGLSLKTFALALLGVFVVGAAANFGRVYLLRIAGERIVARLRKRLFKSILRQDAAFFD 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  876 dpKNTTGALTTRLANDAAQVKGAIGSRLAVITQNIANLGTGIIISFIYGWQLTLLLLAIVPIIAIAGVVEMKMLSGQALK 955
Cdd:cd18573     94 --KNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRYVRKLSKQ 171
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  956 DKKELEGSGKIATEAIENFRTVVSLTQEQKFEHMYAQSLQVPYRNSLRKAHIFGITFSFTQAMMYFSYAGCFRFGAYLVA 1035
Cdd:cd18573    172 VQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLLSVLYYGGSLVA 251
                          250       260       270
                   ....*....|....*....|....*....|
gi 1149123047 1036 HklmsfedvllvfsavvfGAMAVGQVSSFA 1065
Cdd:cd18573    252 S-----------------GELTVGDLTSFL 264
ABC_6TM_bac_exporter_ABCB8_10_like cd18576
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ...
217-432 2.27e-34

Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.


Pssm-ID: 350020 [Multi-domain]  Cd Length: 289  Bit Score: 133.76  E-value: 2.27e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  217 IRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQSMATFFTGFIVGFTRGWKLTLVILAISPVLG 296
Cdd:cd18576     71 LRKDLYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVV 150
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  297 LSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKRIGIKKAITANISIGAAFLLI 376
Cdd:cd18576    151 LVAVLFGRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLL 230
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1149123047  377 YASYALAFWYGTTLVLSGEYSIGQVLT-VFFSVLIGAfSVGQASPSIEAFANARGAA 432
Cdd:cd18576    231 FGAIVAVLWYGGRLVLAGELTAGDLVAfLLYTLFIAG-SIGSLADLYGQLQKALGAS 286
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
1116-1333 3.13e-34

ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 135.27  E-value: 3.13e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1116 TRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQL---LERfydPLAGKVLLDGKEIK-RLNVQwlRAHLGIVSQEPI 1191
Cdd:COG1118     11 RFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIiagLET---PDSGRIVLNGRDLFtNLPPR--ERRVGFVFQHYA 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1192 LF-DCSIAENIAYGDNSRVVSQEEIVRAAKEaNIHAF-IESLPNKYSTkvgdkgtQLSGGQKQRIAIARALVRQPHILLL 1269
Cdd:COG1118     86 LFpHMTVAENIAFGLRVRPPSKAEIRARVEE-LLELVqLEGLADRYPS-------QLSGGQRQRVALARALAVEPEVLLL 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1149123047 1270 DEATSALDT----ESEKVVQEALDkaREGRTCIVIAH------RLstiqnADLIVVFQNGRVKEHGTHQQLLAQ 1333
Cdd:COG1118    158 DEPFGALDAkvrkELRRWLRRLHD--ELGGTTVFVTHdqeealEL-----ADRVVVMNQGRIEQVGTPDEVYDR 224
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
462-686 3.16e-34

ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 443332 [Multi-domain]  Cd Length: 533  Bit Score: 139.43  E-value: 3.16e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSRK--------EVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLyDPTEGMVSVDGQDIRTIN- 532
Cdd:COG4172    276 LEARDLKVWFPIKRglfrrtvgHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLSr 354
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  533 --VRFLREIIGVVSQEPvlFAT-----TIAENIRYG----RENVTMDEIEKAVKEA-----------NAYdfimklPHKF 590
Cdd:COG4172    355 raLRPLRRRMQVVFQDP--FGSlsprmTVGQIIAEGlrvhGPGLSAAERRARVAEAleevgldpaarHRY------PHEF 426
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  591 dtlvgergaqlSGGQKQRIAIARALVRNPKILLLDEATSALDteseAVVQ---VALDK---ARKGRTTIVIAHRLSTVRN 664
Cdd:COG4172    427 -----------SGGQRQRIAIARALILEPKLLVLDEPTSALD----VSVQaqiLDLLRdlqREHGLAYLFISHDLAVVRA 491
                          250       260
                   ....*....|....*....|...
gi 1149123047  665 -ADVIAGFDDGVIVEKGNHDELM 686
Cdd:COG4172    492 lAHRVMVMKDGKVVEQGPTEQVF 514
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
462-685 8.53e-34

ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 134.12  E-value: 8.53e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRT-INVRFLReiI 540
Cdd:COG1118      3 IEVRNISKRFGSFT---LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTnLPPRERR--V 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  541 GVVSQEPVLFA-TTIAENIRYG--RENVTMDEIEKAVKE----------ANAYdfimklPHkfdtlvgergaQLSGGQKQ 607
Cdd:COG1118     78 GFVFQHYALFPhMTVAENIAFGlrVRPPSKAEIRARVEEllelvqleglADRY------PS-----------QLSGGQRQ 140
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  608 RIAIARALVRNPKILLLDEATSALDTeseavvqvaldKARK-------------GRTTIVIAH-RLSTVRNADVIAGFDD 673
Cdd:COG1118    141 RVALARALAVEPEVLLLDEPFGALDA-----------KVRKelrrwlrrlhdelGGTTVFVTHdQEEALELADRVVVMNQ 209
                          250
                   ....*....|..
gi 1149123047  674 GVIVEKGNHDEL 685
Cdd:COG1118    210 GRIEQVGTPDEV 221
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
462-685 9.78e-34

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 131.74  E-value: 9.78e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSRKEVkiLKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFL--REI 539
Cdd:PRK13639     2 LETRDLKYSYPDGTEA--LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLevRKT 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  540 IGVVSQEP--VLFATTIAENIRYGRENV--TMDEIEKAVKEA----NAYDFIMKLPHkfdtlvgergaQLSGGQKQRIAI 611
Cdd:PRK13639    80 VGIVFQNPddQLFAPTVEEDVAFGPLNLglSKEEVEKRVKEAlkavGMEGFENKPPH-----------HLSGGQKKRVAI 148
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1149123047  612 ARALVRNPKILLLDEATSALDTE-SEAVVQVALDKARKGRTTIVIAHRLSTV-RNADVIAGFDDGVIVEKGNHDEL 685
Cdd:PRK13639   149 AGILAMKPEIIVLDEPTSGLDPMgASQIMKLLYDLNKEGITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEV 224
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
462-688 1.28e-33

ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 130.21  E-value: 1.28e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRflreiIG 541
Cdd:COG1121      7 IELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRR-----IG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  542 VVSQEPVL---FATTIAENI---RYGRENVTM-------DEIEKAVKEANAYDFImklphkfDTLVGErgaqLSGGQKQR 608
Cdd:COG1121     79 YVPQRAEVdwdFPITVRDVVlmgRYGRRGLFRrpsradrEAVDEALERVGLEDLA-------DRPIGE----LSGGQQQR 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  609 IAIARALVRNPKILLLDEATSALDTESEAVVQVALDK-ARKGRTTIVIAHRLSTVR-NADVIAGFDDGVIVEkGNHDELM 686
Cdd:COG1121    148 VLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVReYFDRVLLLNRGLVAH-GPPEEVL 226

                   ..
gi 1149123047  687 KE 688
Cdd:COG1121    227 TP 228
ABC_6TM_AtABCB27_like cd18780
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ...
784-1071 1.48e-33

Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.


Pssm-ID: 350053 [Multi-domain]  Cd Length: 295  Bit Score: 131.60  E-value: 1.48e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  784 GVFCAIINGGLQPAFAIIFSKIIGVFTRIDDPETKRQNSNLFSLLFLALGIISF--ITFFLQGFTFGKAGEILTKRLRYM 861
Cdd:cd18780      1 GTIALLVSSGTNLALPYFFGQVIDAVTNHSGSGGEEALRALNQAVLILLGVVLIgsIATFLRSWLFTLAGERVVARLRKR 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  862 VFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIGSRLAVITQNIANLGTGIIISFIYGWQLTLLLLAIVPIIAIA 941
Cdd:cd18780     81 LFSAIIAQEIAFFD--VTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIG 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  942 GVVEMKMLSGQALKDKKELEGSGKIATEAIENFRTVVSLTQEQKFEHMYAQSLQVPYRNSLRKAHIFGITFSFTQAMMYF 1021
Cdd:cd18780    159 AVIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQL 238
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1149123047 1022 SYAGCFRFGAYLVAHK------LMSFedVLLVFSAvvfgAMAVGQVSSFAPDYAKA 1071
Cdd:cd18780    239 AIVLVLWYGGRLVIDGelttglLTSF--LLYTLTV----AMSFAFLSSLYGDFMQA 288
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
1105-1325 1.54e-33

Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 129.40  E-value: 1.54e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1105 VTFGEVVFNYPtrPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLN---VQWLRA 1181
Cdd:COG2884      2 IRFENVSKRYP--GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrreIPYLRR 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1182 HLGIVSQE-PILFDCSIAENIAY-----GdnsrvVSQEEIVRAAKEA----NIHAFIESLPNkystkvgdkgtQLSGGQK 1251
Cdd:COG2884     80 RIGVVFQDfRLLPDRTVYENVALplrvtG-----KSRKEIRRRVREVldlvGLSDKAKALPH-----------ELSGGEQ 143
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1149123047 1252 QRIAIARALVRQPHILLLDEATSALDTE-SEKVVqEALDKAREGRTCIVIA-HRLSTIQNADL-IVVFQNGRVKEHG 1325
Cdd:COG2884    144 QRVAIARALVNRPELLLADEPTGNLDPEtSWEIM-ELLEEINRRGTTVLIAtHDLELVDRMPKrVLELEDGRLVRDE 219
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
462-687 5.01e-33

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 129.75  E-value: 5.01e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSRKEVKiLKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIG 541
Cdd:PRK13635     6 IRVEHISFRYPDAATYA-LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVG 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  542 VVSQEP--VLFATTIAENIRYGREN--VTMDE----IEKAVKEANAYDFIMKLPHKfdtlvgergaqLSGGQKQRIAIAR 613
Cdd:PRK13635    85 MVFQNPdnQFVGATVQDDVAFGLENigVPREEmverVDQALRQVGMEDFLNREPHR-----------LSGGQKQRVAIAG 153
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1149123047  614 ALVRNPKILLLDEATSALDTE--SEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELMK 687
Cdd:PRK13635   154 VLALQPDIIILDEATSMLDPRgrREVLETVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFK 229
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
463-680 5.25e-33

ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.


Pssm-ID: 213181 [Multi-domain]  Cd Length: 180  Bit Score: 126.40  E-value: 5.25e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  463 EFRNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIGV 542
Cdd:cd03214      1 EVENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAY 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  543 VSQepvlfattiaenirygrenvtmdeiekAVKEANAYDFIMKLphkFDTlvgergaqLSGGQKQRIAIARALVRNPKIL 622
Cdd:cd03214     78 VPQ---------------------------ALELLGLAHLADRP---FNE--------LSGGERQRVLLARALAQEPPIL 119
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1149123047  623 LLDEATSALDTESeavvQVALDK------ARKGRTTIVIAHRLS-TVRNADVIAGFDDGVIVEKG 680
Cdd:cd03214    120 LLDEPTSHLDIAH----QIELLEllrrlaRERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
480-687 5.86e-33

ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213266 [Multi-domain]  Cd Length: 235  Bit Score: 128.22  E-value: 5.86e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  480 LKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRflREIIGVVSQEPVLFA-TTIAENI 558
Cdd:cd03299     15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFPhMTVYKNI 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  559 RYGRENVTMD--EIEKAVKEANAydfIMKLPHkfdtLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESE 636
Cdd:cd03299     93 AYGLKKRKVDkkEIERKVLEIAE---MLGIDH----LLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTK 165
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1149123047  637 AVVQVALDKARK--GRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKGNHDELMK 687
Cdd:cd03299    166 EKLREELKKIRKefGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFK 219
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
466-657 5.89e-33

Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.


Pssm-ID: 213193 [Multi-domain]  Cd Length: 205  Bit Score: 126.99  E-value: 5.89e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  466 NVHFSYpsRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIrtiNVRFLREIIGVVSQ 545
Cdd:cd03226      4 NISFSY--KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI---KAKERRKSIGYVMQ 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  546 EP--VLFATTIAENIRYGRENVTMD--EIEKAVKEANAYDFIMKLPHkfdtlvgergaQLSGGQKQRIAIARALVRNPKI 621
Cdd:cd03226     79 DVdyQLFTDSVREELLLGLKELDAGneQAETVLKDLDLYALKERHPL-----------SLSGGQKQRLAIAAALLSGKDL 147
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1149123047  622 LLLDEATSALDTES-EAVVQVALDKARKGRTTIVIAH 657
Cdd:cd03226    148 LIFDEPTSGLDYKNmERVGELIRELAAQGKAVIVITH 184
ABCC_SUR2 cd03288
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...
479-696 7.19e-33

ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.


Pssm-ID: 213255 [Multi-domain]  Cd Length: 257  Bit Score: 128.49  E-value: 7.19e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  479 ILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIGVVSQEPVLFATTIAENI 558
Cdd:cd03288     36 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL 115
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  559 RYGREnVTMDEIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAV 638
Cdd:cd03288    116 DPECK-CTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENI 194
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1149123047  639 VQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELM-KEKGIYFKLV 696
Cdd:cd03288    195 LQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLaQEDGVFASLV 253
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
1119-1326 7.38e-33

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 131.99  E-value: 7.38e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1119 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQwlRAHLGIVSQEPILF-DCSI 1197
Cdd:PRK09452    26 GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVNTVFQSYALFpHMTV 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1198 AENIAYGDNSRVVSQEEIVRAAKEANIHAFIESLPNKystkvgdKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALD 1277
Cdd:PRK09452   104 FENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQR-------KPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALD 176
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1149123047 1278 TESEKVVQEALdKA--RE-GRTCIVIAH-RLSTIQNADLIVVFQNGRVKEHGT 1326
Cdd:PRK09452   177 YKLRKQMQNEL-KAlqRKlGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGT 228
PhnC COG3638
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ...
1121-1321 1.05e-32

ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 442855 [Multi-domain]  Cd Length: 249  Bit Score: 127.87  E-value: 1.05e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1121 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLN---VQWLRAHLGIVSQEPILFD-CS 1196
Cdd:COG3638     17 PALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRgraLRRLRRRIGMIFQQFNLVPrLS 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1197 IAENI---AYGDNS------RVVSQEEIVRAakeaniHAFIES--LPNKYSTKVGdkgtQLSGGQKQRIAIARALVRQPH 1265
Cdd:COG3638     97 VLTNVlagRLGRTStwrsllGLFPPEDRERA------LEALERvgLADKAYQRAD----QLSGGQQQRVAIARALVQEPK 166
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1149123047 1266 ILLLDEATSALDTESEKVVQEAL-DKARE-GRTCIVIAHRLSTIQN-ADLIVVFQNGRV 1321
Cdd:COG3638    167 LILADEPVASLDPKTARQVMDLLrRIAREdGITVVVNLHQVDLARRyADRIIGLRDGRV 225
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
1119-1330 2.11e-32

ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 129.81  E-value: 2.11e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1119 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQwlRAHLGIVSQEPILFD-CSI 1197
Cdd:COG3839     15 GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPK--DRNIAMVFQSYALYPhMTV 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1198 AENIAYGDNSRVVSQEEIVRAAKEA----NIHAFIESLPnkystkvgdkgTQLSGGQKQRIAIARALVRQPHILLLDEAT 1273
Cdd:COG3839     93 YENIAFPLKLRKVPKAEIDRRVREAaellGLEDLLDRKP-----------KQLSGGQRQRVALGRALVREPKVFLLDEPL 161
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1149123047 1274 SALD------TESE-KVVQEALdkareGRTCIVIAHRLS---TIqnADLIVVFQNGRVKEHGTHQQL 1330
Cdd:COG3839    162 SNLDaklrveMRAEiKRLHRRL-----GTTTIYVTHDQVeamTL--ADRIAVMNDGRIQQVGTPEEL 221
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
1114-1333 2.13e-32

ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];


Pssm-ID: 440213 [Multi-domain]  Cd Length: 320  Bit Score: 129.02  E-value: 2.13e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1114 YPTRP-DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLA---GKVLLDGKEIKRLNVQWLRA----HLGI 1185
Cdd:COG0444     11 FPTRRgVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGitsGEILFDGEDLLKLSEKELRKirgrEIQM 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1186 VSQEP---------ILFdcSIAENI-AYGDNSRVVSQEEIVRAAKEANIH---AFIESLPNkystkvgdkgtQLSGGQKQ 1252
Cdd:COG0444     91 IFQDPmtslnpvmtVGD--QIAEPLrIHGGLSKAEARERAIELLERVGLPdpeRRLDRYPH-----------ELSGGMRQ 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1253 RIAIARALVRQPHILLLDEATSALDTesekVVQ-EALD-----KAREGRTCIVIAHRLSTI-QNADLIVVFQNGRVKEHG 1325
Cdd:COG0444    158 RVMIARALALEPKLLIADEPTTALDV----TIQaQILNllkdlQRELGLAILFITHDLGVVaEIADRVAVMYAGRIVEEG 233

                   ....*...
gi 1149123047 1326 THQQLLAQ 1333
Cdd:COG0444    234 PVEELFEN 241
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
462-688 3.11e-32

ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213267 [Multi-domain]  Cd Length: 232  Bit Score: 125.81  E-value: 3.11e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSrkeVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIrtINVRFLREIIG 541
Cdd:cd03300      1 IELENVSKFYGG---FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--TNLPPHKRPVN 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  542 VVSQEPVLFA-TTIAENIRYG--RENVTMDEIEKAVKEAnaydfiMKLPhKFDTLVGERGAQLSGGQKQRIAIARALVRN 618
Cdd:cd03300     76 TVFQNYALFPhLTVFENIAFGlrLKKLPKAEIKERVAEA------LDLV-QLEGYANRKPSQLSGGQQQRVAIARALVNE 148
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1149123047  619 PKILLLDEATSALDTESEAVVQVALDKARK--GRTTIVIAHRLS---TVrnADVIAGFDDGVIVEKGNHDELMKE 688
Cdd:cd03300    149 PKVLLLDEPLGALDLKLRKDMQLELKRLQKelGITFVFVTHDQEealTM--SDRIAVMNKGKIQQIGTPEEIYEE 221
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
462-685 3.78e-32

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 126.43  E-value: 3.78e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSRKEvkiLKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYD-----PTEGMVSVDGQDI---RTINV 533
Cdd:PRK14239     6 LQVSDLSVYYNKKKA---LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIyspRTDTV 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  534 RfLREIIGVVSQEPVLFATTIAENIRYG------RENVTMDE-IEKAVKEANAYDFIMKLPHkfDTLVGergaqLSGGQK 606
Cdd:PRK14239    83 D-LRKEIGMVFQQPNPFPMSIYENVVYGlrlkgiKDKQVLDEaVEKSLKGASIWDEVKDRLH--DSALG-----LSGGQQ 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  607 QRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTV-RNADVIAGFDDGVIVEKGNHDEL 685
Cdd:PRK14239   155 QRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQAsRISDRTGFFLDGDLIEYNDTKQM 234
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
1110-1321 5.52e-32

ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213197 [Multi-domain]  Cd Length: 173  Bit Score: 122.89  E-value: 5.52e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1110 VVFNYPTRPdipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQwLRAHLGIVSQE 1189
Cdd:cd03230      6 LSKRYGKKT---ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEE-VKRRIGYLPEE 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1190 PILF-DCSIAENIaygdnsrvvsqeeivraakeanihafieslpnkystkvgdkgtQLSGGQKQRIAIARALVRQPHILL 1268
Cdd:cd03230     82 PSLYeNLTVRENL-------------------------------------------KLSGGMKQRLALAQALLHDPELLI 118
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1149123047 1269 LDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVFQNGRV 1321
Cdd:cd03230    119 LDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
462-680 6.32e-32

The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.


Pssm-ID: 213268 [Multi-domain]  Cd Length: 213  Bit Score: 124.29  E-value: 6.32e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPsrkEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRtiNVRFLREIIG 541
Cdd:cd03301      1 VELENVTKRFG---NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVT--DLPPKDRDIA 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  542 VVSQEPVLFA-TTIAENIRYG--RENVTMDEIEKAVKEANAydfIMKLPHkfdtLVGERGAQLSGGQKQRIAIARALVRN 618
Cdd:cd03301     76 MVFQNYALYPhMTVYDNIAFGlkLRKVPKDEIDERVREVAE---LLQIEH----LLDRKPKQLSGGQRQRVALGRAIVRE 148
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1149123047  619 PKILLLDEATSALDTESEAVVQVALDK--ARKGRTTIVIAH-RLSTVRNADVIAGFDDGVIVEKG 680
Cdd:cd03301    149 PKVFLMDEPLSNLDAKLRVQMRAELKRlqQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
1116-1315 1.33e-31

ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443308 [Multi-domain]  Cd Length: 206  Bit Score: 123.36  E-value: 1.33e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1116 TRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWlRAHLGIVSQEPILF-D 1194
Cdd:COG4133     11 RRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDY-RRRLAYLGHADGLKpE 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1195 CSIAENIA-----YGdnsRVVSQEEIVRAAKEANIHAFIEslpnkysTKVGdkgtQLSGGQKQRIAIARALVRQPHILLL 1269
Cdd:COG4133     90 LTVRENLRfwaalYG---LRADREAIDEALEAVGLAGLAD-------LPVR----QLSAGQKRRVALARLLLSPAPLWLL 155
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1149123047 1270 DEATSALDTESEKVVQEALDKAREGRTCIVIA-HRLSTIQNADLIVV 1315
Cdd:COG4133    156 DEPFTALDAAGVALLAELIAAHLARGGAVLLTtHQPLELAAARVLDL 202
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
1104-1333 1.69e-31

ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 124.05  E-value: 1.69e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1104 NVTFGevvfnYPTRPdipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLnvqwlRAHL 1183
Cdd:COG1121     11 NLTVS-----YGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-----RRRI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1184 GIVSQE-------PIlfdcSIAENIAYGDNSRV-----VSQE--EIVRAA-KEANIHAFIeslpnkySTKVGdkgtQLSG 1248
Cdd:COG1121     78 GYVPQRaevdwdfPI----TVRDVVLMGRYGRRglfrrPSRAdrEAVDEAlERVGLEDLA-------DRPIG----ELSG 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1249 GQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTI-QNADLIVVFqNGRVKEHGT 1326
Cdd:COG1121    143 GQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVrEYFDRVLLL-NRGLVAHGP 221

                   ....*..
gi 1149123047 1327 HQQLLAQ 1333
Cdd:COG1121    222 PEEVLTP 228
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
1116-1333 1.91e-31

ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 443332 [Multi-domain]  Cd Length: 533  Bit Score: 130.96  E-value: 1.91e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1116 TRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFyDPLAGKVLLDGKEIKRLN---VQWLRAHLGIVSQEPil 1192
Cdd:COG4172    295 TVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDP-- 371
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1193 FDC-----SIAENIAYGdnsRVVSQEEIVRAAKEANIhafIESLpnkysTKVG-DKGT------QLSGGQKQRIAIARAL 1260
Cdd:COG4172    372 FGSlsprmTVGQIIAEG---LRVHGPGLSAAERRARV---AEAL-----EEVGlDPAArhryphEFSGGQRQRIAIARAL 440
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1261 VRQPHILLLDEATSALDteseKVVQ-EALD-----KAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLLAQ 1333
Cdd:COG4172    441 ILEPKLLVLDEPTSALD----VSVQaQILDllrdlQREHGLAYLFISHDLAVVRAlAHRVMVMKDGKVVEQGPTEQVFDA 516
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
462-668 2.16e-31

ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443308 [Multi-domain]  Cd Length: 206  Bit Score: 122.59  E-value: 2.16e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFlREIIG 541
Cdd:COG4133      3 LEAENLSCRRGERL---LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDY-RRRLA 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  542 VVSQEPVLFAT-TIAENIR-----YGREnVTMDEIEKAVKEanaydfiMKLPHKFDTLVGergaQLSGGQKQRIAIARAL 615
Cdd:COG4133     79 YLGHADGLKPElTVRENLRfwaalYGLR-ADREAIDEALEA-------VGLAGLADLPVR----QLSAGQKRRVALARLL 146
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1149123047  616 VRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIA-HRLSTVRNADVI 668
Cdd:COG4133    147 LSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTtHQPLELAAARVL 200
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
1104-1325 2.36e-31

ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.


Pssm-ID: 213181 [Multi-domain]  Cd Length: 180  Bit Score: 121.39  E-value: 2.36e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1104 NVTFGevvfnYPTRPdipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHL 1183
Cdd:cd03214      4 NLSVG-----YGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKI 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1184 GIVSQepilfdcsiaeniaygdnsrvvsqeeivrAAKEANIHAFIeslpnkystkvgDKG-TQLSGGQKQRIAIARALVR 1262
Cdd:cd03214     76 AYVPQ-----------------------------ALELLGLAHLA------------DRPfNELSGGERQRVLLARALAQ 114
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1149123047 1263 QPHILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVFQNGRVKEHG 1325
Cdd:cd03214    115 EPPILLLDEPTSHLDIAHQIELLELLRRlaRERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
cbiO PRK13637
energy-coupling factor transporter ATPase;
476-688 2.71e-31

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 124.77  E-value: 2.71e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  476 EVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDI--RTINVRFLREIIGVVSQEP--VLFA 551
Cdd:PRK13637    19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIRKKVGLVFQYPeyQLFE 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  552 TTIAENIRYGRENVTM--DEIEKAVKEANAydfIMKLPhkFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATS 629
Cdd:PRK13637    99 ETIEKDIAFGPINLGLseEEIENRVKRAMN---IVGLD--YEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTA 173
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1149123047  630 ALD--TESEAVVQVALDKARKGRTTIVIAHRLSTV-RNADVIAGFDDGVIVEKGNHDELMKE 688
Cdd:PRK13637   174 GLDpkGRDEILNKIKELHKEYNMTIILVSHSMEDVaKLADRIIVMNKGKCELQGTPREVFKE 235
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
1119-1332 3.62e-31

ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.


Pssm-ID: 213191 [Multi-domain]  Cd Length: 222  Bit Score: 122.54  E-value: 3.62e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1119 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQwLRAHLGI--VSQEPILF-DC 1195
Cdd:cd03224     12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPH-ERARAGIgyVPEGRRIFpEL 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1196 SIAENIAYGDNSRVvsqeeivRAAKEANIHAFIESLPNKYsTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSA 1275
Cdd:cd03224     91 TVEENLLLGAYARR-------RAKRKARLERVYELFPRLK-ERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEG 162
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1149123047 1276 LdteSEKVVQE---ALDKAREGRTCIVIAHrlstiQNADLI-------VVFQNGRVKEHGTHQQLLA 1332
Cdd:cd03224    163 L---APKIVEEifeAIRELRDEGVTILLVE-----QNARFAleiadraYVLERGRVVLEGTAAELLA 221
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
462-678 4.96e-31

Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 443338 [Multi-domain]  Cd Length: 233  Bit Score: 122.54  E-value: 4.96e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSR-KEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTIN----VRFL 536
Cdd:COG4181      9 IELRGLTKTVGTGaGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDedarARLR 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  537 REIIGVVSQEPVLFATTIAEnirygrENVTM--------DEIEKAVKEANAYDfimklphkfdtlVGERG----AQLSGG 604
Cdd:COG4181     89 ARHVGFVFQSFQLLPTLTAL------ENVMLplelagrrDARARARALLERVG------------LGHRLdhypAQLSGG 150
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1149123047  605 QKQRIAIARALVRNPKILLLDEATSALDTE-SEAVVQVALDKARKGRTTIVIA-HRLSTVRNADVIAGFDDGVIVE 678
Cdd:COG4181    151 EQQRVALARAFATEPAILFADEPTGNLDAAtGEQIIDLLFELNRERGTTLVLVtHDPALAARCDRVLRLRAGRLVE 226
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
1123-1330 6.01e-31

ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 443658 [Multi-domain]  Cd Length: 329  Bit Score: 125.23  E-value: 6.01e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1123 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLN---VQWLRAHLGIVSQEPilFDC---- 1195
Cdd:COG4608     34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSgreLRPLRRRMQMVFQDP--YASlnpr 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1196 -SIAENIAYG-DNSRVVSqeeivRAAKEANIHAFIES--LP----NKYStkvgdkgTQLSGGQKQRIAIARALVRQPHIL 1267
Cdd:COG4608    112 mTVGDIIAEPlRIHGLAS-----KAERRERVAELLELvgLRpehaDRYP-------HEFSGGQRQRIGIARALALNPKLI 179
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1149123047 1268 LLDEATSALDtesekV-VQ-------EALdKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQL 1330
Cdd:COG4608    180 VCDEPVSALD-----VsIQaqvlnllEDL-QDELGLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDEL 245
cbiO PRK13650
energy-coupling factor transporter ATPase;
1110-1333 7.58e-31

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 123.30  E-value: 7.58e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1110 VVFNYPTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQE 1189
Cdd:PRK13650    10 LTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMVFQN 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1190 P--ILFDCSIAENIAYGDNSRVVSQEEIVRAAKEA----NIHAFIESLPnkystkvgdkgTQLSGGQKQRIAIARALVRQ 1263
Cdd:PRK13650    90 PdnQFVGATVEDDVAFGLENKGIPHEEMKERVNEAlelvGMQDFKEREP-----------ARLSGGQKQRVAIAGAVAMR 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1149123047 1264 PHILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQ 1333
Cdd:PRK13650   159 PKIIILDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSR 230
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
1118-1321 1.05e-30

ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 128.21  E-value: 1.05e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1118 PDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNV-QWLRAHLGIVSQEPILF-DC 1195
Cdd:COG1129     15 GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPrDAQAAGIAIIHQELNLVpNL 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1196 SIAENIAYGD---NSRVVSQEEIVRAAKEAnihafIESL-----PNkysTKVGDkgtqLSGGQKQRIAIARALVRQPHIL 1267
Cdd:COG1129     95 SVAENIFLGReprRGGLIDWRAMRRRAREL-----LARLgldidPD---TPVGD----LSVAQQQLVEIARALSRDARVL 162
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1149123047 1268 LLDEATSAL-DTESE---KVVQEaLdkAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRV 1321
Cdd:COG1129    163 ILDEPTASLtEREVErlfRIIRR-L--KAQGVAIIYISHRLDEVFEiADRVTVLRDGRL 218
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
462-632 1.06e-30

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 125.44  E-value: 1.06e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDI-------RTINVR 534
Cdd:PRK09452    15 VELRGISKSFDGKE---VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIthvpaenRHVNTV 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  535 FlreiigvvsQEPVLFA-TTIAENIRYG--RENVTMDEIEKAVKEAnaydfiMKLPHkFDTLVGERGAQLSGGQKQRIAI 611
Cdd:PRK09452    92 F---------QSYALFPhMTVFENVAFGlrMQKTPAAEITPRVMEA------LRMVQ-LEEFAQRKPHQLSGGQQQRVAI 155
                          170       180
                   ....*....|....*....|.
gi 1149123047  612 ARALVRNPKILLLDEATSALD 632
Cdd:PRK09452   156 ARAVVNKPKVLLLDESLSALD 176
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
463-665 1.71e-30

ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.


Pssm-ID: 213202 [Multi-domain]  Cd Length: 213  Bit Score: 120.33  E-value: 1.71e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  463 EFRNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRflreiIGV 542
Cdd:cd03235      1 EVEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR-----IGY 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  543 VSQEPVL---FATTIAENIRYGREN----------VTMDEIEKAVKEANAYDFImklphkfDTLVGErgaqLSGGQKQRI 609
Cdd:cd03235     73 VPQRRSIdrdFPISVRDVVLMGLYGhkglfrrlskADKAKVDEALERVGLSELA-------DRQIGE----LSGGQQQRV 141
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1149123047  610 AIARALVRNPKILLLDEATSALDTESEAVVQVALDK-ARKGRTTIVIAHRLSTVRNA 665
Cdd:cd03235    142 LLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEY 198
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
462-685 1.82e-30

ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 127.44  E-value: 1.82e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSrkeVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREI-I 540
Cdd:COG1129      5 LEMRGISKSFGG---VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAgI 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  541 GVVSQEPVLFAT-TIAENIRYGRENVT---MD--EIEKAVKEANAYdfiMKLPHKFDTLVGErgaqLSGGQKQRIAIARA 614
Cdd:COG1129     82 AIIHQELNLVPNlSVAENIFLGREPRRgglIDwrAMRRRARELLAR---LGLDIDPDTPVGD----LSVAQQQLVEIARA 154
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1149123047  615 LVRNPKILLLDEATSAL-DTESEAVVQVALDKARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKGNHDEL 685
Cdd:COG1129    155 LSRDARVLILDEPTASLtEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEiADRVTVLRDGRLVGTGPVAEL 227
ABC_6TM_TAP cd18572
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ...
827-1040 1.91e-30

Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.


Pssm-ID: 350016 [Multi-domain]  Cd Length: 289  Bit Score: 122.65  E-value: 1.91e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  827 LLFLALGIISFITFFLQGFTFGKAGEILTKRLRYMVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIGSRLAVI 906
Cdd:cd18572     40 LLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFD--ATKTGELTSRLTSDCQKVSDPLSTNLNVF 117
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  907 TQNIANLGTGIIISFIYGWQLTLLLLAIVPIIAIAGVVE---MKMLSGQAlkdKKELEGSGKIATEAIENFRTVVSLTQE 983
Cdd:cd18572    118 LRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYgryYRKLSKEI---QDALAEANQVAEEALSNIRTVRSFATE 194
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1149123047  984 QKFEHMYAQSLQVPYRNSLRKAHIFGITFSFTQAMMYFSYAGCFRFGAYLVAHKLMS 1040
Cdd:cd18572    195 EREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFYGGHLVLSGRMS 251
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
462-697 2.06e-30

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 121.68  E-value: 2.06e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYD-----PTEGMVSVDGQDI--RTINVR 534
Cdd:PRK14258     8 IKVNNLSFYYDTQK---ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElesevRVEGRVEFFNQNIyeRRVNLN 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  535 FLREIIGVVSQEPVLFATTIAENIRYG------RENVTMDEI-EKAVKEANAYDFIMKLPHKfdtlvgeRGAQLSGGQKQ 607
Cdd:PRK14258    85 RLRRQVSMVHPKPNLFPMSVYDNVAYGvkivgwRPKLEIDDIvESALKDADLWDEIKHKIHK-------SALDLSGGQQQ 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  608 RIAIARALVRNPKILLLDEATSALDTESEAVVQ--VALDKARKGRTTIVIAHRLSTV-RNADVIAGFddgviveKGNHDE 684
Cdd:PRK14258   158 RLCIARALAVKPKVLLMDEPCFGLDPIASMKVEslIQSLRLRSELTMVIVSHNLHQVsRLSDFTAFF-------KGNENR 230
                          250
                   ....*....|....*
gi 1149123047  685 L--MKEKGIYFKLVT 697
Cdd:PRK14258   231 IgqLVEFGLTKKIFN 245
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
462-688 2.12e-30

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 122.12  E-value: 2.12e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSRKEVK---ILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTI-NVRFLR 537
Cdd:PRK13633     5 IKCKNVSYKYESNEESTeklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEeNLWDIR 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  538 EIIGVVSQEP--VLFATTIAENIRYGREN--VTMDEIEKAVKEA----NAYDFIMKLPHkfdtlvgergaQLSGGQKQRI 609
Cdd:PRK13633    85 NKAGMVFQNPdnQIVATIVEEDVAFGPENlgIPPEEIRERVDESlkkvGMYEYRRHAPH-----------LLSGGQKQRV 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  610 AIARALVRNPKILLLDEATSALDTESEAVVQVALDKARK--GRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELMK 687
Cdd:PRK13633   154 AIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKkyGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFK 233

                   .
gi 1149123047  688 E 688
Cdd:PRK13633   234 E 234
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
462-677 2.38e-30

First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.


Pssm-ID: 213183 [Multi-domain]  Cd Length: 163  Bit Score: 117.91  E-value: 2.38e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSrkeVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREI-I 540
Cdd:cd03216      1 LELRGITKRFGG---VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAgI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  541 GVVSQepvlfattiaenirygrenvtmdeiekavkeanaydfimklphkfdtlvgergaqLSGGQKQRIAIARALVRNPK 620
Cdd:cd03216     78 AMVYQ-------------------------------------------------------LSVGERQMVEIARALARNAR 102
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1149123047  621 ILLLDEATSAL-DTESEAVVQVALDKARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIV 677
Cdd:cd03216    103 LLILDEPTAALtPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
1121-1325 2.61e-30

ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.


Pssm-ID: 213202 [Multi-domain]  Cd Length: 213  Bit Score: 119.56  E-value: 2.61e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1121 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLnvqwlRAHLGIVSQEPIL---FDCSI 1197
Cdd:cd03235     13 PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGYVPQRRSIdrdFPISV 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1198 AENIAYGDNSRVVSQEEIVRAAKEANIHAFieslpnkysTKVGDKG------TQLSGGQKQRIAIARALVRQPHILLLDE 1271
Cdd:cd03235     88 RDVVLMGLYGHKGLFRRLSKADKAKVDEAL---------ERVGLSEladrqiGELSGGQQQRVLLARALVQDPDLLLLDE 158
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1149123047 1272 ATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVFqNGRVKEHG 1325
Cdd:cd03235    159 PFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEyFDRVLLL-NRTVVASG 213
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
462-688 2.63e-30

ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.


Pssm-ID: 213191 [Multi-domain]  Cd Length: 222  Bit Score: 119.85  E-value: 2.63e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYpsrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINV-RFLREII 540
Cdd:cd03224      1 LEVENLNAGY---GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPhERARAGI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  541 GVVSQEPVLFAT-TIAENIRYGRENVTMDEIEKAVKEAnaYDFIMKLPHKFDTLVGergaQLSGGQKQRIAIARALVRNP 619
Cdd:cd03224     78 GYVPEGRRIFPElTVEENLLLGAYARRRAKRKARLERV--YELFPRLKERRKQLAG----TLSGGEQQMLAIARALMSRP 151
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1149123047  620 KILLLDEATSALdteSEAVVQV---ALDKARKGRTTIVI----AHRLSTVrnADVIAGFDDGVIVEKGNHDELMKE 688
Cdd:cd03224    152 KLLLLDEPSEGL---APKIVEEifeAIRELRDEGVTILLveqnARFALEI--ADRAYVLERGRVVLEGTAAELLAD 222
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
1121-1321 4.87e-30

ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213223 [Multi-domain]  Cd Length: 241  Bit Score: 119.98  E-value: 4.87e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1121 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEI---KRLNVQWLRAHLGIVSQEPILFD-CS 1196
Cdd:cd03256     15 KALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDInklKGKALRQLRRQIGMIFQQFNLIErLS 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1197 IAENIAYGDNSRV---------VSQEEIVRAakeanIHAFIES-LPNKYSTKVGdkgtQLSGGQKQRIAIARALVRQPHI 1266
Cdd:cd03256     95 VLENVLSGRLGRRstwrslfglFPKEEKQRA-----LAALERVgLLDKAYQRAD----QLSGGQQQRVAIARALMQQPKL 165
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1149123047 1267 LLLDEATSALDTESEKVVQEAL-DKARE-GRTCIVIAHRLSTI-QNADLIVVFQNGRV 1321
Cdd:cd03256    166 ILADEPVASLDPASSRQVMDLLkRINREeGITVIVSLHQVDLArEYADRIVGLKDGRI 223
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
1105-1301 4.89e-30

Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages


Pssm-ID: 213259 [Multi-domain]  Cd Length: 214  Bit Score: 119.05  E-value: 4.89e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1105 VTFGEVVFNYPtrPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLN---VQWLRA 1181
Cdd:cd03292      1 IEFINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraIPYLRR 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1182 HLGIVSQE-PILFDCSIAENIAYGDNSRVVSQEEIVRAAKEA----NIHAFIESLPNkystkvgdkgtQLSGGQKQRIAI 1256
Cdd:cd03292     79 KIGVVFQDfRLLPDRNVYENVAFALEVTGVPPREIRKRVPAAlelvGLSHKHRALPA-----------ELSGGEQQRVAI 147
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1149123047 1257 ARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIA 1301
Cdd:cd03292    148 ARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVA 192
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
1118-1330 6.27e-30

ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213263 [Multi-domain]  Cd Length: 239  Bit Score: 119.37  E-value: 6.27e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1118 PDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQwlRAHLGIVSQEPILF-DCS 1196
Cdd:cd03296     13 GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVGFVFQHYALFrHMT 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1197 IAENIAYG----DNSRVVSQEEIVRAAKEANIHAFIESLPNKYSTkvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEA 1272
Cdd:cd03296     91 VFDNVAFGlrvkPRSERPPEAEIRAKVHELLKLVQLDWLADRYPA-------QLSGGQRQRVALARALAVEPKVLLLDEP 163
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1149123047 1273 TSALDTESEKVVQEALDKARE--GRTCIVIAHRLS-TIQNADLIVVFQNGRVKEHGTHQQL 1330
Cdd:cd03296    164 FGALDAKVRKELRRWLRRLHDelHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPDEV 224
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
1123-1321 6.86e-30

ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213264 [Multi-domain]  Cd Length: 214  Bit Score: 118.55  E-value: 6.86e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1123 LQGLSLEVK---KGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEI----KRLNVQWLRAHLGIVSQEPILF-D 1194
Cdd:cd03297     10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdsrKKINLPPQQRKIGLVFQQYALFpH 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1195 CSIAENIAYGdnSRVVSQEEIVRAAKEANIHAFIESLPNKYSTkvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEATS 1274
Cdd:cd03297     90 LNVRENLAFG--LKRKRNREDRISVDELLDLLGLDHLLNRYPA-------QLSGGEKQRVALARALAAQPELLLLDEPFS 160
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1275 ALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVFQNGRV 1321
Cdd:cd03297    161 ALDRALRLQLLPELKQikKNLNIPVIFVTHDLSEAEYlADRIVVMEDGRL 210
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
1110-1322 8.91e-30

Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.


Pssm-ID: 213193 [Multi-domain]  Cd Length: 205  Bit Score: 117.74  E-value: 8.91e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1110 VVFNYPTRPDIpvLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRlnvQWLRAHLGIVSQE 1189
Cdd:cd03226      5 ISFSYKKGTEI--LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA---KERRKSIGYVMQD 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1190 P--ILFDCSIAENIAYGDNSRVVSQEEIVRAAKEANIHAFIESLPnkystkvgdkgTQLSGGQKQRIAIARALVRQPHIL 1267
Cdd:cd03226     80 VdyQLFTDSVREELLLGLKELDAGNEQAETVLKDLDLYALKERHP-----------LSLSGGQKQRLAIAAALLSGKDLL 148
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1149123047 1268 LLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVK 1322
Cdd:cd03226    149 IFDEPTSGLDYKNMERVGELIRElAAQGKAVIVITHDYEFLAKvCDRVLLLANGAIV 205
cbiO PRK13650
energy-coupling factor transporter ATPase;
462-666 1.03e-29

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 120.22  E-value: 1.03e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIG 541
Cdd:PRK13650     5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  542 VVSQEP--VLFATTIAENIRYGREN--VTMDEIEKAVKEA----NAYDFIMKLPhkfdtlvgergAQLSGGQKQRIAIAR 613
Cdd:PRK13650    85 MVFQNPdnQFVGATVEDDVAFGLENkgIPHEEMKERVNEAlelvGMQDFKEREP-----------ARLSGGQKQRVAIAG 153
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1149123047  614 ALVRNPKILLLDEATSALDTES--EAVVQVALDKARKGRTTIVIAHRLSTVRNAD 666
Cdd:PRK13650   154 AVAMRPKIIILDEATSMLDPEGrlELIKTIKGIRDDYQMTVISITHDLDEVALSD 208
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
1123-1333 1.20e-29

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 119.50  E-value: 1.20e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1123 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLA-----GKVLLDGKEI--KRLNVQWLRAHLGIVSQEPILFDC 1195
Cdd:PRK14243    26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPgfrveGKVTFHGKNLyaPDVDPVEVRRRIGMVFQKPNPFPK 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1196 SIAENIAYGD--NSRVVSQEEIV-RAAKEAnihafieSLPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEA 1272
Cdd:PRK14243   106 SIYDNIAYGAriNGYKGDMDELVeRSLRQA-------ALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEP 178
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1149123047 1273 TSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQ 1333
Cdd:PRK14243   179 CSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFNVELTEGGGRYGYLVE 239
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
456-697 1.29e-29

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 119.84  E-value: 1.29e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  456 DNIkgnLEFRNVHFSYpsRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRF 535
Cdd:PRK13647     2 DNI---IEVEDLHFRY--KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKW 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  536 LREIIGVVSQEP--VLFATTIAENIRYGREN--VTMDEIEKAVKEA----NAYDFIMKLPHkfdtlvgergaQLSGGQKQ 607
Cdd:PRK13647    77 VRSKVGLVFQDPddQVFSSTVWDDVAFGPVNmgLDKDEVERRVEEAlkavRMWDFRDKPPY-----------HLSYGQKK 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  608 RIAIARALVRNPKILLLDEATSALDTESEAVVQVALDK-ARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKG----- 680
Cdd:PRK13647   146 RVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRlHNQGKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGdksll 225
                          250
                   ....*....|....*..
gi 1149123047  681 NHDELMKEKGIYFKLVT 697
Cdd:PRK13647   226 TDEDIVEQAGLRLPLVA 242
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
478-680 1.68e-29

ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213264 [Multi-domain]  Cd Length: 214  Bit Score: 117.40  E-value: 1.68e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  478 KILKGLNLKVQ---SGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQ---DIR-TINVRFLREIIGVVSQEPVLF 550
Cdd:cd03297      8 KRLPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfDSRkKINLPPQQRKIGLVFQQYALF 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  551 A-TTIAENIRYGRENVTMDEIEKAVKEANAYdfiMKLPHkfdtLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATS 629
Cdd:cd03297     88 PhLNVRENLAFGLKRKRNREDRISVDELLDL---LGLDH----LLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFS 160
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1149123047  630 ALDTESEAVVQVALDKARK--GRTTIVIAHRLSTV-RNADVIAGFDDGVIVEKG 680
Cdd:cd03297    161 ALDRALRLQLLPELKQIKKnlNIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
1123-1342 1.87e-29

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 119.07  E-value: 1.87e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1123 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEP--ILFDCSIAEN 1200
Cdd:PRK13647    21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQDPddQVFSSTVWDD 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1201 IAYGDNSRVVSQEEIVRAAKEA----NIHAFIESLPNkystkvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEATSAL 1276
Cdd:PRK13647   101 VAFGPVNMGLDKDEVERRVEEAlkavRMWDFRDKPPY-----------HLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYL 169
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1149123047 1277 DTESEKVVQEALDK-AREGRTCIVIAHRLS-TIQNADLIVVFQNGRVKEHG-----THQQLLAQKGIYFSMVS 1342
Cdd:PRK13647   170 DPRGQETLMEILDRlHNQGKTVIVATHDVDlAAEWADQVIVLKEGRVLAEGdksllTDEDIVEQAGLRLPLVA 242
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
1105-1326 1.96e-29

ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).


Pssm-ID: 213186 [Multi-domain]  Cd Length: 236  Bit Score: 117.92  E-value: 1.96e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1105 VTFGEVVfnyptrpdipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQwLRAHLG 1184
Cdd:cd03219      8 KRFGGLV----------ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPH-EIARLG 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1185 IVS--QEPILF-DCSIAENI----------AYGDNSRVVSQEEIVRAAKEanIHAFIEsLPNKYSTKVGDkgtqLSGGQK 1251
Cdd:cd03219     77 IGRtfQIPRLFpELTVLENVmvaaqartgsGLLLARARREEREARERAEE--LLERVG-LADLADRPAGE----LSYGQQ 149
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1149123047 1252 QRIAIARALVRQPHILLLDEATSAL-DTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGT 1326
Cdd:cd03219    150 RRLEIARALATDPKLLLLDEPAAGLnPEETEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGT 226
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
1118-1321 2.47e-29

First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.


Pssm-ID: 213183 [Multi-domain]  Cd Length: 163  Bit Score: 115.22  E-value: 2.47e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1118 PDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVqwlrahlgivsqepilfdcsi 1197
Cdd:cd03216     11 GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASP--------------------- 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1198 aeniaygdnsrvvsqeeivRAAKEANIhAFIeslpnkystkvgdkgTQLSGGQKQRIAIARALVRQPHILLLDEATSAL- 1276
Cdd:cd03216     70 -------------------RDARRAGI-AMV---------------YQLSVGERQMVEIARALARNARLLILDEPTAALt 114
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1149123047 1277 DTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRV 1321
Cdd:cd03216    115 PAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEiADRVTVLRDGRV 160
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
1092-1350 2.73e-29

multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]


Pssm-ID: 188098 [Multi-domain]  Cd Length: 1522  Bit Score: 127.37  E-value: 2.73e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1092 STEGLMPNTLE--------GN-VTFGEVVFNYpTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAG 1162
Cdd:TIGR00957  615 SHEELEPDSIErrtikpgeGNsITVHNATFTW-ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEG 693
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1163 KVLLDGKeikrlnvqwlrahLGIVSQEPILFDCSIAENIAYGDNSrvvsQEEIVRAAKEA-NIHAFIESLPNKYSTKVGD 1241
Cdd:TIGR00957  694 HVHMKGS-------------VAYVPQQAWIQNDSLRENILFGKAL----NEKYYQQVLEAcALLPDLEILPSGDRTEIGE 756
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1242 KGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEAL---DKAREGRTCIVIAHRLSTIQNADLIVVFQN 1318
Cdd:TIGR00957  757 KGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVigpEGVLKNKTRILVTHGISYLPQVDVIIVMSG 836
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1149123047 1319 GRVKEHGTHQQLLAQKGIYFSMVSVQAGTKRQ 1350
Cdd:TIGR00957  837 GKISEMGSYQELLQRDGAFAEFLRTYAPDEQQ 868
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
1127-1333 4.80e-29

ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 116.78  E-value: 4.80e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1127 SLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQwLRAhLGIVSQEPILFD-CSIAENIAYGD 1205
Cdd:COG3840     19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPA-ERP-VSMLFQENNLFPhLTVAQNIGLGL 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1206 NSR----VVSQEEIVRAAKEANIHAFIESLPNkystkvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEATSALD---- 1277
Cdd:COG3840     97 RPGlkltAEQRAQVEQALERVGLAGLLDRLPG-----------QLSGGQRQRVALARCLVRKRPILLLDEPFSALDpalr 165
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1149123047 1278 TESEKVVQEALDkaREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLLAQ 1333
Cdd:COG3840    166 QEMLDLVDELCR--ERGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDG 220
cbiO PRK13642
energy-coupling factor transporter ATPase;
462-685 6.31e-29

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 117.89  E-value: 6.31e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIG 541
Cdd:PRK13642     5 LEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  542 VVSQEP--VLFATTIAENIRYGREN--VTMDEIEKAVKEA----NAYDFIMKLPhkfdtlvgergAQLSGGQKQRIAIAR 613
Cdd:PRK13642    85 MVFQNPdnQFVGATVEDDVAFGMENqgIPREEMIKRVDEAllavNMLDFKTREP-----------ARLSGGQKQRVAVAG 153
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1149123047  614 ALVRNPKILLLDEATSALDT--ESEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDEL 685
Cdd:PRK13642   154 IIALRPEIIILDESTSMLDPtgRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSEL 227
cbiO PRK13640
energy-coupling factor transporter ATPase;
456-696 6.91e-29

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 117.98  E-value: 6.91e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  456 DNIkgnLEFRNVHFSYPSRKEvKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDP---TEGMVSVDGQDIRTIN 532
Cdd:PRK13640     3 DNI---VEFKHVSFTYPDSKK-PALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKT 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  533 VRFLREIIGVVSQEP--VLFATTIAENIRYGREN--VTMDEIEKAVKEANA----YDFIMKLPhkfdtlvgergAQLSGG 604
Cdd:PRK13640    79 VWDIREKVGIVFQNPdnQFVGATVGDDVAFGLENraVPRPEMIKIVRDVLAdvgmLDYIDSEP-----------ANLSGG 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  605 QKQRIAIARALVRNPKILLLDEATSALDTES-EAVVQVALD-KARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKG-- 680
Cdd:PRK13640   148 QKQRVAIAGILAVEPKIIILDESTSMLDPAGkEQILKLIRKlKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGsp 227
                          250       260
                   ....*....|....*....|
gi 1149123047  681 ----NHDELMKEKGIYFKLV 696
Cdd:PRK13640   228 veifSKVEMLKEIGLDIPFV 247
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
1116-1279 7.89e-29

ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 115.27  E-value: 7.89e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1116 TRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDP---LAGKVLLDGKEIKRLNVQwlRAHLGIVSQEPIL 1192
Cdd:COG4136     10 TLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAE--QRRIGILFQDDLL 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1193 FD-CSIAENIAYG---DNSRVVSQEEIVRAAKEANIHAFIESLPNkystkvgdkgtQLSGGQKQRIAIARALVRQPHILL 1268
Cdd:COG4136     88 FPhLSVGENLAFAlppTIGRAQRRARVEQALEEAGLAGFADRDPA-----------TLSGGQRARVALLRALLAEPRALL 156
                          170
                   ....*....|.
gi 1149123047 1269 LDEATSALDTE 1279
Cdd:COG4136    157 LDEPFSKLDAA 167
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
456-687 1.15e-28

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 116.77  E-value: 1.15e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  456 DNIkgnLEFRNVHFSYPSrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRF 535
Cdd:PRK13648     5 NSI---IVFKNVSFQYQS-DASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEK 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  536 LREIIGVVSQEP--VLFATTIAENIRYGREN--VTMDEIEKAVKEA----NAYDFIMKLPHkfdtlvgergaQLSGGQKQ 607
Cdd:PRK13648    81 LRKHIGIVFQNPdnQFVGSIVKYDVAFGLENhaVPYDEMHRRVSEAlkqvDMLERADYEPN-----------ALSGGQKQ 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  608 RIAIARALVRNPKILLLDEATSALDTE--SEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDEL 685
Cdd:PRK13648   150 RVAIAGVLALNPSVIILDEATSMLDPDarQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229

                   ..
gi 1149123047  686 MK 687
Cdd:PRK13648   230 FD 231
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
462-689 1.18e-28

ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];


Pssm-ID: 440736 [Multi-domain]  Cd Length: 250  Bit Score: 115.95  E-value: 1.18e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGM-VSVDGQDIRTINVRFLREII 540
Cdd:COG1119      4 LELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGEDVWELRKRI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  541 GVVS---------QEPVL-------FATTiaeniryGR-ENVTMDEIEKAVKEANAydfiMKLPHKFDTLVGergaQLSG 603
Cdd:COG1119     81 GLVSpalqlrfprDETVLdvvlsgfFDSI-------GLyREPTDEQRERARELLEL----LGLAHLADRPFG----TLSQ 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  604 GQKQRIAIARALVRNPKILLLDEATSALDTES-EAVVQVaLDK-ARKGRTTIV-IAHRLStvrnaDVIAGFD------DG 674
Cdd:COG1119    146 GEQRRVLIARALVKDPELLILDEPTAGLDLGArELLLAL-LDKlAAEGAPTLVlVTHHVE-----EIPPGIThvlllkDG 219
                          250
                   ....*....|....*
gi 1149123047  675 VIVEKGNHDELMKEK 689
Cdd:COG1119    220 RVVAAGPKEEVLTSE 234
nickel_nikE TIGR02769
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ...
462-678 1.22e-28

nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 131816 [Multi-domain]  Cd Length: 265  Bit Score: 116.44  E-value: 1.22e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPS------RKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTIN--- 532
Cdd:TIGR02769    3 LEVRDVTHTYRTgglfgaKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDrkq 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  533 -VRFLREIIGVVSQEPVLF--ATTIAENIRYGRENVT-MDEIEKAVKEANAYDfIMKLPhkfDTLVGERGAQLSGGQKQR 608
Cdd:TIGR02769   83 rRAFRRDVQLVFQDSPSAVnpRMTVRQIIGEPLRHLTsLDESEQKARIAELLD-MVGLR---SEDADKLPRQLSGGQLQR 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1149123047  609 IAIARALVRNPKILLLDEATSALDTESEAVVQVALDK--ARKGRTTIVIAHRLSTV-RNADVIAGFDDGVIVE 678
Cdd:TIGR02769  159 INIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKlqQAFGTAYLFITHDLRLVqSFCQRVAVMDKGQIVE 231
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
462-687 1.60e-28

ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).


Pssm-ID: 213186 [Multi-domain]  Cd Length: 236  Bit Score: 115.23  E-value: 1.60e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYpsrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRflrEI-- 539
Cdd:cd03219      1 LEVRGLTKRF---GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPH---EIar 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  540 --IGVVSQEPVLFAT-TIAENIRYG-----RENVTMDEIEKAVKEANAYDF----IMKLPHKFDTLVGErgaqLSGGQKQ 607
Cdd:cd03219     75 lgIGRTFQIPRLFPElTVLENVMVAaqartGSGLLLARARREEREARERAEelleRVGLADLADRPAGE----LSYGQQR 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  608 RIAIARALVRNPKILLLDEATSAL-DTESEAVVQVALDKARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKGNHDEL 685
Cdd:cd03219    151 RLEIARALATDPKLLLLDEPAAGLnPEETEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEV 230

                   ..
gi 1149123047  686 MK 687
Cdd:cd03219    231 RN 232
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
1118-1325 1.67e-28

The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.


Pssm-ID: 213268 [Multi-domain]  Cd Length: 213  Bit Score: 114.66  E-value: 1.67e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1118 PDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKrlNVQWLRAHLGIVSQEPILF-DCS 1196
Cdd:cd03301     11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVT--DLPPKDRDIAMVFQNYALYpHMT 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1197 IAENIAYGDNSRVVSQEEIVRAAKEANIHAFIESLPNKYSTkvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEATSAL 1276
Cdd:cd03301     89 VYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPK-------QLSGGQRQRVALGRAIVREPKVFLMDEPLSNL 161
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1149123047 1277 DTESEKVVQEALDK--AREGRTCIVIAH-RLSTIQNADLIVVFQNGRVKEHG 1325
Cdd:cd03301    162 DAKLRVQMRAELKRlqQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
479-685 3.62e-28

putative amino-acid ABC transporter ATP-binding protein YecC; Provisional


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 114.85  E-value: 3.62e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  479 ILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDI---RTIN-----VRFLREIIGVVSQEPVLF 550
Cdd:PRK11264    18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtaRSLSqqkglIRQLRQHVGFVFQNFNLF 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  551 A-TTIAENIRYGreNVTMDEIEKAVKEANAYDFIMKLphkfdTLVGERGA---QLSGGQKQRIAIARALVRNPKILLLDE 626
Cdd:PRK11264    98 PhRTVLENIIEG--PVIVKGEPKEEATARARELLAKV-----GLAGKETSyprRLSGGQQQRVAIARALAMRPEVILFDE 170
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1149123047  627 ATSALDTESEAVVQVALDK-ARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKGNHDEL 685
Cdd:PRK11264   171 PTSALDPELVGEVLNTIRQlAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKAL 231
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
1117-1326 5.75e-28

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 116.82  E-value: 5.75e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1117 RPDIPVLQGLSLEVKKGQTLALVGSSGCGKST---VVQLLERfydPLAGKVLLDGKEIKRLNVQWLRA---HLGIVSQE- 1189
Cdd:PRK11153    15 GRTIHALNNVSLHIPAGEIFGVIGASGAGKSTlirCINLLER---PTSGRVLVDGQDLTALSEKELRKarrQIGMIFQHf 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1190 PILFDCSIAENIAY-----GdnsrvVSQEEIvraakEANIHAFIEslpnkystKVG--DKG----TQLSGGQKQRIAIAR 1258
Cdd:PRK11153    92 NLLSSRTVFDNVALplelaG-----TPKAEI-----KARVTELLE--------LVGlsDKAdrypAQLSGGQKQRVAIAR 153
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1149123047 1259 ALVRQPHILLLDEATSALDTESEKVVQEALDKA-RE-GRTCIVIAHRLSTI-QNADLIVVFQNGRVKEHGT 1326
Cdd:PRK11153   154 ALASNPKVLLCDEATSALDPATTRSILELLKDInRElGLTIVLITHEMDVVkRICDRVAVIDAGRLVEQGT 224
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
462-681 6.75e-28

Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.


Pssm-ID: 213180 [Multi-domain]  Cd Length: 194  Bit Score: 112.26  E-value: 6.75e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHF---SYPSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQL--MQRLYDPTEGMVSVDGQDIRTINvrfL 536
Cdd:cd03213      4 LSFRNLTVtvkSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNAlaGRRTGLGVSGEVLINGRPLDKRS---F 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  537 REIIGVVSQEPVLFAT-TIAENIrygrenvtmdeiekavkeanayDFIMKLphkfdtlvgeRGaqLSGGQKQRIAIARAL 615
Cdd:cd03213     81 RKIIGYVPQDDILHPTlTVRETL----------------------MFAAKL----------RG--LSGGERKRVSIALEL 126
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1149123047  616 VRNPKILLLDEATSALDTESEAVVQVALDK-ARKGRTTIVIAHRLSTvrnaDVIAGFDDGVIVEKGN 681
Cdd:cd03213    127 VSNPSLLFLDEPTSGLDSSSALQVMSLLRRlADTGRTIICSIHQPSS----EIFELFDKLLLLSQGR 189
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
1119-1331 6.88e-28

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 113.65  E-value: 6.88e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1119 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIK--RLNVQWLRAHLGIVSQEPILFDCS 1196
Cdd:PRK09493    13 PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQEAGMVFQQFYLFPHL 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1197 IA-ENIAYGDNSrvvsqeeiVRAAKEANIHAFIESLPNK--YSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEAT 1273
Cdd:PRK09493    93 TAlENVMFGPLR--------VRGASKEEAEKQARELLAKvgLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPT 164
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1274 SALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVF-QNGRVKEHGTHQQLL 1331
Cdd:PRK09493   165 SALDPElRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFiDKGRIAEDGDPQVLI 224
ABC_6TM_bac_exporter_ABCB8_10_like cd18576
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ...
784-1057 8.46e-28

Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.


Pssm-ID: 350020 [Multi-domain]  Cd Length: 289  Bit Score: 114.89  E-value: 8.46e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  784 GVFCAIINGGLQPAFAIIFSKIIGVFTRIDDPETKRQNSNLFSLLFLALGIISFItfflQGFTFGKAGEILTKRLRYMVF 863
Cdd:cd18576      1 GLILLLLSSAIGLVFPLLAGQLIDAALGGGDTASLNQIALLLLGLFLLQAVFSFF----RIYLFARVGERVVADLRKDLY 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  864 RSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIGSRLAVITQNIANLGTGIIISFIYGWQLTLLLLAIVPIIAIAGV 943
Cdd:cd18576     77 RHLQRLPLSFFH--ERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAV 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  944 V---EMKMLSGQALkdkKELEGSGKIATEAIENFRTVVSLTQEQKFEHMYAQSLQVPYRNSLRKAHIFGITFSFTQAMMY 1020
Cdd:cd18576    155 LfgrRIRKLSKKVQ---DELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLF 231
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1149123047 1021 FSYAGCFRFGAYLVAHKLMSFEDV--LLVFSAVVFGAMA 1057
Cdd:cd18576    232 GAIVAVLWYGGRLVLAGELTAGDLvaFLLYTLFIAGSIG 270
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
462-657 9.53e-28

ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.


Pssm-ID: 213230 [Multi-domain]  Cd Length: 220  Bit Score: 112.60  E-value: 9.53e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTiNVRFLREIIG 541
Cdd:cd03263      1 LQIRNLTKTYKK-GTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  542 VVSQEPVLFAT-TIAENIRY-----GRENVTMDEiekavkEANAYDFIMKLPHKFDTLVGergaQLSGGQKQRIAIARAL 615
Cdd:cd03263     79 YCPQFDALFDElTVREHLRFyarlkGLPKSEIKE------EVELLLRVLGLTDKANKRAR----TLSGGMKRKLSLAIAL 148
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1149123047  616 VRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAH 657
Cdd:cd03263    149 IGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTH 190
ABC_6TM_bac_exporter_ABCB8_10_like cd18575
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ...
170-432 9.94e-28

Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.


Pssm-ID: 350019 [Multi-domain]  Cd Length: 289  Bit Score: 114.50  E-value: 9.94e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  170 DTGFFMNLEEDMTRYAYYYSGIGAGVLVAAYIQVSFWCLAAGRQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDV 249
Cdd:cd18575     24 DQGFAAGNTALLNRAFLLLLAVALVLALASALRFYLVSWLGERVVADLRKAVFAHLLRLSPSFFETTRTGEVLSRLTTDT 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  250 SKINEGIGDKIGMFFQSMATFFTGFIVGFTRGWKLTLVILAISPVLGLSAAV---WAKILSSFTDKELlayAKAGAVAEE 326
Cdd:cd18575    104 TLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILfgrRVRRLSRASQDRL---ADLSAFAEE 180
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  327 VLAAIRTVIAFGGQKKELERYNKNLEEA-----KRIGIKKAITAnisigAAFLLIYASYALAFWYGTTLVLSGEYSIGQv 401
Cdd:cd18575    181 TLSAIKTVQAFTREDAERQRFATAVEAAfaaalRRIRARALLTA-----LVIFLVFGAIVFVLWLGAHDVLAGRMSAGE- 254
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1149123047  402 LTVF-FSVLIGAFSVGQASPSIEAFANARGAA 432
Cdd:cd18575    255 LSQFvFYAVLAAGSVGALSEVWGDLQRAAGAA 286
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
479-678 2.17e-27

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 112.86  E-value: 2.17e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  479 ILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTIN---VRFLREIIGVVSQEP---VLFAT 552
Cdd:PRK10419    27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqRKAFRRDIQMVFQDSisaVNPRK 106
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  553 TIAENIRYG-RENVTMDEIEKAVKEANAYDfIMKLPhkfDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSAL 631
Cdd:PRK10419   107 TVREIIREPlRHLLSLDKAERLARASEMLR-AVDLD---DSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNL 182
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1149123047  632 DTESEAVVQVALDKARKGRTT--IVIAHRLSTV-RNADVIAGFDDGVIVE 678
Cdd:PRK10419   183 DLVLQAGVIRLLKKLQQQFGTacLFITHDLRLVeRFCQRVMVMDNGQIVE 232
cbiO PRK13646
energy-coupling factor transporter ATPase;
462-689 2.27e-27

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 113.34  E-value: 2.27e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYP--SRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDI----RTINVRF 535
Cdd:PRK13646     3 IRFDNVSYTYQkgTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktKDKYIRP 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  536 LREIIGVVSQ--EPVLFATTIAENIRYGRENVTMDeIEKAvkEANAYDFIMKLPHKFDTLvGERGAQLSGGQKQRIAIAR 613
Cdd:PRK13646    83 VRKRIGMVFQfpESQLFEDTVEREIIFGPKNFKMN-LDEV--KNYAHRLLMDLGFSRDVM-SQSPFQMSGGQMRKIAIVS 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1149123047  614 ALVRNPKILLLDEATSALDTESEAVVQVALDKAR--KGRTTIVIAHRLSTV-RNADVIAGFDDGVIVEKGNHDELMKEK 689
Cdd:PRK13646   159 ILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFKDK 237
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
455-689 2.35e-27

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 113.40  E-value: 2.35e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  455 PDNIkgnLEFRNVHFSYPSRKEVkiLKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQ--DIRTIN 532
Cdd:PRK13636     2 EDYI---LKVEELNYNYSDGTHA--LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKG 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  533 VRFLREIIGVVSQEP--VLFATTIAENIRYGRENVTM--DEIEKAVKEANAYDFIMKLPHKfdtlvgeRGAQLSGGQKQR 608
Cdd:PRK13636    77 LMKLRESVGMVFQDPdnQLFSASVYQDVSFGAVNLKLpeDEVRKRVDNALKRTGIEHLKDK-------PTHCLSFGQKKR 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  609 IAIARALVRNPKILLLDEATSALDTE--SEaVVQVALDKARKGRTTIVIA-HRLSTVR-NADVIAGFDDGVIVEKGNHDE 684
Cdd:PRK13636   150 VAIAGVLVMEPKVLVLDEPTAGLDPMgvSE-IMKLLVEMQKELGLTIIIAtHDIDIVPlYCDNVFVMKEGRVILQGNPKE 228

                   ....*
gi 1149123047  685 LMKEK 689
Cdd:PRK13636   229 VFAEK 233
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
1123-1330 2.46e-27

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 112.56  E-value: 2.46e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1123 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD-----PLAGKVLLDGKEI--KRLNVQWLRAHLGIVSQEPILFDC 1195
Cdd:PRK14239    21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIysPRTDTVDLRKEIGMVFQQPNPFPM 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1196 SIAENIAYGDNSRVVSQEEIVRAAKEANIHAfiESLPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSA 1275
Cdd:PRK14239   101 SIYENVVYGLRLKGIKDKQVLDEAVEKSLKG--ASIWDEVKDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTSA 178
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1149123047 1276 LDTESEKVVQEALDKAREGRTCIVIAHRL---STIqnADLIVVFQNGRVKEHGTHQQL 1330
Cdd:PRK14239   179 LDPISAGKIEETLLGLKDDYTMLLVTRSMqqaSRI--SDRTGFFLDGDLIEYNDTKQM 234
cbiO PRK13642
energy-coupling factor transporter ATPase;
1110-1332 2.71e-27

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 112.88  E-value: 2.71e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1110 VVFNYPTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQE 1189
Cdd:PRK13642    10 LVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQN 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1190 P--ILFDCSIAENIAYGDNSRVVSQEEIVRAAKEANIHAFIESLPNKystkvgdKGTQLSGGQKQRIAIARALVRQPHIL 1267
Cdd:PRK13642    90 PdnQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTR-------EPARLSGGQKQRVAVAGIIALRPEII 162
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1149123047 1268 LLDEATSALD----TESEKVVQEALDKARegRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLA 1332
Cdd:PRK13642   163 ILDESTSMLDptgrQEIMRVIHEIKEKYQ--LTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
462-634 2.75e-27

ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213263 [Multi-domain]  Cd Length: 239  Bit Score: 111.66  E-value: 2.75e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSrkeVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRflREIIG 541
Cdd:cd03296      3 IEVRNVSKRFGD---FVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVG 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  542 VVSQEPVLFA-TTIAENIRYG------RENVTMDEIEKAVKEanaydfIMKLPHkFDTLVGERGAQLSGGQKQRIAIARA 614
Cdd:cd03296     78 FVFQHYALFRhMTVFDNVAFGlrvkprSERPPEAEIRAKVHE------LLKLVQ-LDWLADRYPAQLSGGQRQRVALARA 150
                          170       180
                   ....*....|....*....|
gi 1149123047  615 LVRNPKILLLDEATSALDTE 634
Cdd:cd03296    151 LAVEPKVLLLDEPFGALDAK 170
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
1105-1330 3.63e-27

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 112.54  E-value: 3.63e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1105 VTFGEVVFNYptRPDIP-VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHL 1183
Cdd:PRK13648     8 IVFKNVSFQY--QSDASfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHI 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1184 GIVSQEPI-LFDCSIAE-NIAYGDNSRVVSQEEIVR----AAKEANIHAFIESLPNkystkvgdkgtQLSGGQKQRIAIA 1257
Cdd:PRK13648    86 GIVFQNPDnQFVGSIVKyDVAFGLENHAVPYDEMHRrvseALKQVDMLERADYEPN-----------ALSGGQKQRVAIA 154
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1149123047 1258 RALVRQPHILLLDEATSALDTESEKVVQEALDKAREGR--TCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQL 1330
Cdd:PRK13648   155 GVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
462-685 5.39e-27

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 113.52  E-value: 5.39e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSRK-------EVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDI------ 528
Cdd:PRK11308     6 LQAIDLKKHYPVKRglfkperLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLlkadpe 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  529 ------RTINVRFL--------REIIGVVSQEPVLFATTIAENIRygRENVtMDEIEKAVKEANAYDfimKLPHKFdtlv 594
Cdd:PRK11308    86 aqkllrQKIQIVFQnpygslnpRKKVGQILEEPLLINTSLSAAER--REKA-LAMMAKVGLRPEHYD---RYPHMF---- 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  595 gergaqlSGGQKQRIAIARALVRNPKILLLDEATSALDTESEA-VVQVALDKARKGRTTIV-IAHRLSTVRNadvIAgfD 672
Cdd:PRK11308   156 -------SGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAqVLNLMMDLQQELGLSYVfISHDLSVVEH---IA--D 223
                          250
                   ....*....|....*....
gi 1149123047  673 D------GVIVEKGNHDEL 685
Cdd:PRK11308   224 EvmvmylGRCVEKGTKEQI 242
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
462-677 5.39e-27

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 118.29  E-value: 5.39e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSRKE-VKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTIN----VRFL 536
Cdd:PRK10535     5 LELKDIRRSYPSGEEqVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDadalAQLR 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  537 REIIGVVSQEPVLFATTIAEnirygrENVTMDEI----EKAVKEANAYDFIMKLphKFDTLVGERGAQLSGGQKQRIAIA 612
Cdd:PRK10535    85 REHFGFIFQRYHLLSHLTAA------QNVEVPAVyaglERKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIA 156
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1149123047  613 RALVRNPKILLLDEATSALDTESEAVVQVALDKAR-KGRTTIVIAHRLSTVRNADVIAGFDDGVIV 677
Cdd:PRK10535   157 RALMNGGQVILADEPTGALDSHSGEEVMAILHQLRdRGHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
1122-1333 5.77e-27

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 114.05  E-value: 5.77e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1122 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQwlRAHLGIVSQEPILF-DCSIAEN 1200
Cdd:PRK11432    21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ--QRDICMVFQSYALFpHMSLGEN 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1201 IAYGDNSRVVSQEEIVRAAKEANIHAFIESLPNKYSTkvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEATSALDTES 1280
Cdd:PRK11432    99 VGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVD-------QISGGQQQRVALARALILKPKVLLFDEPLSNLDANL 171
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1149123047 1281 EKVVQEaldKARE-----GRTCIVIAHRLS-TIQNADLIVVFQNGRVKEHGTHQQLLAQ 1333
Cdd:PRK11432   172 RRSMRE---KIRElqqqfNITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQELYRQ 227
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
462-685 6.75e-27

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 113.26  E-value: 6.75e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRN--VHFSYPSRKE--------VKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTI 531
Cdd:PRK15079     9 LEVADlkVHFDIKDGKQwfwqppktLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGM 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  532 NVRFLREI---IGVVSQEPV-------LFATTIAENIRYGRENVTMDEIEKAVKEANAY-----DFIMKLPHKFdtlvge 596
Cdd:PRK15079    89 KDDEWRAVrsdIQMIFQDPLaslnprmTIGEIIAEPLRTYHPKLSRQEVKDRVKAMMLKvgllpNLINRYPHEF------ 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  597 rgaqlSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARK--GRTTIVIAHRLSTVRN-ADVIAGFDD 673
Cdd:PRK15079   163 -----SGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVKHiSDRVLVMYL 237
                          250
                   ....*....|..
gi 1149123047  674 GVIVEKGNHDEL 685
Cdd:PRK15079   238 GHAVELGTYDEV 249
cbiO PRK13637
energy-coupling factor transporter ATPase;
1123-1326 6.94e-27

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 112.06  E-value: 6.94e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1123 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEI--KRLNVQWLRAHLGIVSQEP--ILFDCSIA 1198
Cdd:PRK13637    23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIRKKVGLVFQYPeyQLFEETIE 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1199 ENIAYGDNSRVVSQEEIVRAAKEAnihafIESLPNKYSTkVGDKGT-QLSGGQKQRIAIARALVRQPHILLLDEATSALD 1277
Cdd:PRK13637   103 KDIAFGPINLGLSEEEIENRVKRA-----MNIVGLDYED-YKDKSPfELSGGQKRRVAIAGVVAMEPKILILDEPTAGLD 176
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1149123047 1278 TeseKVVQEALDKARE-----GRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGT 1326
Cdd:PRK13637   177 P---KGRDEILNKIKElhkeyNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGT 228
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
461-686 8.03e-27

ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 110.23  E-value: 8.03e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  461 NLEFRNVHFSYPSRkevkiLKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVrFLREIi 540
Cdd:COG3840      1 MLRLDDLTYRYGDF-----PLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPP-AERPV- 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  541 GVVSQEPVLFA-TTIAENI--------RYGRENVTmdEIEKAVKEANAYDFIMKLPhkfdtlvgergAQLSGGQKQRIAI 611
Cdd:COG3840     74 SMLFQENNLFPhLTVAQNIglglrpglKLTAEQRA--QVEQALERVGLAGLLDRLP-----------GQLSGGQRQRVAL 140
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  612 ARALVRNPKILLLDEATSALD----TESEAVV-QVAldkARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKGNHDEL 685
Cdd:COG3840    141 ARCLVRKRPILLLDEPFSALDpalrQEMLDLVdELC---RERGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAAL 217

                   .
gi 1149123047  686 M 686
Cdd:COG3840    218 L 218
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
462-632 9.15e-27

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 109.80  E-value: 9.15e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIG 541
Cdd:PRK10247     8 LQLQNVGYLAGDAK---ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVS 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  542 VVSQEPVLFATTIAENIRYGRenvtmdEIEKAVKEANAY-DFIMK--LPhkfDTLVGERGAQLSGGQKQRIAIARALVRN 618
Cdd:PRK10247    85 YCAQTPTLFGDTVYDNLIFPW------QIRNQQPDPAIFlDDLERfaLP---DTILTKNIAELSGGEKQRISLIRNLQFM 155
                          170
                   ....*....|....
gi 1149123047  619 PKILLLDEATSALD 632
Cdd:PRK10247   156 PKVLLLDEITSALD 169
cbiO PRK13644
energy-coupling factor transporter ATPase;
1110-1332 1.34e-26

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 110.85  E-value: 1.34e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1110 VVFNYPTrpDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLN-VQWLRAHLGIVSQ 1188
Cdd:PRK13644     7 VSYSYPD--GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVGIVFQ 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1189 EP--ILFDCSIAENIAYGDNSRVVSQEEIVRAAKEAnihaFIESLPNKYSTKvgdKGTQLSGGQKQRIAIARALVRQPHI 1266
Cdd:PRK13644    85 NPetQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRA----LAEIGLEKYRHR---SPKTLSGGQGQCVALAGILTMEPEC 157
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1149123047 1267 LLLDEATSALDTESEKVVQEALDKA-REGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLA 1332
Cdd:PRK13644   158 LIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLS 224
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
462-632 1.41e-26

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 112.89  E-value: 1.41e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSrkeVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDI--RTINVRflreI 539
Cdd:PRK11432     7 VVLKNITKRFGS---NTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVthRSIQQR----D 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  540 IGVVSQEPVLFA-TTIAENIRYG--RENVTMDEIEKAVKEANAydfIMKLPHKFDTLVGergaQLSGGQKQRIAIARALV 616
Cdd:PRK11432    80 ICMVFQSYALFPhMSLGENVGYGlkMLGVPKEERKQRVKEALE---LVDLAGFEDRYVD----QISGGQQQRVALARALI 152
                          170
                   ....*....|....*.
gi 1149123047  617 RNPKILLLDEATSALD 632
Cdd:PRK11432   153 LKPKVLLFDEPLSNLD 168
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
1112-1331 2.58e-26

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 109.74  E-value: 2.58e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1112 FNYPTRPdipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD-----PLAGKVLLDGKEI--KRLNVQWLRAHLG 1184
Cdd:PRK14258    15 FYYDTQK---ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElesevRVEGRVEFFNQNIyeRRVNLNRLRRQVS 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1185 IVSQEPILFDCSIAENIAYGdnsrvvsqEEIVRAAKEANIHAFIES------LPNKYSTKVGDKGTQLSGGQKQRIAIAR 1258
Cdd:PRK14258    92 MVHPKPNLFPMSVYDNVAYG--------VKIVGWRPKLEIDDIVESalkdadLWDEIKHKIHKSALDLSGGQQQRLCIAR 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1259 ALVRQPHILLLDEATSALDTESEKVVQEALD--KAREGRTCIVIAHRLSTIQN-ADLIVVFQN-----GRVKEHGTHQQL 1330
Cdd:PRK14258   164 ALAVKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVSHNLHQVSRlSDFTAFFKGnenriGQLVEFGLTKKI 243

                   .
gi 1149123047 1331 L 1331
Cdd:PRK14258   244 F 244
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
1109-1334 2.83e-26

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 110.17  E-value: 2.83e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1109 EVVFNYPTrpDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWL--RAHLGIV 1186
Cdd:PRK13639     6 DLKYSYPD--GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLevRKTVGIV 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1187 SQEP--ILFDCSIAENIAYGDNSRVVSQEEIVRAAKEANIHAFIESLPNKystkvgdKGTQLSGGQKQRIAIARALVRQP 1264
Cdd:PRK13639    84 FQNPddQLFAPTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENK-------PPHHLSGGQKKRVAIAGILAMKP 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1149123047 1265 HILLLDEATSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQ-NADLIVVFQNGRVKEHGTHQQLLAQK 1334
Cdd:PRK13639   157 EIIVLDEPTSGLDPMgASQIMKLLYDLNKEGITIIISTHDVDLVPvYADKVYVMSDGKIIKEGTPKEVFSDI 228
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
1122-1332 3.30e-26

putative amino-acid ABC transporter ATP-binding protein YecC; Provisional


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 109.07  E-value: 3.30e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1122 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEI---KRLNVQW-----LRAHLGIVSQEPILF 1193
Cdd:PRK11264    18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtaRSLSQQKglirqLRQHVGFVFQNFNLF 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1194 DC-SIAENIAYGDnsrVVSQEEIVRAAkeanihafiESLPNKYSTKVGDKGTQ------LSGGQKQRIAIARALVRQPHI 1266
Cdd:PRK11264    98 PHrTVLENIIEGP---VIVKGEPKEEA---------TARARELLAKVGLAGKEtsyprrLSGGQQQRVAIARALAMRPEV 165
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1149123047 1267 LLLDEATSALDTEsekVVQEALDK----AREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLLA 1332
Cdd:PRK11264   166 ILFDEPTSALDPE---LVGEVLNTirqlAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFA 233
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
1121-1319 3.34e-26

ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 115.29  E-value: 3.34e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1121 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLL-DGKEIkrlnvqwlrahLgIVSQEPILFDCSIAE 1199
Cdd:COG4178    377 PLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARV-----------L-FLPQRPYLPLGTLRE 444
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1200 NIAYGDNSRVVSQEEIVRAAKEANIHAFIESLpnkysTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTE 1279
Cdd:COG4178    445 ALLYPATAEAFSDAELREALEAVGLGHLAERL-----DEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEE 519
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1149123047 1280 SEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNG 1319
Cdd:COG4178    520 NEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLELTGD 559
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
1109-1334 3.77e-26

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 109.94  E-value: 3.77e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1109 EVVFNYPTRPDipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEI--KRLNVQWLRAHLGIV 1186
Cdd:PRK13636    10 ELNYNYSDGTH--ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdySRKGLMKLRESVGMV 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1187 SQEP--ILFDCSIAENIAYGDNSRVVSQEEIVRAAKEANIHAFIESLPNKYStkvgdkgTQLSGGQKQRIAIARALVRQP 1264
Cdd:PRK13636    88 FQDPdnQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPT-------HCLSFGQKKRVAIAGVLVMEP 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1149123047 1265 HILLLDEATSALD----TESEKVVQEALDKAreGRTCIVIAHRLSTIQ-NADLIVVFQNGRVKEHGTHQQLLAQK 1334
Cdd:PRK13636   161 KVLVLDEPTAGLDpmgvSEIMKLLVEMQKEL--GLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAEK 233
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
461-683 4.06e-26

ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 443326 [Multi-domain]  Cd Length: 242  Bit Score: 108.56  E-value: 4.06e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  461 NLEFRNVHFSYPSrkeVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDG------QDIRTINVR 534
Cdd:COG4161      2 SIQLKNINCFYGS---HQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIR 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  535 FLREIIGVVSQE----PVLfatTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPHKFDTLvgerGAQLSGGQKQRIA 610
Cdd:COG4161     79 LLRQKVGMVFQQynlwPHL---TVMENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRF----PLHLSGGQQQRVA 151
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1149123047  611 IARALVRNPKILLLDEATSALDTESEA-VVQVALDKARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKGNHD 683
Cdd:COG4161    152 IARALMMEPQVLLFDEPTAALDPEITAqVVEIIRELSQTGITQVIVTHEVEFARKvASQVVYMEKGRIIEQGDAS 226
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
1121-1331 4.23e-26

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 109.09  E-value: 4.23e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1121 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEPIL-FDCSIAE 1199
Cdd:PRK13548    16 TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFTVEE 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1200 NIAYG--DNSRVVSQ-EEIVRAA-KEANIHAFIESLpnkYstkvgdkgTQLSGGQKQRIAIARALVR------QPHILLL 1269
Cdd:PRK13548    96 VVAMGraPHGLSRAEdDALVAAAlAQVDLAHLAGRD---Y--------PQLSGGEQQRVQLARVLAQlwepdgPPRWLLL 164
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1149123047 1270 DEATSALD-TESEKVVQEALDKARE-GRTCIVIAHRLS-TIQNADLIVVFQNGRVKEHGTHQQLL 1331
Cdd:PRK13548   165 DEPTSALDlAHQHHVLRLARQLAHErGLAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPAEVL 229
cbiO PRK13649
energy-coupling factor transporter ATPase;
1105-1326 4.76e-26

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 109.45  E-value: 4.76e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1105 VTFGEVVFNYP--TRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEI----KRLNVQW 1178
Cdd:PRK13649     3 INLQNVSYTYQagTPFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstsKNKDIKQ 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1179 LRAHLGIVSQ--EPILFDCSIAENIAYGDNSRVVSQEEIVRAAKEA-NIHAFIESLPNKystkvgdKGTQLSGGQKQRIA 1255
Cdd:PRK13649    83 IRKKVGLVFQfpESQLFEETVLKDVAFGPQNFGVSQEEAEALAREKlALVGISESLFEK-------NPFELSGGQMRRVA 155
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1149123047 1256 IARALVRQPHILLLDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGT 1326
Cdd:PRK13649   156 IAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQsGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGK 228
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
1122-1323 5.13e-26

Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 443338 [Multi-domain]  Cd Length: 233  Bit Score: 107.90  E-value: 5.13e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1122 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQL---LERfydPLAGKVLLDGKEIKRLN----VQWLRAHLGIVSQE----P 1190
Cdd:COG4181     27 ILKGISLEVEAGESVAIVGASGSGKSTLLGLlagLDR---PTSGTVRLAGQDLFALDedarARLRARHVGFVFQSfqllP 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1191 ILfdcSIAEN------IAYGDNSRVVSQEEIVRAAKEANIHAFieslPNkystkvgdkgtQLSGGQKQRIAIARALVRQP 1264
Cdd:COG4181    104 TL---TALENvmlpleLAGRRDARARARALLERVGLGHRLDHY----PA-----------QLSGGEQQRVALARAFATEP 165
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1149123047 1265 HILLLDEATSALDTESEKVVQEAL-DKARE-GRTCIVIAHRLSTIQNADLIVVFQNGRVKE 1323
Cdd:COG4181    166 AILFADEPTGNLDAATGEQIIDLLfELNRErGTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
1118-1319 6.01e-26

ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.


Pssm-ID: 213257 [Multi-domain]  Cd Length: 218  Bit Score: 107.42  E-value: 6.01e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1118 PDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAH----LGIVSQEPILF 1193
Cdd:cd03290     12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWLL 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1194 DCSIAENIAYGDNSRVVSQEEIVRAAkeaNIHAFIESLPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEAT 1273
Cdd:cd03290     92 NATVEENITFGSPFNKQRYKAVTDAC---SLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPF 168
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1149123047 1274 SALDTE-SEKVVQEALDK--AREGRTCIVIAHRLSTIQNADLIVVFQNG 1319
Cdd:cd03290    169 SALDIHlSDHLMQEGILKflQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
cbiO PRK13641
energy-coupling factor transporter ATPase;
462-680 6.03e-26

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 109.53  E-value: 6.03e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYP--SRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIR----TINVRF 535
Cdd:PRK13641     3 IKFENVDYIYSpgTPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKK 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  536 LREIIGVVSQ--EPVLFATTIAENIRYGRENVTMDEIEKAVKeanAYDFIMKLPHKfDTLVGERGAQLSGGQKQRIAIAR 613
Cdd:PRK13641    83 LRKKVSLVFQfpEAQLFENTVLKDVEFGPKNFGFSEDEAKEK---ALKWLKKVGLS-EDLISKSPFELSGGQMRRVAIAG 158
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1149123047  614 ALVRNPKILLLDEATSALDTES-EAVVQVALDKARKGRTTIVIAHrlstvrNADVIAGFDDGVIV-EKG 680
Cdd:PRK13641   159 VMAYEPEILCLDEPAAGLDPEGrKEMMQLFKDYQKAGHTVILVTH------NMDDVAEYADDVLVlEHG 221
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
474-680 6.69e-26

White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.


Pssm-ID: 213201 [Multi-domain]  Cd Length: 226  Bit Score: 107.36  E-value: 6.69e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  474 RKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQL-MQRLYDP--TEGMVSVDGQDIRTINVRFlreIIGVVSQEPVLF 550
Cdd:cd03234     17 NKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAiSGRVEGGgtTSGQILFNGQPRKPDQFQK---CVAYVRQDDILL 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  551 AT-TIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPHkfDTLVG-ERGAQLSGGQKQRIAIARALVRNPKILLLDEAT 628
Cdd:cd03234     94 PGlTVRETLTYTAILRLPRKSSDAIRKKRVEDVLLRDLA--LTRIGgNLVKGISGGERRRVSIAVQLLWDPKVLILDEPT 171
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1149123047  629 SALDTESE-AVVQVALDKARKGRTTIVIAH--RLSTVRNADVIAGFDDGVIVEKG 680
Cdd:cd03234    172 SGLDSFTAlNLVSTLSQLARRNRIVILTIHqpRSDLFRLFDRILLLSSGEIVYSG 226
cbiO PRK13649
energy-coupling factor transporter ATPase;
462-689 6.70e-26

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 109.06  E-value: 6.70e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSRK--EVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTI----NVRF 535
Cdd:PRK13649     3 INLQNVSYTYQAGTpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTsknkDIKQ 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  536 LREIIGVVSQ--EPVLFATTIAENIRYGREN--VTMDEIEKAVKEANAYDFIMklphkfDTLVGERGAQLSGGQKQRIAI 611
Cdd:PRK13649    83 IRKKVGLVFQfpESQLFEETVLKDVAFGPQNfgVSQEEAEALAREKLALVGIS------ESLFEKNPFELSGGQMRRVAI 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  612 ARALVRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIV-IAHRLSTVRN-ADVIAGFDDGVIVEKG------NHD 683
Cdd:PRK13649   157 AGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVlVTHLMDDVANyADFVYVLEKGKLVLSGkpkdifQDV 236

                   ....*.
gi 1149123047  684 ELMKEK 689
Cdd:PRK13649   237 DFLEEK 242
cbiO PRK13640
energy-coupling factor transporter ATPase;
1105-1326 8.07e-26

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 108.73  E-value: 8.07e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1105 VTFGEVVFNYPTRPDiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLA---GKVLLDGKEIKRLNVQWLRA 1181
Cdd:PRK13640     6 VEFKHVSFTYPDSKK-PALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTAKTVWDIRE 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1182 HLGIVSQEP--ILFDCSIAENIAYGDNSRVVSQEEIVR----AAKEANIHAFIESLPnkystkvgdkgTQLSGGQKQRIA 1255
Cdd:PRK13640    85 KVGIVFQNPdnQFVGATVGDDVAFGLENRAVPRPEMIKivrdVLADVGMLDYIDSEP-----------ANLSGGQKQRVA 153
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1149123047 1256 IARALVRQPHILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGT 1326
Cdd:PRK13640   154 IAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGS 226
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
1114-1330 8.19e-26

ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.


Pssm-ID: 213230 [Multi-domain]  Cd Length: 220  Bit Score: 106.82  E-value: 8.19e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1114 YPTRPDiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRlNVQWLRAHLGIVSQEPILF 1193
Cdd:cd03263     10 YKKGTK-PAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGYCPQFDALF 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1194 D-CSIAENIAYgdNSRV--VSQEEIvraakEANIHAFIE--SLPNKYSTKVGDkgtqLSGGQKQRIAIARALVRQPHILL 1268
Cdd:cd03263     88 DeLTVREHLRF--YARLkgLPKSEI-----KEEVELLLRvlGLTDKANKRART----LSGGMKRKLSLAIALIGGPSVLL 156
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1149123047 1269 LDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQL 1330
Cdd:cd03263    157 LDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
476-686 8.76e-26

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 108.13  E-value: 8.76e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  476 EVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTI-------------NVRFLREIIGV 542
Cdd:PRK10619    17 EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlkvadknQLRLLRTRLTM 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  543 VSQEPVLFA-TTIAENIRygRENVTMDEIEKAVKEANAYDFIMKLPHKfDTLVGERGAQLSGGQKQRIAIARALVRNPKI 621
Cdd:PRK10619    97 VFQHFNLWShMTVLENVM--EAPIQVLGLSKQEARERAVKYLAKVGID-ERAQGKYPVHLSGGQQQRVSIARALAMEPEV 173
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1149123047  622 LLLDEATSALDTE-SEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGF-DDGVIVEKGNHDELM 686
Cdd:PRK10619   174 LLFDEPTSALDPElVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFlHQGKIEEEGAPEQLF 240
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
1121-1333 1.08e-25

ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 443332 [Multi-domain]  Cd Length: 533  Bit Score: 113.24  E-value: 1.08e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1121 PVLQGLSLEVKKGQTLALVGSSGCGKS----TVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRA----HLGIVSQEPI- 1191
Cdd:COG4172     24 EAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRirgnRIAMIFQEPMt 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1192 ----LFdcSIAENIAygdnsrvvsqeEIVRA-----AKEANIHAfIESLpnkysTKVG--DKGT-------QLSGGQKQR 1253
Cdd:COG4172    104 slnpLH--TIGKQIA-----------EVLRLhrglsGAAARARA-LELL-----ERVGipDPERrldayphQLSGGQRQR 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1254 IAIARALVRQPHILLLDEATSALDTesekVVQ-EALD-----KAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGT 1326
Cdd:COG4172    165 VMIAMALANEPDLLIADEPTTALDV----TVQaQILDllkdlQRELGMALLLITHDLGVVRRfADRVAVMRQGEIVEQGP 240

                   ....*..
gi 1149123047 1327 HQQLLAQ 1333
Cdd:COG4172    241 TAELFAA 247
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
1126-1325 1.15e-25

ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213265 [Multi-domain]  Cd Length: 211  Bit Score: 106.42  E-value: 1.15e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1126 LSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQwlRAHLGIVSQEPILF-DCSIAENIAYG 1204
Cdd:cd03298     17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVSMLFQENNLFaHLTVEQNVGLG 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1205 DNSRV----VSQEEIVRAAKEANIHAFIESLPNkystkvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEATSALDTES 1280
Cdd:cd03298     95 LSPGLkltaEDRQAIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALARVLVRDKPVLLLDEPFAALDPAL 163
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1149123047 1281 EKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHG 1325
Cdd:cd03298    164 RAEMLDLVLDlhAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
ABC_6TM_MsbA_like cd18552
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ...
197-415 1.33e-25

Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349996 [Multi-domain]  Cd Length: 292  Bit Score: 108.28  E-value: 1.33e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  197 VAAYIQVSFWCLAAGRQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQSMATFFTGFIV 276
Cdd:cd18552     54 LASYLQTYLMAYVGQRVVRDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGV 133
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  277 GFTRGWKLTLVILAISPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKR 356
Cdd:cd18552    134 LFYLDWKLTLIALVVLPLAALPIRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRR 213
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1149123047  357 IGIKKAITANISIGAAFLLIYASYALAFWYGTTLVLSGEYSIGQvltvFFSVLIGAFSV 415
Cdd:cd18552    214 LSMKIARARALSSPLMELLGAIAIALVLWYGGYQVISGELTPGE----FISFITALLLL 268
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
462-680 1.37e-25

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 107.31  E-value: 1.37e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSrkeVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYD-----PTEGMVSVDGQDIRTINVRFL 536
Cdd:PRK14247     4 IEIRDLKVSFGQ---VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIEL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  537 REIIGVVSQEPVLFAT-TIAENIRYG----RENVTMDEIEKAVKEANAYdfiMKLPHKFDTLVGERGAQLSGGQKQRIAI 611
Cdd:PRK14247    81 RRRVQMVFQIPNPIPNlSIFENVALGlklnRLVKSKKELQERVRWALEK---AQLWDEVKDRLDAPAGKLSGGQQQRLCI 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  612 ARALVRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAH-RLSTVRNADVIAGFDDGVIVEKG 680
Cdd:PRK14247   158 ARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWG 227
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
478-634 1.73e-25

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 109.79  E-value: 1.73e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  478 KILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLReiIGVVSQEPVLFA-TTIAE 556
Cdd:PRK10851    16 QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRK--VGFVFQHYALFRhMTVFD 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  557 NIRYG------RENVTMDEIEKAVKEANAydfIMKLPHkfdtLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSA 630
Cdd:PRK10851    94 NIAFGltvlprRERPNAAAIKAKVTQLLE---MVQLAH----LADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGA 166

                   ....
gi 1149123047  631 LDTE 634
Cdd:PRK10851   167 LDAQ 170
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
1126-1334 1.76e-25

molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]


Pssm-ID: 131197 [Multi-domain]  Cd Length: 354  Bit Score: 109.82  E-value: 1.76e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1126 LSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEI----KRLNVQWLRAHLGIVSQEPILF-DCSIAEN 1200
Cdd:TIGR02142   16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLfdsrKGIFLPPEKRRIGYVFQEARLFpHLSVRGN 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1201 IAYG-----DNSRVVSQEEIVRAAkeaNIHAFIESLPNKystkvgdkgtqLSGGQKQRIAIARALVRQPHILLLDEATSA 1275
Cdd:TIGR02142   96 LRYGmkrarPSERRISFERVIELL---GIGHLLGRLPGR-----------LSGGEKQRVAIGRALLSSPRLLLMDEPLAA 161
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1149123047 1276 LDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLLAQK 1334
Cdd:TIGR02142  162 LDDPRKYEILPYLERLHAefGIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWASP 223
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
1119-1332 1.98e-25

ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];


Pssm-ID: 440179 [Multi-domain]  Cd Length: 236  Bit Score: 106.22  E-value: 1.98e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1119 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVqWLRAHLGI--VSQEPILF-DC 1195
Cdd:COG0410     15 GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPP-HRIARLGIgyVPEGRRIFpSL 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1196 SIAENIAYGdnSRVVSQEEIVRAAKEANIHAFieslPN-KysTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATS 1274
Cdd:COG0410     94 TVEENLLLG--AYARRDRAEVRADLERVYELF----PRlK--ERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSL 165
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1149123047 1275 ALdteSEKVVQEALDK----AREGRTCIVI---AHRLSTIqnADLIVVFQNGRVKEHGTHQQLLA 1332
Cdd:COG0410    166 GL---APLIVEEIFEIirrlNREGVTILLVeqnARFALEI--ADRAYVLERGRIVLEGTAAELLA 225
cbiO PRK13644
energy-coupling factor transporter ATPase;
462-688 2.14e-25

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 107.38  E-value: 2.14e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSRKEVkiLKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTIN-VRFLREII 540
Cdd:PRK13644     2 IRLENVSYSYPDGTPA--LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  541 GVVSQEP--VLFATTIAENIRYGRENVTMD--EIEKAVKEANAYDFIMKLPHKfdtlvgeRGAQLSGGQKQRIAIARALV 616
Cdd:PRK13644    80 GIVFQNPetQFVGRTVEEDLAFGPENLCLPpiEIRKRVDRALAEIGLEKYRHR-------SPKTLSGGQGQCVALAGILT 152
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1149123047  617 RNPKILLLDEATSALDTES-EAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELMKE 688
Cdd:PRK13644   153 MEPECLIFDEVTSMLDPDSgIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSD 225
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
462-680 2.76e-25

ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213231 [Multi-domain]  Cd Length: 211  Bit Score: 104.97  E-value: 2.76e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSRKevkILKGLNLKVQSGQTvALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRtINVRFLREIIG 541
Cdd:cd03264      1 LQLENLTKRYGKKR---ALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVL-KQPQKLRRRIG 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  542 VVSQEPVLFAT-TIAENIRY-----GRENVTMD-EIEKAVKEANAYDFimklphkfdtlVGERGAQLSGGQKQRIAIARA 614
Cdd:cd03264     76 YLPQEFGVYPNfTVREFLDYiawlkGIPSKEVKaRVDEVLELVNLGDR-----------AKKKIGSLSGGMRRRVGIAQA 144
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1149123047  615 LVRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKG 680
Cdd:cd03264    145 LVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
462-628 3.11e-25

ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];


Pssm-ID: 440179 [Multi-domain]  Cd Length: 236  Bit Score: 105.83  E-value: 3.11e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPsrkEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINV-RFLREII 540
Cdd:COG0410      4 LEVENLHAGYG---GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPhRIARLGI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  541 GVVSQEPVLFAT-TIAENIRYGRENVTMDEIEKAVKEAnAYDFimklphkFDTLvGER----GAQLSGGQKQRIAIARAL 615
Cdd:COG0410     81 GYVPEGRRIFPSlTVEENLLLGAYARRDRAEVRADLER-VYEL-------FPRL-KERrrqrAGTLSGGEQQMLAIGRAL 151
                          170
                   ....*....|...
gi 1149123047  616 VRNPKILLLDEAT 628
Cdd:COG0410    152 MSRPKLLLLDEPS 164
TauB COG4525
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
462-632 3.42e-25

ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 443596 [Multi-domain]  Cd Length: 262  Bit Score: 106.48  E-value: 3.42e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSRKEVK-ILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRflReii 540
Cdd:COG4525      4 LTVRHVSVRYPGGGQPQpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGAD--R--- 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  541 GVVSQEPVLFA-TTIAENIRYGrenVTMDEIEKAVKEANAYDFImklphkfdTLVGERGA------QLSGGQKQRIAIAR 613
Cdd:COG4525     79 GVVFQKDALLPwLNVLDNVAFG---LRLRGVPKAERRARAEELL--------ALVGLADFarrriwQLSGGMRQRVGIAR 147
                          170
                   ....*....|....*....
gi 1149123047  614 ALVRNPKILLLDEATSALD 632
Cdd:COG4525    148 ALAADPRFLLMDEPFGALD 166
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
1123-1333 3.65e-25

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 108.13  E-value: 3.65e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1123 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIK---RLNVQWLRAHLGIVSQEPilfdcsiae 1199
Cdd:PRK11308    31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLkadPEAQKLLRQKIQIVFQNP--------- 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1200 niaYGD-NSR-VVSQ--EE-------IVRAAKEANIHAFIEslpnkystKVGDKGTQ-------LSGGQKQRIAIARALV 1261
Cdd:PRK11308   102 ---YGSlNPRkKVGQilEEpllintsLSAAERREKALAMMA--------KVGLRPEHydryphmFSGGQRQRIAIARALM 170
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1149123047 1262 RQPHILLLDEATSALDTESE-KVVQEALDKAREGRTCIV-IAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLLAQ 1333
Cdd:PRK11308   171 LDPDVVVADEPVSALDVSVQaQVLNLMMDLQQELGLSYVfISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIFNN 245
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...
1104-1321 3.80e-25

ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];


Pssm-ID: 440180 [Multi-domain]  Cd Length: 257  Bit Score: 106.28  E-value: 3.80e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1104 NVT--FGEVVfnyptrpdipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVqWLRA 1181
Cdd:COG0411      9 GLTkrFGGLV----------AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPP-HRIA 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1182 HLGIVS--QEPILF-DCSIAENIAYG--------------DNSRVVSQEEIVRAAKEANIHAFieSLPNKYSTKVGDkgt 1244
Cdd:COG0411     78 RLGIARtfQNPRLFpELTVLENVLVAaharlgrgllaallRLPRARREEREARERAEELLERV--GLADRADEPAGN--- 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1245 qLSGGQKQRIAIARALVRQPHILLLDEATSAL-DTESEKVVqEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVFQNGR 1320
Cdd:COG0411    153 -LSYGQQRRLEIARALATEPKLLLLDEPAAGLnPEETEELA-ELIRRLRDerGITILLIEHDMDLVMGlADRIVVLDFGR 230

                   .
gi 1149123047 1321 V 1321
Cdd:COG0411    231 V 231
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
461-685 3.86e-25

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 108.96  E-value: 3.86e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  461 NLEFRNVHFSYpsrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQdiRTINVRFLREII 540
Cdd:PRK11000     3 SVTLRNVTKAY---GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEK--RMNDVPPAERGV 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  541 GVVSQEPVLFA-TTIAENIRYGRE--NVTMDEIEKAVKEANAydfIMKLPHkfdtLVGERGAQLSGGQKQRIAIARALVR 617
Cdd:PRK11000    78 GMVFQSYALYPhLSVAENMSFGLKlaGAKKEEINQRVNQVAE---VLQLAH----LLDRKPKALSGGQRQRVAIGRTLVA 150
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1149123047  618 NPKILLLDEATSALDTESEAVVQVALDKARK--GRTTIVIAH-RLSTVRNADVIAGFDDGVIVEKGNHDEL 685
Cdd:PRK11000   151 EPSVFLLDEPLSNLDAALRVQMRIEISRLHKrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
1123-1333 3.92e-25

ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 443319 [Multi-domain]  Cd Length: 358  Bit Score: 108.65  E-value: 3.92e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1123 LQGLSLEVK-----KGQTlALVGSSGCGKSTVVQL---LERfydP------LAGKVLLDGKeikrlNVQWLRAH---LGI 1185
Cdd:COG4148     11 RGGFTLDVDftlpgRGVT-ALFGPSGSGKTTLLRAiagLER---PdsgrirLGGEVLQDSA-----RGIFLPPHrrrIGY 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1186 VSQEPILFD-CSIAENIAYG-----DNSRVVSQEEIVRAAKeanihafIESLPNKYStkvgdkgTQLSGGQKQRIAIARA 1259
Cdd:COG4148     82 VFQEARLFPhLSVRGNLLYGrkrapRAERRISFDEVVELLG-------IGHLLDRRP-------ATLSGGERQRVAIGRA 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1260 LVRQPHILLLDEATSALDTESeKvvQEALDK----AREGRTCIV-IAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLLAQ 1333
Cdd:COG4148    148 LLSSPRLLLMDEPLAALDLAR-K--AEILPYlerlRDELDIPILyVSHSLDEVARlADHVVLLEQGRVVASGPLAEVLSR 224
ABC_6TM_YknU_like cd18542
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ...
191-407 3.94e-25

Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349986 [Multi-domain]  Cd Length: 292  Bit Score: 107.13  E-value: 3.94e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  191 IGAGVL--VAAYIQVSFWCLAAGRQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQSMA 268
Cdd:cd18542     46 LGVALLrgVFRYLQGYLAEKASQKVAYDLRNDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVL 125
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  269 TFFTGFIVGFTRGWKLTLVILAISPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYN 348
Cdd:cd18542    126 LFIGALIIMFSINWKLTLISLAIIPFIALFSYVFFKKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFD 205
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1149123047  349 KNLEEAKRIGIKKAITANISIGAAFLLIYASYALAFWYGTTLVLSGEYSIGQvLTVFFS 407
Cdd:cd18542    206 KENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVLVLWVGGYLVINGEITLGE-LVAFIS 263
nickel_nikE TIGR02769
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ...
1121-1334 3.95e-25

nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 131816 [Multi-domain]  Cd Length: 265  Bit Score: 106.43  E-value: 3.95e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1121 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRA---HLGIVSQEpilfdcsi 1197
Cdd:TIGR02769   25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAfrrDVQLVFQD-------- 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1198 aeniAYGDNSRVVSQEEIVR-----------AAKEANIHAFIE--SLPNKYSTKVGdkgTQLSGGQKQRIAIARALVRQP 1264
Cdd:TIGR02769   97 ----SPSAVNPRMTVRQIIGeplrhltsldeSEQKARIAELLDmvGLRSEDADKLP---RQLSGGQLQRINIARALAVKP 169
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1149123047 1265 HILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLLAQK 1334
Cdd:TIGR02769  170 KLIVLDEAVSNLDMVLQAVILELLRKlqQAFGTAYLFITHDLRLVQSfCQRVAVMDKGQIVEECDVAQLLSFK 242
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
1122-1342 4.54e-25

ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.


Pssm-ID: 213256 [Multi-domain]  Cd Length: 275  Bit Score: 106.48  E-value: 4.54e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1122 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDpLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEPILFDCSIAENI 1201
Cdd:cd03289     19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTFRKNL 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1202 -AYGDNSrvvsQEEIVRAAKEANIHAFIESLPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTES 1280
Cdd:cd03289     98 dPYGKWS----DEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPIT 173
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1149123047 1281 EKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQKGIYFSMVS 1342
Cdd:cd03289    174 YQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQAIS 235
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
462-685 5.68e-25

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 108.77  E-value: 5.68e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSRKEVKilkGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDI-------RTINVR 534
Cdd:PRK11607    20 LEIRNLTKSFDGQHAVD---DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLshvppyqRPINMM 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  535 FlreiigvvsQEPVLFA-TTIAENIRYG--RENVTMDEIEKAVKE----ANAYDFIMKLPHkfdtlvgergaQLSGGQKQ 607
Cdd:PRK11607    97 F---------QSYALFPhMTVEQNIAFGlkQDKLPKAEIASRVNEmlglVHMQEFAKRKPH-----------QLSGGQRQ 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  608 RIAIARALVRNPKILLLDEATSALDTESEAVVQVALDK--ARKGRTTIVIAH-RLSTVRNADVIAGFDDGVIVEKGNHDE 684
Cdd:PRK11607   157 RVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDilERVGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEE 236

                   .
gi 1149123047  685 L 685
Cdd:PRK11607   237 I 237
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
1123-1319 5.68e-25

nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]


Pssm-ID: 130252 [Multi-domain]  Cd Length: 230  Bit Score: 104.86  E-value: 5.68e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1123 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLrahlgIVSQEPILFD-CSIAENI 1201
Cdd:TIGR01184    1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPwLTVRENI 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1202 AYGDNS-----RVVSQEEIVRAakeaniHAFIESLpnkysTKVGDKG-TQLSGGQKQRIAIARALVRQPHILLLDEATSA 1275
Cdd:TIGR01184   76 ALAVDRvlpdlSKSERRAIVEE------HIALVGL-----TEAADKRpGQLSGGMKQRVAIARALSIRPKVLLLDEPFGA 144
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1149123047 1276 LDTESEKVVQEALDKARE--GRTCIVIAHRL-STIQNADLIVVFQNG 1319
Cdd:TIGR01184  145 LDALTRGNLQEELMQIWEehRVTVLMVTHDVdEALLLSDRVVMLTNG 191
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
462-672 5.91e-25

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 106.02  E-value: 5.91e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSRKEVKilkGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYD--PT---EGMVSVDGQDI--RTINVR 534
Cdd:PRK14243    11 LRTENLNVYYGSFLAVK---NVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGfrvEGKVTFHGKNLyaPDVDPV 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  535 FLREIIGVVSQEPVLFATTIAENIRYG-REN---VTMDE-IEKAVKEANAYDFIMklphkfDTLvGERGAQLSGGQKQRI 609
Cdd:PRK14243    88 EVRRRIGMVFQKPNPFPKSIYDNIAYGaRINgykGDMDElVERSLRQAALWDEVK------DKL-KQSGLSLSGGQQQRL 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1149123047  610 AIARALVRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTV-RNADVIAGFD 672
Cdd:PRK14243   161 CIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAaRVSDMTAFFN 224
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
461-632 6.61e-25

sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 108.01  E-value: 6.61e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  461 NLEFRNVHFSYPSRKEVkiLKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRfLREIi 540
Cdd:PRK11650     3 GLKLQAVRKSYDGKTQV--IKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPA-DRDI- 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  541 GVVSQEPVLFA-TTIAENIRYGRENVTM--DEIEKAVKEANAydfIMKLphkfDTLVGERGAQLSGGQKQRIAIARALVR 617
Cdd:PRK11650    79 AMVFQNYALYPhMSVRENMAYGLKIRGMpkAEIEERVAEAAR---ILEL----EPLLDRKPRELSGGQRQRVAMGRAIVR 151
                          170
                   ....*....|....*
gi 1149123047  618 NPKILLLDEATSALD 632
Cdd:PRK11650   152 EPAVFLFDEPLSNLD 166
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
1119-1325 7.85e-25

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 104.99  E-value: 7.85e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1119 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD-----PLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEP-IL 1192
Cdd:PRK14247    15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPnPI 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1193 FDCSIAENIAYGD--NSRVVSQEEIVRAAKEANIHAfieSLPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLD 1270
Cdd:PRK14247    95 PNLSIFENVALGLklNRLVKSKKELQERVRWALEKA---QLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLAD 171
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1149123047 1271 EATSALDTESEKVVQEALDKAREGRTCIVIAH------RLStiqnaDLIVVFQNGRVKEHG 1325
Cdd:PRK14247   172 EPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRIS-----DYVAFLYKGQIVEWG 227
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
1117-1325 7.89e-25

ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];


Pssm-ID: 440736 [Multi-domain]  Cd Length: 250  Bit Score: 105.17  E-value: 7.89e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1117 RPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVL-LDGKEIKRLNVQWLRAHLGIVS---QEPIL 1192
Cdd:COG1119     13 RGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVrLFGERRGGEDVWELRKRIGLVSpalQLRFP 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1193 FDCSIAENIAYGDNS-----RVVSQEEIVRAakEANIHAF-IESLPNK-YSTkvgdkgtqLSGGQKQRIAIARALVRQPH 1265
Cdd:COG1119     93 RDETVLDVVLSGFFDsiglyREPTDEQRERA--RELLELLgLAHLADRpFGT--------LSQGEQRRVLIARALVKDPE 162
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1149123047 1266 ILLLDEATSALDTESEKVVQEALDK-AREGRTCIV-IAHRL----STIQNAdliVVFQNGRVKEHG 1325
Cdd:COG1119    163 LLILDEPTAGLDLGARELLLALLDKlAAEGAPTLVlVTHHVeeipPGITHV---LLLKDGRVVAAG 225
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
1108-1331 1.09e-24

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 104.74  E-value: 1.09e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1108 GEVVFN----YPTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERF---YDP---LAGKVLLDGKEIKRLNVQ 1177
Cdd:PRK14246     7 AEDVFNisrlYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiYDSkikVDGKVLYFGKDIFQIDAI 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1178 WLRAHLGIVSQEPILF-DCSIAENIAYGDNSRVVSQEEIVRAAKEANIHAFieSLPNKYSTKVGDKGTQLSGGQKQRIAI 1256
Cdd:PRK14246    87 KLRKEVGMVFQQPNPFpHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKV--GLWKEVYDRLNSPASQLSGGQQQRLTI 164
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1149123047 1257 ARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLL 1331
Cdd:PRK14246   165 ARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIF 240
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
1120-1302 1.35e-24

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 107.61  E-value: 1.35e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1120 IPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRlnVQWLRAHLGIVSQEPILF-DCSIA 1198
Cdd:PRK11607    32 QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSH--VPPYQRPINMMFQSYALFpHMTVE 109
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1199 ENIAYGdnsrvVSQEEIVRAAKEANIHAFIESLPNKYSTKvgDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDT 1278
Cdd:PRK11607   110 QNIAFG-----LKQDKLPKAEIASRVNEMLGLVHMQEFAK--RKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDK 182
                          170       180
                   ....*....|....*....|....*.
gi 1149123047 1279 ESEKVVQ-EALD-KAREGRTCIVIAH 1302
Cdd:PRK11607   183 KLRDRMQlEVVDiLERVGVTCVMVTH 208
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
462-680 1.39e-24

ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 443332 [Multi-domain]  Cd Length: 533  Bit Score: 109.77  E-value: 1.39e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPS-RKEVKILKGLNLKVQSGQTVALVGNSGCGKSTT----VQLMQRLYDPTEGMVSVDGQDIRTINVRFL 536
Cdd:COG4172      7 LSVEDLSVAFGQgGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTalsiLRLLPDPAAHPSGSILFDGQDLLGLSEREL 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  537 REI----IGVVSQEPV-----LFatTI----AENIRYGReNVTMDEIEKAVKE-------------ANAYdfimklPHkf 590
Cdd:COG4172     87 RRIrgnrIAMIFQEPMtslnpLH--TIgkqiAEVLRLHR-GLSGAAARARALEllervgipdperrLDAY------PH-- 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  591 dtlvgergaQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAvvQVaLD-----KARKGRTTIVIAHRLSTVRN- 664
Cdd:COG4172    156 ---------QLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQA--QI-LDllkdlQRELGMALLLITHDLGVVRRf 223
                          250
                   ....*....|....*.
gi 1149123047  665 ADVIAGFDDGVIVEKG 680
Cdd:COG4172    224 ADRVAVMRQGEIVEQG 239
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
476-692 1.48e-24

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 106.09  E-value: 1.48e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  476 EVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVD----GQDIRTI------------NVRFLREI 539
Cdd:PRK13631    38 ELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyiGDKKNNHelitnpyskkikNFKELRRR 117
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  540 IGVVSQEP--VLFATTIAENIRYGRENVTMDEIEkAVKEANAYDFIMKLPHKFDtlvgERGA-QLSGGQKQRIAIARALV 616
Cdd:PRK13631   118 VSMVFQFPeyQLFKDTIEKDIMFGPVALGVKKSE-AKKLAKFYLNKMGLDDSYL----ERSPfGLSGGQKRRVAIAGILA 192
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1149123047  617 RNPKILLLDEATSALDTESEA-VVQVALDKARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKGNHDELMKEKGIY 692
Cdd:PRK13631   193 IQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVLEvADEVIVMDKGKILKTGTPYEIFTDQHII 270
ABC_6TM_LmrA_like cd18551
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ...
781-1078 1.50e-24

Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349995 [Multi-domain]  Cd Length: 289  Bit Score: 105.21  E-value: 1.50e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  781 FVVGVFCAIINGGLQPAFAIIFSKIIgvftriDDPETKRQNSNLFSLLfLALGIISFITFFLQGFTFGKAGEILTKRLRY 860
Cdd:cd18551      1 LILALLLSLLGTAASLAQPLLVKNLI------DALSAGGSSGGLLALL-VALFLLQAVLSALSSYLLGRTGERVVLDLRR 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  861 MVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKgaigsrlAVITQNIANLGTGII-------ISFIYGWQLTLLLLA 933
Cdd:cd18551     74 RLWRRLLRLPVSFFD--RRRSGDLVSRVTNDTTLLR-------ELITSGLPQLVTGVLtvvgavvLMFLLDWVLTLVTLA 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  934 IVPIIAIAGVVEMKMLSGQALKDKKELEGSGKIATEAIENFRTVVSLTQEQKFEHMYAQSLQVPYRNSLRKAHIFGITFS 1013
Cdd:cd18551    145 VVPLAFLIILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGP 224
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1149123047 1014 FTQAMMYFSYAGCFRFGAYLVAHKLMSFED----VLLVFSAVvfgaMAVGQVSSFAPDYAKAKISAAHI 1078
Cdd:cd18551    225 LMGLAVQLALLVVLGVGGARVASGALTVGTlvafLLYLFQLI----TPLSQLSSFFTQLQKALGALERI 289
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
1105-1332 1.93e-24

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 105.10  E-value: 1.93e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1105 VTFGEVVFNYptRPDIP----VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEI----KRLNV 1176
Cdd:PRK13634     3 ITFQKVEHRY--QYKTPferrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkKNKKL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1177 QWLRAHLGIVSQ--EPILFDCSIAENIAYGDNSRVVSQEEIVRAAKEAnihafIE--SLPNKYSTKvgdKGTQLSGGQKQ 1252
Cdd:PRK13634    81 KPLRKKVGIVFQfpEHQLFEETVEKDICFGPMNFGVSEEDAKQKAREM-----IElvGLPEELLAR---SPFELSGGQMR 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1253 RIAIARALVRQPHILLLDEATSALDTESEKVVQE---ALDKaREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQ 1328
Cdd:PRK13634   153 RVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEmfyKLHK-EKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPR 231

                   ....
gi 1149123047 1329 QLLA 1332
Cdd:PRK13634   232 EIFA 235
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
1122-1325 2.22e-24

ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213231 [Multi-domain]  Cd Length: 211  Bit Score: 102.66  E-value: 2.22e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1122 VLQGLSLEVKKGQTlALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRlNVQWLRAHLGIVSQEPILFD-CSIAEN 1200
Cdd:cd03264     15 ALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGYLPQEFGVYPnFTVREF 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1201 IAY-----GDNSRVVsQEEIVRAAKEANihafiesLPNKYSTKVGdkgtQLSGGQKQRIAIARALVRQPHILLLDEATSA 1275
Cdd:cd03264     93 LDYiawlkGIPSKEV-KARVDEVLELVN-------LGDRAKKKIG----SLSGGMRRRVGIAQALVGDPSILIVDEPTAG 160
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1149123047 1276 LDTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHG 1325
Cdd:cd03264    161 LDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
1121-1333 2.74e-24

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 104.40  E-value: 2.74e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1121 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQW-LRAHLGIVSQEPilfDCSIA- 1198
Cdd:PRK13633    24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWdIRNKAGMVFQNP---DNQIVa 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1199 ----ENIAYGDNSRVVSQEEIVR----AAKEANIHAFIESLPNkystkvgdkgtQLSGGQKQRIAIARALVRQPHILLLD 1270
Cdd:PRK13633   101 tiveEDVAFGPENLGIPPEEIRErvdeSLKKVGMYEYRRHAPH-----------LLSGGQKQRVAIAGILAMRPECIIFD 169
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1149123047 1271 EATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQ 1333
Cdd:PRK13633   170 EPTAMLDPSGRREVVNTIKElnKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFKE 234
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
480-685 2.79e-24

Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213232 [Multi-domain]  Cd Length: 220  Bit Score: 102.45  E-value: 2.79e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  480 LKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDI--RTINVrflREIIGVVSQEPvlfattIAEN 557
Cdd:cd03265     16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVvrEPREV---RRRIGIVFQDL------SVDD 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  558 IRYGRENVTM---------DEIEKAVKEANAYdfiMKLPHKFDTLVGergaQLSGGQKQRIAIARALVRNPKILLLDEAT 628
Cdd:cd03265     87 ELTGWENLYIharlygvpgAERRERIDELLDF---VGLLEAADRLVK----TYSGGMRRRLEIARSLVHRPEVLFLDEPT 159
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  629 SALDTESEAVVQVALDK--ARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKGNHDEL 685
Cdd:cd03265    160 IGLDPQTRAHVWEYIEKlkEEFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
ABC_6TM_LmrA_like cd18551
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ...
212-435 3.75e-24

Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349995 [Multi-domain]  Cd Length: 289  Bit Score: 104.05  E-value: 3.75e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  212 RQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQSMATFFTGFIVGFTRGWKLTLVILAI 291
Cdd:cd18551     66 RVVLDLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAV 145
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  292 SPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKRIGIKKAITANISIGA 371
Cdd:cd18551    146 VPLAFLIILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPL 225
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1149123047  372 AFLLIYASYALAFWYGTTLVLSGEYSIGQVLTVFFSVLIGAFSVGQASPSIEAFANARGAAYEI 435
Cdd:cd18551    226 MGLAVQLALLVVLGVGGARVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGALERI 289
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
460-658 3.96e-24

ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 108.74  E-value: 3.96e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  460 GNLEFRNVHFSYPSRKEvkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSV-DGQDirtinVRFLre 538
Cdd:COG4178    361 GALALEDLTLRTPDGRP--LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGAR-----VLFL-- 431
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  539 iigvvSQEPVLFATTIAENIRY--GRENVTMDEIEKAVKEANaydfimkLPH---KFDTlVGERGAQLSGGQKQRIAIAR 613
Cdd:COG4178    432 -----PQRPYLPLGTLREALLYpaTAEAFSDAELREALEAVG-------LGHlaeRLDE-EADWDQVLSLGEQQRLAFAR 498
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1149123047  614 ALVRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHR 658
Cdd:COG4178    499 LLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR 543
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
462-689 4.15e-24

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 103.95  E-value: 4.15e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSRK--EVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDI----RTINVRF 535
Cdd:PRK13634     3 ITFQKVEHRYQYKTpfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkKNKKLKP 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  536 LREIIGVVSQ--EPVLFATTIAENIRYGRENVTMDEiEKAVKEANAYDFIMKLPHK------FDtlvgergaqLSGGQKQ 607
Cdd:PRK13634    83 LRKKVGIVFQfpEHQLFEETVEKDICFGPMNFGVSE-EDAKQKAREMIELVGLPEEllarspFE---------LSGGQMR 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  608 RIAIARALVRNPKILLLDEATSALDTES-EAVVQV--ALDKaRKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKGNHD 683
Cdd:PRK13634   153 RVAIAGVLAMEPEVLVLDEPTAGLDPKGrKEMMEMfyKLHK-EKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPR 231

                   ....*.
gi 1149123047  684 ELMKEK 689
Cdd:PRK13634   232 EIFADP 237
ABC_6TM_YknU_like cd18542
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ...
781-1078 4.35e-24

Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349986 [Multi-domain]  Cd Length: 292  Bit Score: 104.05  E-value: 4.35e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  781 FVVGVFCAIINGglqpAFAIIFSKIIGVFtrIDD--PETKRQNSNLFSLLFLALGIISFITFFLQGFTFGKAGEILTKRL 858
Cdd:cd18542      1 YLLAILALLLAT----ALNLLIPLLIRRI--IDSviGGGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDL 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  859 RYMVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIGSRLAVITQNIANLGTGIIISFIYGWQLTLLLLAIVPII 938
Cdd:cd18542     75 RNDLYDHLQRLSFSFHD--KARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFI 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  939 AIAGVVEMKMLsGQALKDKKELEGS-GKIATEAIENFRTVVSLTQE----QKFEHMYAQslqvpYRN-SLRKAHIFGITF 1012
Cdd:cd18542    153 ALFSYVFFKKV-RPAFEEIREQEGElNTVLQENLTGVRVVKAFAREdyeiEKFDKENEE-----YRDlNIKLAKLLAKYW 226
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1149123047 1013 SFTQAMMYFSYAGCFRFGAYLVAHKLMSFeDVLLVFSAVVFG-AMAVGQVSSFAPDYAKAKISAAHI 1078
Cdd:cd18542    227 PLMDFLSGLQIVLVLWVGGYLVINGEITL-GELVAFISYLWMlIWPVRQLGRLINDMSRASASAERI 292
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
1122-1333 4.52e-24

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 103.12  E-value: 4.52e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1122 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIK-------------RLNVQWLRAHLGIVSQ 1188
Cdd:PRK10619    20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvadKNQLRLLRTRLTMVFQ 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1189 EPILFD-CSIAENI--AYGDNSRVVSQEEIVRAAKEANIHAFIESLPNKYSTkvgdkgtQLSGGQKQRIAIARALVRQPH 1265
Cdd:PRK10619   100 HFNLWShMTVLENVmeAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPV-------HLSGGQQQRVSIARALAMEPE 172
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1266 ILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQNADLIVVF-QNGRVKEHGTHQQLLAQ 1333
Cdd:PRK10619   173 VLLFDEPTSALDPELVGEVLRIMQQlAEEGKTMVVVTHEMGFARHVSSHVIFlHQGKIEEEGAPEQLFGN 242
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
464-766 4.73e-24

ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 107.84  E-value: 4.73e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  464 FRNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGqdirtiNVRflreiIGVV 543
Cdd:COG0488      1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK------GLR-----IGYL 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  544 SQEPVLFAT-TIAENIRYGRENV--TMDEIEKAVKEANAYDFIM----KLPHKFDTLVG---ERGA-------------- 599
Cdd:COG0488     67 PQEPPLDDDlTVLDTVLDGDAELraLEAELEELEAKLAEPDEDLerlaELQEEFEALGGweaEARAeeilsglgfpeedl 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  600 -----QLSGGQKQRIAIARALVRNPKILLLDEATSALDTES----EAVVqvaldKARKGrTTIVIAH-R--LSTVrnADV 667
Cdd:COG0488    147 drpvsELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESiewlEEFL-----KNYPG-TVLVVSHdRyfLDRV--ATR 218
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  668 IAGFDDGVIVE-KGNHDELMkekgiyfklvtmqtagnevelenaadESKSEIDALEMSSNDSRSSLIRK------RSTRR 740
Cdd:COG0488    219 ILELDRGKLTLyPGNYSAYL--------------------------EQRAERLEQEAAAYAKQQKKIAKeeefirRFRAK 272
                          330       340
                   ....*....|....*....|....*...
gi 1149123047  741 SVRGSQAQDRKlstK--EALDESIPPVS 766
Cdd:COG0488    273 ARKAKQAQSRI---KalEKLEREEPPRR 297
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
462-685 5.63e-24

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 103.34  E-value: 5.63e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSRKEVkiLKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIG 541
Cdd:PRK13652     4 IETRDLCYSYSGSKEA--LNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVG 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  542 VVSQEP--VLFATTIAENIRYGRENVTMDE------IEKAVKEANAYDFIMKLPHkfdtlvgergaQLSGGQKQRIAIAR 613
Cdd:PRK13652    82 LVFQNPddQIFSPTVEQDIAFGPINLGLDEetvahrVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAG 150
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1149123047  614 ALVRNPKILLLDEATSALDTESEAVVQVALDK--ARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKGNHDEL 685
Cdd:PRK13652   151 VIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDlpETYGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEI 225
TauB COG4525
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
1113-1302 5.82e-24

ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 443596 [Multi-domain]  Cd Length: 262  Bit Score: 103.02  E-value: 5.82e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1113 NYP-TRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEikrlnVQWLRAHLGIVSQEPI 1191
Cdd:COG4525     12 RYPgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVP-----VTGPGADRGVVFQKDA 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1192 LFD-CSIAENIAYGDNSRVVSQEEIVRAAKEanihafieslpnkYSTKVGDKGT------QLSGGQKQRIAIARALVRQP 1264
Cdd:COG4525     87 LLPwLNVLDNVAFGLRLRGVPKAERRARAEE-------------LLALVGLADFarrriwQLSGGMRQRVGIARALAADP 153
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1149123047 1265 HILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAH 1302
Cdd:COG4525    154 RFLLMDEPFGALDALTREQMQELLLDvwQRTGKGVFLITH 193
PTZ00243 PTZ00243
ABC transporter; Provisional
445-696 5.93e-24

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 110.25  E-value: 5.93e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  445 IDSYSKSGHKPDNIK-GNLEFRNVHFSYpsRKEVK-ILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVS 522
Cdd:PTZ00243  1291 IEPASPTSAAPHPVQaGSLVFEGVQMRY--REGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIR 1368
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  523 VDGQDIRTINVRFLREIIGVVSQEPVLFATTIAENIRYGREnVTMDEIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLS 602
Cdd:PTZ00243  1369 VNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVDPFLE-ASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYS 1447
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  603 GGQKQRIAIARALV-RNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGN 681
Cdd:PTZ00243  1448 VGQRQLMCMARALLkKGSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGS 1527
                          250
                   ....*....|....*.
gi 1149123047  682 HDEL-MKEKGIYFKLV 696
Cdd:PTZ00243  1528 PRELvMNRQSIFHSMV 1543
cbiO PRK13641
energy-coupling factor transporter ATPase;
1113-1334 6.75e-24

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 103.37  E-value: 6.75e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1113 NYPTRPDIPV----LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIK----RLNVQWLRAHLG 1184
Cdd:PRK13641     9 DYIYSPGTPMekkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKKLRKKVS 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1185 IVSQ--EPILFDCSIAENIAYGDNSRVVSQEEivraAKEANIhafieslpnKYSTKVG------DKGT-QLSGGQKQRIA 1255
Cdd:PRK13641    89 LVFQfpEAQLFENTVLKDVEFGPKNFGFSEDE----AKEKAL---------KWLKKVGlsedliSKSPfELSGGQMRRVA 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1256 IARALVRQPHILLLDEATSALDTESEK-VVQEALDKAREGRTCIVIAHRLSTI-QNADLIVVFQNGRVKEHGTHQQLLAQ 1333
Cdd:PRK13641   156 IAGVMAYEPEILCLDEPAAGLDPEGRKeMMQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKLIKHASPKEIFSD 235

                   .
gi 1149123047 1334 K 1334
Cdd:PRK13641   236 K 236
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
466-674 6.99e-24

ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.


Pssm-ID: 213257 [Multi-domain]  Cd Length: 218  Bit Score: 101.25  E-value: 6.99e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  466 NVHFSYPSrkEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMV--------SVDGQDIRTINvrflR 537
Cdd:cd03290      5 NGYFSWGS--GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnknesEPSFEATRSRN----R 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  538 EIIGVVSQEPVLFATTIAENIRYGreNVTMDEIEKAVKEANAYD-FIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALV 616
Cdd:cd03290     79 YSVAYAAQKPWLLNATVEENITFG--SPFNKQRYKAVTDACSLQpDIDLLPFGDQTEIGERGINLSGGQRQRICVARALY 156
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1149123047  617 RNPKILLLDEATSALDTE-SEAVVQVALDKARKG--RTTIVIAHRLSTVRNADVIAGFDDG 674
Cdd:cd03290    157 QNTNIVFLDDPFSALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
462-683 7.19e-24

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 102.01  E-value: 7.19e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDG------QDIRTINVRF 535
Cdd:PRK11124     3 IQLNGINCFYGAHQ---ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAIRE 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  536 LREIIGVVSQEPVLFA-TTIAENIRYGRENVT-MDEiEKAVKEAnaydfiMKLphkFDTLVGERGA-----QLSGGQKQR 608
Cdd:PRK11124    80 LRRNVGMVFQQYNLWPhLTVQQNLIEAPCRVLgLSK-DQALARA------EKL---LERLRLKPYAdrfplHLSGGQQQR 149
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1149123047  609 IAIARALVRNPKILLLDEATSALDTESEA-VVQVALDKARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKGNHD 683
Cdd:PRK11124   150 VAIARALMMEPQVLLFDEPTAALDPEITAqIVSIIRELAETGITQVIVTHEVEVARKtASRVVYMENGHIVEQGDAS 226
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
1122-1330 8.81e-24

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 104.78  E-value: 8.81e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1122 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQwlRAHLGIVSQEPILF-DCSIAEN 1200
Cdd:PRK10851    17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHAR--DRKVGFVFQHYALFrHMTVFDN 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1201 IAYG---------DNSRVVSQE-----EIVRaakeanihafIESLPNKYSTkvgdkgtQLSGGQKQRIAIARALVRQPHI 1266
Cdd:PRK10851    95 IAFGltvlprrerPNAAAIKAKvtqllEMVQ----------LAHLADRYPA-------QLSGGQKQRVALARALAVEPQI 157
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1149123047 1267 LLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAH-RLSTIQNADLIVVFQNGRVKEHGTHQQL 1330
Cdd:PRK10851   158 LLLDEPFGALDAQVRKELRRWLRQLHEelKFTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
1122-1325 9.93e-24

ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213236 [Multi-domain]  Cd Length: 210  Bit Score: 100.82  E-value: 9.93e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1122 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNvqwlRAHLGIVSQEPILF-DCSIAEN 1200
Cdd:cd03269     15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIGYLPEERGLYpKMKVIDQ 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1201 IAYGDNSRVVSQEEIVRAAKEanihaFIESLpnKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTES 1280
Cdd:cd03269     91 LVYLAQLKGLKKEEARRRIDE-----WLERL--ELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVN 163
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1149123047 1281 EKVVQEAL-DKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHG 1325
Cdd:cd03269    164 VELLKDVIrELARAGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
462-680 1.12e-23

ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.


Pssm-ID: 213233 [Multi-domain]  Cd Length: 218  Bit Score: 100.91  E-value: 1.12e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSY-PSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTiNVRFLREII 540
Cdd:cd03266      2 ITADALTKRFrDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  541 GVVSQEPVLFA-TTIAENIRY--GRENVTMDEIEKAVKEanaydFIMKLphKFDTLVGERGAQLSGGQKQRIAIARALVR 617
Cdd:cd03266     81 GFVSDSTGLYDrLTARENLEYfaGLYGLKGDELTARLEE-----LADRL--GMEELLDRRVGGFSTGMRQKVAIARALVH 153
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1149123047  618 NPKILLLDEATSALD-TESEAVVQVALDKARKGRTTIVIAHRLSTV-RNADVIAGFDDGVIVEKG 680
Cdd:cd03266    154 DPPVLLLDEPTTGLDvMATRALREFIRQLRALGKCILFSTHIMQEVeRLCDRVVVLHRGRVVYEG 218
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
1121-1325 1.23e-23

Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.


Pssm-ID: 213180 [Multi-domain]  Cd Length: 194  Bit Score: 99.93  E-value: 1.23e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1121 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL--ERFYDPLAGKVLLDGKEIKRlnvQWLRAHLGIVSQEPILFDC-SI 1197
Cdd:cd03213     23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLDK---RSFRKIIGYVPQDDILHPTlTV 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1198 AENIAYgdnsrvvsqeeivrAAKeanihafiesLpnkystkvgdKGtqLSGGQKQRIAIARALVRQPHILLLDEATSALD 1277
Cdd:cd03213    100 RETLMF--------------AAK----------L----------RG--LSGGERKRVSIALELVSNPSLLFLDEPTSGLD 143
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1149123047 1278 TESEKVVQEALDK-AREGRTCIVIAHRLST--IQNADLIVVFQNGRVKEHG 1325
Cdd:cd03213    144 SSSALQVMSLLRRlADTGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
1121-1334 1.55e-23

Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 101.63  E-value: 1.55e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1121 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEPIL-FDCSIAE 1199
Cdd:PRK11231    16 RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTpEGITVRE 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1200 NIAYGDNSRV-----VSQE--EIVRAAKEAnihAFIESLPNKystkvgdKGTQLSGGQKQRIAIARALVRQPHILLLDEA 1272
Cdd:PRK11231    96 LVAYGRSPWLslwgrLSAEdnARVNQAMEQ---TRINHLADR-------RLTDLSGGQRQRAFLAMVLAQDTPVVLLDEP 165
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1149123047 1273 TSALD----TESEKVVQEAldkAREGRTCIVIAHRLS-TIQNADLIVVFQNGRVKEHGTHQQLLAQK 1334
Cdd:PRK11231   166 TTYLDinhqVELMRLMREL---NTQGKTVVTVLHDLNqASRYCDHLVVLANGHVMAQGTPEEVMTPG 229
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
480-686 1.67e-23

proline/glycine betaine ABC transporter ATP-binding protein ProV;


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 104.73  E-value: 1.67e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  480 LKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREI----IGVVSQEPVLFA-TTI 554
Cdd:PRK10070    44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVrrkkIAMVFQSFALMPhMTV 123
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  555 AENIRYGREnvtMDEIEKAVKEANAYDFIMKLphKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTE 634
Cdd:PRK10070   124 LDNTAFGME---LAGINAEERREKALDALRQV--GLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1149123047  635 SEAVVQVALDK--ARKGRTTIVIAHRL-STVRNADVIAGFDDGVIVEKGNHDELM 686
Cdd:PRK10070   199 IRTEMQDELVKlqAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
483-680 1.75e-23

ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213265 [Multi-domain]  Cd Length: 211  Bit Score: 99.87  E-value: 1.75e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  483 LNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRflREIIGVVSQEPVLFA-TTIAENIRYG 561
Cdd:cd03298     17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVSMLFQENNLFAhLTVEQNVGLG 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  562 R------ENVTMDEIEKAVKEANAYDFIMKLPhkfdtlvgergAQLSGGQKQRIAIARALVRNPKILLLDEATSALDT-- 633
Cdd:cd03298     95 LspglklTAEDRQAIEVALARVGLAGLEKRLP-----------GELSGGERQRVALARVLVRDKPVLLLDEPFAALDPal 163
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 1149123047  634 ESEAVVQVALDKARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKG 680
Cdd:cd03298    164 RAEMLDLVLDLHAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
1110-1321 1.88e-23

ABC-type uncharacterized transport system, ATPase component [General function prediction only];


Pssm-ID: 440718 [Multi-domain]  Cd Length: 264  Bit Score: 101.32  E-value: 1.88e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1110 VVFNYPTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVqWLRA-HLGIVSQ 1188
Cdd:COG1101      9 KTFNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPE-YKRAkYIGRVFQ 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1189 EPILFDC---SIAEN--IAYGDNSRvvsqEEIVRAAKEANIHAFIES-------LPNKYSTKVGdkgtQLSGGQKQRIAI 1256
Cdd:COG1101     88 DPMMGTApsmTIEENlaLAYRRGKR----RGLRRGLTKKRRELFRELlatlglgLENRLDTKVG----LLSGGQRQALSL 159
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1149123047 1257 ARALVRQPHILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVFQNGRV 1321
Cdd:COG1101    160 LMATLTKPKLLLLDEHTAALDPKTAALVLELTEKivEENNLTTLMVTHNMEqALDYGNRLIMMHEGRI 227
ABC_6TM_ABCB9_like cd18784
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ...
182-422 1.92e-23

Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit.


Pssm-ID: 350057 [Multi-domain]  Cd Length: 289  Bit Score: 102.00  E-value: 1.92e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  182 TRYAYYYSGIGAGVLVAAYIQVSFWCLAAGRQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIG 261
Cdd:cd18784     36 SRAIIIMGLLAIASSVAAGIRGGLFTLAMARLNIRIRNLLFRSIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLN 115
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  262 MFFQSMATFFTGFIVGFTRGWKLTLVILAISPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQK 341
Cdd:cd18784    116 IFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYYKKLSKAVQDSLAKANEVAEETISSIRTVRSFANED 195
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  342 KELERYNKNLEEAKRIGIKKAITANISIGAAFLLIYASYALAFWYGTTLVLSGEYSIGQvltvFFSVLIGAFSVGQASPS 421
Cdd:cd18784    196 GEANRYSEKLKDTYKLKIKEALAYGGYVWSNELTELALTVSTLYYGGHLVITGQISGGN----LISFILYQLELGSCLES 271

                   .
gi 1149123047  422 I 422
Cdd:cd18784    272 V 272
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
1119-1325 1.99e-23

ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.


Pssm-ID: 213235 [Multi-domain]  Cd Length: 208  Bit Score: 99.60  E-value: 1.99e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1119 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWlrAHLGIVSQEPILFD-CSI 1197
Cdd:cd03268     12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAL--RRIGALIEAPGFYPnLTA 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1198 AENIAYGDNSRVVSQEEIVRAAKEANIHAfieslpnkystkVGDKGT-QLSGGQKQRIAIARALVRQPHILLLDEATSAL 1276
Cdd:cd03268     90 RENLRLLARLLGIRKKRIDEVLDVVGLKD------------SAKKKVkGFSLGMKQRLGIALALLGNPDLLILDEPTNGL 157
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1149123047 1277 DTESEKVVQEAL-DKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHG 1325
Cdd:cd03268    158 DPDGIKELRELIlSLRDQGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
462-663 2.23e-23

ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 105.88  E-value: 2.23e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSrkeVKILKGLNLKVQSGQTVALVGNSGCGKSTtvqLMQRL---YDPTEGMVSVDGQDirtinVRF--- 535
Cdd:COG3845      6 LELRGITKRFGG---VVANDDVSLTVRPGEIHALLGENGAGKST---LMKILyglYQPDSGEILIDGKP-----VRIrsp 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  536 ---LREIIGVVSQEPVLFAT-TIAENIRYGRENVT-----MDEIEKAVKE-ANAYDFIMKLphkfDTLVGergaQLSGGQ 605
Cdd:COG3845     75 rdaIALGIGMVHQHFMLVPNlTVAENIVLGLEPTKggrldRKAARARIRElSERYGLDVDP----DAKVE----DLSVGE 146
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  606 KQRIAIARALVRNPKILLLDEATSAL-DTESEAVVQVaLDK-ARKGRTTIVIAHRLSTVR 663
Cdd:COG3845    147 QQRVEILKALYRGARILILDEPTAVLtPQEADELFEI-LRRlAAEGKSIIFITHKLREVM 205
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
475-680 3.06e-23

ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.


Pssm-ID: 213235 [Multi-domain]  Cd Length: 208  Bit Score: 99.21  E-value: 3.06e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  475 KEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDI-RTINVRflrEIIGVVSQEPVLFAT- 552
Cdd:cd03268     11 GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYqKNIEAL---RRIGALIEAPGFYPNl 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  553 TIAENIR-----YGRENVTMDEIEKAVKEANAydfimklPHKfdtlvgeRGAQLSGGQKQRIAIARALVRNPKILLLDEA 627
Cdd:cd03268     88 TARENLRllarlLGIRKKRIDEVLDVVGLKDS-------AKK-------KVKGFSLGMKQRLGIALALLGNPDLLILDEP 153
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1149123047  628 TSALDTES-EAVVQVALDKARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKG 680
Cdd:cd03268    154 TNGLDPDGiKELRELILSLRDQGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
SapF COG4167
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
462-686 3.53e-23

ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];


Pssm-ID: 443328 [Multi-domain]  Cd Length: 265  Bit Score: 100.68  E-value: 3.53e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSY------PSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRF 535
Cdd:COG4167      5 LEVRNLSKTFkyrtglFRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKY 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  536 LREIIGVVSQEPvlfATTIAENIRYG-------RENVTMDEIEKAVKeanaydfImklphkFDTL--VGERGAQ------ 600
Cdd:COG4167     85 RCKHIRMIFQDP---NTSLNPRLNIGqileeplRLNTDLTAEEREER-------I------FATLrlVGLLPEHanfyph 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  601 -LSGGQKQRIAIARALVRNPKILLLDEATSALDTESEA-VVQVALD-KARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVI 676
Cdd:COG4167    149 mLSSGQKQRVALARALILQPKIIIADEALAALDMSVRSqIINLMLElQEKLGISYIYVSQHLGIVKHiSDKVLVMHQGEV 228
                          250
                   ....*....|
gi 1149123047  677 VEKGNHDELM 686
Cdd:COG4167    229 VEYGKTAEVF 238
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
462-680 3.70e-23

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 100.30  E-value: 3.70e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYD-----PTEGMVSVDGQDIRTINVRFL 536
Cdd:PRK14267     5 IETVNLRVYYGSNH---VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSPDVDPI 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  537 --REIIGVVSQEPVLFA-TTIAENIRYG-------RENVTMDE-IEKAVKEANAYDfimklphKFDTLVGERGAQLSGGQ 605
Cdd:PRK14267    82 evRREVGMVFQYPNPFPhLTIYDNVAIGvklnglvKSKKELDErVEWALKKAALWD-------EVKDRLNDYPSNLSGGQ 154
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1149123047  606 KQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHR-LSTVRNADVIAGFDDGVIVEKG 680
Cdd:PRK14267   155 RQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVG 230
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
479-685 4.71e-23

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 100.12  E-value: 4.71e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  479 ILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQ------DIRTINVRFLREIIGVVSQEPVLFA- 551
Cdd:PRK14246    25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQPNPFPh 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  552 TTIAENIRYGRENVTMD---EIEKAVKEANAYDFIMKLPHkfDTLvGERGAQLSGGQKQRIAIARALVRNPKILLLDEAT 628
Cdd:PRK14246   105 LSIYDNIAYPLKSHGIKekrEIKKIVEECLRKVGLWKEVY--DRL-NSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1149123047  629 SALDTESEAVVQVALDKARKGRTTIVIAHRLSTV-RNADVIAGFDDGVIVEKGNHDEL 685
Cdd:PRK14246   182 SMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEI 239
SufC COG0396
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ...
1119-1326 6.54e-23

Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440165 [Multi-domain]  Cd Length: 245  Bit Score: 99.37  E-value: 6.54e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1119 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL---ERfYDPLAGKVLLDGKEIKRLNVQwLRAHLGI-VS-QEPIlf 1193
Cdd:COG0396     12 GKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmghPK-YEVTSGSILLDGEDILELSPD-ERARAGIfLAfQYPV-- 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1194 dcsiaeniaygdnsRV--VSQEEIVRAAKEAN------IHAFIESLpNKYSTKVG----------DKGtqLSGGQKQRIA 1255
Cdd:COG0396     88 --------------EIpgVSVSNFLRTALNARrgeelsAREFLKLL-KEKMKELGldedfldryvNEG--FSGGEKKRNE 150
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1149123047 1256 IARALVRQPHILLLDEATSALDTESEKVVQEALDKAR-EGRTCIVIAH--RLSTIQNADLIVVFQNGRVKEHGT 1326
Cdd:COG0396    151 ILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRsPDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGG 224
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
1111-1337 6.58e-23

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 101.47  E-value: 6.58e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1111 VFNYPTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQ-------------LLERFY-----DPLAGKVLLDGKEIK 1172
Cdd:PRK13631    30 VFDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVThfnglikskygtiQVGDIYigdkkNNHELITNPYSKKIK 109
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1173 rlNVQWLRAHLGIVSQEP--ILFDCSIAENIAYGDNSRVVSQEEIVRAAKeanihafieslpnKYSTKVGDKGT------ 1244
Cdd:PRK13631   110 --NFKELRRRVSMVFQFPeyQLFKDTIEKDIMFGPVALGVKKSEAKKLAK-------------FYLNKMGLDDSylersp 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1245 -QLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEK-VVQEALDKAREGRTCIVIAHRLSTI-QNADLIVVFQNGRV 1321
Cdd:PRK13631   175 fGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVlEVADEVIVMDKGKI 254
                          250
                   ....*....|....*.
gi 1149123047 1322 KEHGTHQQLLAQKGIY 1337
Cdd:PRK13631   255 LKTGTPYEIFTDQHII 270
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
475-676 6.58e-23

Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];


Pssm-ID: 443809 [Multi-domain]  Cd Length: 229  Bit Score: 98.66  E-value: 6.58e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  475 KEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQ----DI-----RTI-NVRflREIIGVVS 544
Cdd:COG4778     22 KRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLaqaspREIlALR--RRTIGYVS 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  545 QepvlFATTIAeniRYGRENVTMDE-IEKAVKEANAYDFIMKLPHKFDtlVGERGAQL-----SGGQKQRIAIARALVRN 618
Cdd:COG4778    100 Q----FLRVIP---RVSALDVVAEPlLERGVDREEARARARELLARLN--LPERLWDLppatfSGGEQQRVNIARGFIAD 170
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1149123047  619 PKILLLDEATSALDTES-EAVVQVALDKARKGRTTIVIAHrlstvrNADVIAGFDDGVI 676
Cdd:COG4778    171 PPLLLLDEPTASLDAANrAVVVELIEEAKARGTAIIGIFH------DEEVREAVADRVV 223
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
1127-1331 7.46e-23

proline/glycine betaine ABC transporter ATP-binding protein ProV;


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 102.80  E-value: 7.46e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1127 SLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWL----RAHLGIVSQE-PILFDCSIAENI 1201
Cdd:PRK10070    48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELrevrRKKIAMVFQSfALMPHMTVLDNT 127
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1202 AYGDNSRVVSQEEIVRAAKEANIHAFIESLPNKYStkvgdkgTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESE 1281
Cdd:PRK10070   128 AFGMELAGINAEERREKALDALRQVGLENYAHSYP-------DELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIR 200
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1149123047 1282 KVVQEALDK--AREGRTCIVIAHRL-STIQNADLIVVFQNGRVKEHGTHQQLL 1331
Cdd:PRK10070   201 TEMQDELVKlqAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
480-657 7.69e-23

nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]


Pssm-ID: 130252 [Multi-domain]  Cd Length: 230  Bit Score: 98.69  E-value: 7.69e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  480 LKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLreiigVVSQEPVLFA-TTIAENI 558
Cdd:TIGR01184    1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPwLTVRENI 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  559 RYGRENVTMD----EIEKAVKEANAYDFIMKLPHKfdtlvgeRGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTE 634
Cdd:TIGR01184   76 ALAVDRVLPDlsksERRAIVEEHIALVGLTEAADK-------RPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAL 148
                          170       180
                   ....*....|....*....|....*
gi 1149123047  635 SEAVVQVALDK--ARKGRTTIVIAH 657
Cdd:TIGR01184  149 TRGNLQEELMQiwEEHRVTVLMVTH 173
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
1122-1325 7.91e-23

ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.


Pssm-ID: 213233 [Multi-domain]  Cd Length: 218  Bit Score: 98.21  E-value: 7.91e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1122 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRlNVQWLRAHLGIVSQEPILFD-CSIAEN 1200
Cdd:cd03266     20 AVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRLGFVSDSTGLYDrLTAREN 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1201 IAY-GDnsrvvsqeeiVRAAKEANIHAFIESLPNKYSTK--VGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALD 1277
Cdd:cd03266     99 LEYfAG----------LYGLKGDELTARLEELADRLGMEelLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLD 168
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1278 TESEKVVQEALDKAREGRTCIVIA-HRLSTIQN-ADLIVVFQNGRVKEHG 1325
Cdd:cd03266    169 VMATRALREFIRQLRALGKCILFStHIMQEVERlCDRVVVLHRGRVVYEG 218
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
1121-1324 8.00e-23

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 99.39  E-value: 8.00e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1121 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEikrlnVQWLRAHLGIVSQ-EPILFDCSIAE 1199
Cdd:PRK11248    15 PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKP-----VEGPGAERGVVFQnEGLLPWRNVQD 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1200 NIAYGDNSRVVSQEEIVRAAKEANIHAFIESLPNKYSTkvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEATSALDTE 1279
Cdd:PRK11248    90 NVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIW-------QLSGGQRQRVGIARALAANPQLLLLDEPFGALDAF 162
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1149123047 1280 SEKVVQEALDK--AREGRTCIVIAHrlsTIQNA-----DLIVVFQN-GRVKEH 1324
Cdd:PRK11248   163 TREQMQTLLLKlwQETGKQVLLITH---DIEEAvfmatELVLLSPGpGRVVER 212
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
494-635 8.37e-23

ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 443319 [Multi-domain]  Cd Length: 358  Bit Score: 101.72  E-value: 8.37e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  494 ALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDG---QDIRT-INVRFLREIIGVVSQEPVLFAT-TIAENIRYGRenvtmd 568
Cdd:COG4148     29 ALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlQDSARgIFLPPHRRRIGYVFQEARLFPHlSVRGNLLYGR------ 102
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1149123047  569 eieKAVKEANAYDfimklphKFDTLVG--------ERG-AQLSGGQKQRIAIARALVRNPKILLLDEATSALDTES 635
Cdd:COG4148    103 ---KRAPRAERRI-------SFDEVVEllgighllDRRpATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLAR 168
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
478-689 9.60e-23

Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 99.32  E-value: 9.60e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  478 KILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIGVVSQEPVL-FATTIAE 556
Cdd:PRK11231    16 RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTpEGITVRE 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  557 NIRYGRE------NVTMDEIEKAVKEAnaydfiMKLPHkFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSA 630
Cdd:PRK11231    96 LVAYGRSpwlslwGRLSAEDNARVNQA------MEQTR-INHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTY 168
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1149123047  631 LDTESeavvQVALDK-----ARKGRTTIVIAHRLSTV-RNADVIAGFDDGVIVEKGNHDELMKEK 689
Cdd:PRK11231   169 LDINH----QVELMRlmrelNTQGKTVVTVLHDLNQAsRYCDHLVVLANGHVMAQGTPEEVMTPG 229
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
1120-1320 1.17e-22

Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];


Pssm-ID: 443809 [Multi-domain]  Cd Length: 229  Bit Score: 98.28  E-value: 1.17e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1120 IPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLdgkeikRLNVQW-------------LRAH-LGI 1185
Cdd:COG4778     24 LPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILV------RHDGGWvdlaqaspreilaLRRRtIGY 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1186 VSQ---------------EPILfdcsiaeniaygdnSRVVSQEEIVRAAKEA----NIHafiESL----PNKYStkvgdk 1242
Cdd:COG4778     98 VSQflrviprvsaldvvaEPLL--------------ERGVDREEARARARELlarlNLP---ERLwdlpPATFS------ 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1243 gtqlsGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIV-IAHRLSTIQN-ADLIVVFQNGR 1320
Cdd:COG4778    155 -----GGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIgIFHDEEVREAvADRVVDVTPFS 229
urea_trans_UrtE TIGR03410
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ...
462-689 1.30e-22

urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 274567 [Multi-domain]  Cd Length: 230  Bit Score: 97.98  E-value: 1.30e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYpsrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDI-RTINVRFLREII 540
Cdd:TIGR03410    1 LEVSNLNVYY---GQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDItKLPPHERARAGI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  541 GVVSQEPVLFAT-TIAENIRYGREnvTMDEIEKAVKeanayDFIMKL-PHKFDTLvGERGAQLSGGQKQRIAIARALVRN 618
Cdd:TIGR03410   78 AYVPQGREIFPRlTVEENLLTGLA--ALPRRSRKIP-----DEIYELfPVLKEML-GRRGGDLSGGQQQQLAIARALVTR 149
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1149123047  619 PKILLLDEATSALD----TESEAVVQvaLDKARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKGNHDELMKEK 689
Cdd:TIGR03410  150 PKLLLLDEPTEGIQpsiiKDIGRVIR--RLRAEGGMAILLVEQYLDFARElADRYYVMERGRVVASGAGDELDEDK 223
ABC_6TM_MsbA_like cd18552
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ...
781-1051 1.91e-22

Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349996 [Multi-domain]  Cd Length: 292  Bit Score: 99.03  E-value: 1.91e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  781 FVVGVFCAIINGGLQPAFAIIFSKIIGVFTRIDDPETKRqnsnLFSLLFLALGIISFITFFLQGFTFGKAGEILTKRLRY 860
Cdd:cd18552      1 LALAILGMILVAATTAALAWLLKPLLDDIFVEKDLEALL----LVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRN 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  861 MVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIGSRLAVITQNIANLGTGIIISFIYGWQLTLLLLAIVPIIAI 940
Cdd:cd18552     77 DLFDKLLRLPLSFFD--RNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAAL 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  941 AGVV---EMKMLSgqalkdKKELEGSGKIAT---EAIENFRTVVSLTQEQKFEHMYAQSLQVPYRNSLRKAHIFGITFSF 1014
Cdd:cd18552    155 PIRRigkRLRKIS------RRSQESMGDLTSvlqETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPL 228
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1149123047 1015 TQAMMYFSYAGCFRFGAYLVAHKLMSFEDVLLVFSAV 1051
Cdd:cd18552    229 MELLGAIAIALVLWYGGYQVISGELTPGEFISFITAL 265
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
1122-1302 1.98e-22

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 98.38  E-value: 1.98e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1122 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD-----PLAGKVLLDGKEIKRLNVQWL--RAHLGIVSQEPILF- 1193
Cdd:PRK14267    19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSPDVDPIevRREVGMVFQYPNPFp 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1194 DCSIAENIAYGD--NSRVVSQEEIVRAAKEANIHAfieSLPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDE 1271
Cdd:PRK14267    99 HLTIYDNVAIGVklNGLVKSKKELDERVEWALKKA---ALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDE 175
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1149123047 1272 ATSALDTESEKVVQEALDKAREGRTCIVIAH 1302
Cdd:PRK14267   176 PTANIDPVGTAKIEELLFELKKEYTIVLVTH 206
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
1127-1334 2.09e-22

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 97.35  E-value: 2.09e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1127 SLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQwlRAHLGIVSQEPILFD-CSIAENIAYGD 1205
Cdd:PRK10771    19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQENNLFShLTVAQNIGLGL 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1206 NSRV---VSQEEIVRA-AKEANIHAFIESLPnkystkvgdkgTQLSGGQKQRIAIARALVRQPHILLLDEATSALD---- 1277
Cdd:PRK10771    97 NPGLklnAAQREKLHAiARQMGIEDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEPFSALDpalr 165
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1149123047 1278 TESEKVVQEALDkaREGRTCIVIAHRLS-TIQNADLIVVFQNGRVKEHGTHQQLLAQK 1334
Cdd:PRK10771   166 QEMLTLVSQVCQ--ERQLTLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDELLSGK 221
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
1122-1321 2.65e-22

White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.


Pssm-ID: 213201 [Multi-domain]  Cd Length: 226  Bit Score: 96.96  E-value: 2.65e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1122 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLE---RFYDPLAGKVLLDGKEIKRlnVQWLRaHLGIVSQEPILFDC-SI 1197
Cdd:cd03234     22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISgrvEGGGTTSGQILFNGQPRKP--DQFQK-CVAYVRQDDILLPGlTV 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1198 AENIAYGDNSR--VVSQEEI--VRAAKEANIHAFIESLPNKYSTkvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEAT 1273
Cdd:cd03234     99 RETLTYTAILRlpRKSSDAIrkKRVEDVLLRDLALTRIGGNLVK-------GISGGERRRVSIAVQLLWDPKVLILDEPT 171
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1149123047 1274 SALDTESE-KVVQEALDKAREGRTCIVIAH--RLSTIQNADLIVVFQNGRV 1321
Cdd:cd03234    172 SGLDSFTAlNLVSTLSQLARRNRIVILTIHqpRSDLFRLFDRILLLSSGEI 222
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
1121-1332 3.20e-22

ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.


Pssm-ID: 213185 [Multi-domain]  Cd Length: 232  Bit Score: 96.84  E-value: 3.20e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1121 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVqWLRAHLGI--VSQEPILF-DCSI 1197
Cdd:cd03218     14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPM-HKRARLGIgyLPQEASIFrKLTV 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1198 AENIAYGDNSRVVSQEEIVRAAkEANIHAF-IESLPNKystkvgdKGTQLSGGQKQRIAIARALVRQPHILLLDEATSAL 1276
Cdd:cd03218     93 EENILAVLEIRGLSKKEREEKL-EELLEEFhITHLRKS-------KASSLSGGERRRVEIARALATNPKFLLLDEPFAGV 164
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1149123047 1277 DTESEKVVQEALDKAREGRTCIVIA-HRLS-TIQNADLIVVFQNGRVKEHGTHQQLLA 1332
Cdd:cd03218    165 DPIAVQDIQKIIKILKDRGIGVLITdHNVReTLSITDRAYIIYEGKVLAEGTPEEIAA 222
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
1114-1333 3.40e-22

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 97.95  E-value: 3.40e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1114 YPTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEP--I 1191
Cdd:PRK13652    11 YSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPddQ 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1192 LFDCSIAENIAYGDNSRVVSQEEIVRAAKEANIHAFIESLPNKYStkvgdkgTQLSGGQKQRIAIARALVRQPHILLLDE 1271
Cdd:PRK13652    91 IFSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVP-------HHLSGGEKKRVAIAGVIAMEPQVLVLDE 163
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1149123047 1272 ATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTI-QNADLIVVFQNGRVKEHGTHQQLLAQ 1333
Cdd:PRK13652   164 PTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEIFLQ 228
SufC COG0396
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ...
462-688 3.64e-22

Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440165 [Multi-domain]  Cd Length: 245  Bit Score: 97.06  E-value: 3.64e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSypsRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQ-LMQR-LYDPTEGMVSVDGQDI--RTINVR--- 534
Cdd:COG0396      1 LEIKNLHVS---VEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKvLMGHpKYEVTSGSILLDGEDIleLSPDERara 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  535 --FL-----REIIGV-VSQepvlFATTIAENIRygRENVTMDEIEKAVKEANAydfIMKLPHKFdtlvGERG--AQLSGG 604
Cdd:COG0396     78 giFLafqypVEIPGVsVSN----FLRTALNARR--GEELSAREFLKLLKEKMK---ELGLDEDF----LDRYvnEGFSGG 144
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  605 QKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKAR-KGRTTIVIAH--RLSTVRNADVIAGFDDGVIVEKGN 681
Cdd:COG0396    145 EKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRsPDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGG 224

                   ....*..
gi 1149123047  682 HdELMKE 688
Cdd:COG0396    225 K-ELALE 230
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
435-659 3.65e-22

cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]


Pssm-ID: 273530 [Multi-domain]  Cd Length: 1490  Bit Score: 104.22  E-value: 3.65e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  435 IFKIIDnKPSIDSYSKSGHKPDNIKGNLEFRNVHFS--YPSRKEV--------------KILKGLNLKVQSGQTVALVGN 498
Cdd:TIGR01271 1175 VFKFID-LPQEEPRPSGGGGKYQLSTVLVIENPHAQkcWPSGGQMdvqgltakyteagrAVLQDLSFSVEGGQRVGLLGR 1253
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  499 SGCGKSTTVQLMQRLYDpTEGMVSVDGQDIRTINVRFLREIIGVVSQEPVLFATTIAENIRyGRENVTMDEIEKAVKEAN 578
Cdd:TIGR01271 1254 TGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLD-PYEQWSDEEIWKVAEEVG 1331
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  579 AYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVIAHR 658
Cdd:TIGR01271 1332 LKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHR 1411

                   .
gi 1149123047  659 L 659
Cdd:TIGR01271 1412 V 1412
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
483-686 4.01e-22

molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]


Pssm-ID: 131197 [Multi-domain]  Cd Length: 354  Bit Score: 99.80  E-value: 4.01e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  483 LNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDG---QDIRT-INVRFLREIIGVVSQEPVLFA-TTIAEN 557
Cdd:TIGR02142   16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlFDSRKgIFLPPEKRRIGYVFQEARLFPhLSVRGN 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  558 IRYGRENVTMDEieKAVKEANAYDfIMKLPHkfdtLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEA 637
Cdd:TIGR02142   96 LRYGMKRARPSE--RRISFERVIE-LLGIGH----LLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKY 168
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1149123047  638 VVQVALDKARK--GRTTIVIAHRLSTV-RNADVIAGFDDGVIVEKGNHDELM 686
Cdd:TIGR02142  169 EILPYLERLHAefGIPILYVSHSLQEVlRLADRVVVLEDGRVAAAGPIAEVW 220
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
479-634 5.07e-22

ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 95.63  E-value: 5.07e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  479 ILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDP---TEGMVSVDGQDIRTINVRfLREIiGVVSQEPVLFA-TTI 554
Cdd:COG4136     16 LLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAE-QRRI-GILFQDDLLFPhLSV 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  555 AENIRYG-RENVTM----DEIEKAVKEANaydfimkLPHKFDTLVgergAQLSGGQKQRIAIARALVRNPKILLLDEATS 629
Cdd:COG4136     94 GENLAFAlPPTIGRaqrrARVEQALEEAG-------LAGFADRDP----ATLSGGQRARVALLRALLAEPRALLLDEPFS 162

                   ....*
gi 1149123047  630 ALDTE 634
Cdd:COG4136    163 KLDAA 167
CeuD COG4604
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ...
463-692 6.03e-22

ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 443654 [Multi-domain]  Cd Length: 252  Bit Score: 96.69  E-value: 6.03e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  463 EFRNVHFSYpsrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIGV 542
Cdd:COG4604      3 EIKNVSKRY---GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAI 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  543 VSQEPVlFAT--TIAENIRYGR-----ENVTmDEIEKAVKEANAYDFIMKLPHKF-DtlvgergaQLSGGQKQRIAIARA 614
Cdd:COG4604     80 LRQENH-INSrlTVRELVAFGRfpyskGRLT-AEDREIIDEAIAYLDLEDLADRYlD--------ELSGGQRQRAFIAMV 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  615 LVRNPKILLLDEATSALDTesEAVVQV--ALDKA--RKGRTTIVIAHRLstvrN-----ADVIAGFDDGVIVEKGNHDEL 685
Cdd:COG4604    150 LAQDTDYVLLDEPLNNLDM--KHSVQMmkLLRRLadELGKTVVIVLHDI----NfascyADHIVAMKDGRVVAQGTPEEI 223
                          250
                   ....*....|
gi 1149123047  686 MKE---KGIY 692
Cdd:COG4604    224 ITPevlSDIY 233
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...
462-678 6.60e-22

ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];


Pssm-ID: 440180 [Multi-domain]  Cd Length: 257  Bit Score: 96.65  E-value: 6.60e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYpsrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRflrEII- 540
Cdd:COG0411      5 LEVRGLTKRF---GGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPH---RIAr 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  541 -GVVS--QEPVLFAT-TIAENIRYGRENVTMDEIEKAV--------KEANAYDFIM------KLPHKFDTLVGErgaqLS 602
Cdd:COG0411     79 lGIARtfQNPRLFPElTVLENVLVAAHARLGRGLLAALlrlprarrEEREARERAEellervGLADRADEPAGN----LS 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  603 GGQKQRIAIARALVRNPKILLLDEATSAL-DTESEAVVQVALD-KARKGRTTIVIAHRLSTVRN-ADVIAGFDDG-VIVE 678
Cdd:COG0411    155 YGQQRRLEIARALATEPKLLLLDEPAAGLnPEETEELAELIRRlRDERGITILLIEHDMDLVMGlADRIVVLDFGrVIAE 234
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
1116-1323 9.11e-22

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 96.68  E-value: 9.11e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1116 TRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLN----------VQWL------ 1179
Cdd:PRK10419    21 KHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqrkafrrdIQMVfqdsis 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1180 ----RAHLGIVSQEPI--LFDCSIAENIAygdnsRVvsqEEIVRAAKEANIHAfiESLPnkystkvgdkgTQLSGGQKQR 1253
Cdd:PRK10419   101 avnpRKTVREIIREPLrhLLSLDKAERLA-----RA---SEMLRAVDLDDSVL--DKRP-----------PQLSGGQLQR 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1149123047 1254 IAIARALVRQPHILLLDEATSALDteseKVVQ-EALD-----KAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKE 1323
Cdd:PRK10419   160 VCLARALAVEPKLLILDEAVSNLD----LVLQaGVIRllkklQQQFGTACLFITHDLRLVERfCQRVMVMDNGQIVE 232
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
1116-1331 9.40e-22

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 99.53  E-value: 9.40e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1116 TRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEPIL-FD 1194
Cdd:PRK09536    12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFE 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1195 CSIAENIAYGDN---SRVVSQEEIVRAAKEanihafiESLPNKYSTKVGDKG-TQLSGGQKQRIAIARALVRQPHILLLD 1270
Cdd:PRK09536    92 FDVRQVVEMGRTphrSRFDTWTETDRAAVE-------RAMERTGVAQFADRPvTSLSGGERQRVLLARALAQATPVLLLD 164
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1149123047 1271 EATSALDTESE----KVVQEALDkarEGRTCIVIAHRLS-TIQNADLIVVFQNGRVKEHGTHQQLL 1331
Cdd:PRK09536   165 EPTASLDINHQvrtlELVRRLVD---DGKTAVAAIHDLDlAARYCDELVLLADGRVRAAGPPADVL 227
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
462-659 1.01e-21

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 100.46  E-value: 1.01e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSrkeVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREI-I 540
Cdd:PRK10762     5 LQLKGIDKAFPG---VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAgI 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  541 GVVSQEPVLFAT-TIAENIRYGRENVT-MDEIE--KAVKEANAYDFIMKLPHKFDTLVGErgaqLSGGQKQRIAIARALV 616
Cdd:PRK10762    82 GIIHQELNLIPQlTIAENIFLGREFVNrFGRIDwkKMYAEADKLLARLNLRFSSDKLVGE----LSIGEQQMVEIAKVLS 157
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1149123047  617 RNPKILLLDEATSAL-DTESEAVVQVALDKARKGRTTIVIAHRL 659
Cdd:PRK10762   158 FESKVIIMDEPTDALtDTETESLFRVIRELKSQGRGIVYISHRL 201
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
1121-1317 1.14e-21

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 95.17  E-value: 1.14e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1121 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEPILFDCSIAEN 1200
Cdd:PRK10247    21 KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTVYDN 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1201 IAYGDNSRVVSQEEivrAAKEANIHAFieSLPNKYSTKvgdKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTES 1280
Cdd:PRK10247   101 LIFPWQIRNQQPDP---AIFLDDLERF--ALPDTILTK---NIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESN 172
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1149123047 1281 EKVVQEALDK-AREGRTCIV-IAHRLSTIQNADLIVVFQ 1317
Cdd:PRK10247   173 KHNVNEIIHRyVREQNIAVLwVTHDKDEINHADKVITLQ 211
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
479-692 1.16e-21

ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.


Pssm-ID: 213256 [Multi-domain]  Cd Length: 275  Bit Score: 96.46  E-value: 1.16e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  479 ILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDpTEGMVSVDGQDIRTINVRFLREIIGVVSQEPVLFATTIAENI 558
Cdd:cd03289     19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTFRKNL 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  559 R-YGRENvtMDEIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEA 637
Cdd:cd03289     98 DpYGKWS--DEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQ 175
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1149123047  638 VVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELMKEKGIY 692
Cdd:cd03289    176 VIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHF 230
PTZ00243 PTZ00243
ABC transporter; Provisional
1114-1348 1.33e-21

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 102.55  E-value: 1.33e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1114 YPTRPDIpVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVlldgkeikrlnvqWLRAHLGIVSQEPILF 1193
Cdd:PTZ00243   668 FELEPKV-LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-------------WAERSIAYVPQQAWIM 733
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1194 DCSIAENIAYGDNSRVVSQEEIVRAAKeanIHAFIESLPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEAT 1273
Cdd:PTZ00243   734 NATVRGNILFFDEEDAARLADAVRVSQ---LEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPL 810
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1149123047 1274 SALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQlLAQKGIYFSMVSVQAGTK 1348
Cdd:PTZ00243   811 SALDAHvGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSAD-FMRTSLYATLAAELKENK 885
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
462-680 1.66e-21

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 100.16  E-value: 1.66e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSRK--------EVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYdPTEGMVSVDGQDIRTINV 533
Cdd:PRK15134   276 LDVEQLQVAFPIRKgilkrtvdHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNR 354
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  534 RFL---REIIGVVSQEP---------VLfaTTIAENIRYGRENVTMDEIEKAVKEAnaydfiMK-------LPHKFDtlv 594
Cdd:PRK15134   355 RQLlpvRHRIQVVFQDPnsslnprlnVL--QIIEEGLRVHQPTLSAAQREQQVIAV------MEevgldpeTRHRYP--- 423
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  595 gergAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVqVALDKARKGR---TTIVIAHRLSTVRNA--DVIA 669
Cdd:PRK15134   424 ----AEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQI-LALLKSLQQKhqlAYLFISHDLHVVRALchQVIV 498
                          250
                   ....*....|.
gi 1149123047  670 gFDDGVIVEKG 680
Cdd:PRK15134   499 -LRQGEVVEQG 508
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
778-1334 1.84e-21

cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]


Pssm-ID: 273530 [Multi-domain]  Cd Length: 1490  Bit Score: 101.91  E-value: 1.84e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  778 WPYFVVGVFCAI--INGGLQPafaIIFSKIIGVFtridDPETKRQNSNLFsllFLALGI-ISFI--TFFLQGFTFG--KA 850
Cdd:TIGR01271   80 WRFVFYGILLYFgeATKAVQP---LLLGRIIASY----DPFNAPEREIAY---YLALGLcLLFIvrTLLLHPAIFGlhHL 149
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  851 GEILTKRLRYMVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIGSRLAVItqnIANLGTGIIISFIygWQLT-- 928
Cdd:TIGR01271  150 GMQMRIALFSLIYKKTLKLSSRVLD--KISTGQLVSLLSNNLNKFDEGLALAHFVW---IAPLQVILLMGLI--WELLev 222
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  929 --------LLLLAIVPiiAIAGVVEMKMLSGQALKDKKELegsgKIATEAIENFRTVVSLTQEQKFEHMYAQSLQVPYRN 1000
Cdd:TIGR01271  223 ngfcglgfLILLALFQ--ACLGQKMMPYRDKRAGKISERL----AITSEIIENIQSVKAYCWEEAMEKIIKNIRQDELKL 296
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1001 SlRKAhifGITFSFTQAMMYFSyaGCFRFGAYLVAHKLMSFEDVLLVFSAVVFGAMAVGQVSSFAPDYAKAKISAAHIIM 1080
Cdd:TIGR01271  297 T-RKI---AYLRYFYSSAFFFS--GFFVVFLSVVPYALIKGIILRRIFTTISYCIVLRMTVTRQFPGAIQTWYDSLGAIT 370
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1081 IIEKTPLIDSYSTEGLMPNTLE---GNVT------FGEVV--------------------FNYPTRPDIPVLQGLSLEVK 1131
Cdd:TIGR01271  371 KIQDFLCKEEYKTLEYNLTTTEvemVNVTaswdegIGELFekikqnnkarkqpngddglfFSNFSLYVTPVLKNISFKLE 450
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1132 KGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKeikrlnvqwlrahLGIVSQEPILFDCSIAENIAYG---DNSR 1208
Cdd:TIGR01271  451 KGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQTSWIMPGTIKDNIIFGlsyDEYR 517
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1209 VVSqeeIVRAAK-EANIHAFieslPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEA 1287
Cdd:TIGR01271  518 YTS---VIKACQlEEDIALF----PEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFES 590
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....*...
gi 1149123047 1288 -LDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQK 1334
Cdd:TIGR01271  591 cLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKR 638
ABC_6TM_TmrA_like cd18544
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ...
781-1041 1.87e-21

Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349988 [Multi-domain]  Cd Length: 294  Bit Score: 96.30  E-value: 1.87e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  781 FVVGVFCAIINGGLQPAFAIIFSKIIGVFtrIDDPETKRQNSNLFSLLFLALGIISFITFFLQGFTFGKAGEILTKRLRY 860
Cdd:cd18544      1 FILALLLLLLATALELLGPLLIKRAIDDY--IVPGQGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRR 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  861 MVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIGSRLAVITQNIANLGTGIIISFIYGWQLTLLLLAIVPIIAI 940
Cdd:cd18544     79 DLFSHIQRLPLSFFD--RTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLL 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  941 AGVVeMKMLSGQALKDKKEL--EGSGKIAtEAIENFRTVVSLTQEQKFEHMYAQSLQVPYRNSLRKAHIFGITFSFTQAM 1018
Cdd:cd18544    157 ATYL-FRKKSRKAYREVREKlsRLNAFLQ-ESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELL 234
                          250       260
                   ....*....|....*....|...
gi 1149123047 1019 MYFSYAGCFRFGAYLVAHKLMSF 1041
Cdd:cd18544    235 SSLALALVLWYGGGQVLSGAVTL 257
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
462-659 2.21e-21

ABC-type uncharacterized transport system, ATPase component [General function prediction only];


Pssm-ID: 440718 [Multi-domain]  Cd Length: 264  Bit Score: 95.54  E-value: 2.21e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVH--FSYPSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIrTinvrFLRE- 538
Cdd:COG1101      2 LELKNLSktFNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDV-T----KLPEy 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  539 ----IIGVVSQEPVL---FATTIAEN------------IRYGRENVTMDEIEKAVKEANaydfiMKLPHKFDTLVGerga 599
Cdd:COG1101     77 krakYIGRVFQDPMMgtaPSMTIEENlalayrrgkrrgLRRGLTKKRRELFRELLATLG-----LGLENRLDTKVG---- 147
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1149123047  600 QLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDK--ARKGRTTIVIAHRL 659
Cdd:COG1101    148 LLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKivEENNLTTLMVTHNM 209
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
1119-1332 2.39e-21

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 95.46  E-value: 2.39e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1119 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEI---KRlNVQWLRAHLGIVSQEP--ILF 1193
Cdd:PRK13638    13 DEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdysKR-GLLALRQQVATVFQDPeqQIF 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1194 DCSIAENIAYGDNSRVVSQEEIVRAAKEAnihafieslpnkySTKVGDKGTQ------LSGGQKQRIAIARALVRQPHIL 1267
Cdd:PRK13638    92 YTDIDSDIAFSLRNLGVPEAEITRRVDEA-------------LTLVDAQHFRhqpiqcLSHGQKKRVAIAGALVLQARYL 158
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1149123047 1268 LLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTI-QNADLIVVFQNGRVKEHGTHQQLLA 1332
Cdd:PRK13638   159 LLDEPTAGLDPAGRTQMIAIIRRiVAQGNHVIISSHDIDLIyEISDAVYVLRQGQILTHGAPGEVFA 225
cbiO PRK13643
energy-coupling factor transporter ATPase;
1113-1326 3.03e-21

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 95.57  E-value: 3.03e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1113 NYPTRPDIP----VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKV----LLDGKEIKRLNVQWLRAHLG 1184
Cdd:PRK13643     8 NYTYQPNSPfasrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdIVVSSTSKQKEIKPVRKKVG 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1185 IVSQEP--ILFDCSIAENIAYGDNSRVVSQEEIVRAAKEaniHAFIESLPNKYSTKvgdKGTQLSGGQKQRIAIARALVR 1262
Cdd:PRK13643    88 VVFQFPesQLFEETVLKDVAFGPQNFGIPKEKAEKIAAE---KLEMVGLADEFWEK---SPFELSGGQMRRVAIAGILAM 161
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1149123047 1263 QPHILLLDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGT 1326
Cdd:PRK13643   162 EPEVLVLDEPTAGLDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGT 227
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
462-680 3.50e-21

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 94.45  E-value: 3.50e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIG 541
Cdd:PRK13548     3 LEARNLSVRLGGRT---LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRA 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  542 VVSQEPVL-FATTIAENIRYGRE--NVTMDEIEKAVKEANAydfIMKLPHkfdtLVGERGAQLSGGQKQRIAIARALVR- 617
Cdd:PRK13548    80 VLPQHSSLsFPFTVEEVVAMGRAphGLSRAEDDALVAAALA---QVDLAH----LAGRDYPQLSGGEQQRVQLARVLAQl 152
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1149123047  618 -----NPKILLLDEATSALD-TESEAVVQVALDKARK-GRTTIVIAHRLS-TVRNADVIAGFDDGVIVEKG 680
Cdd:PRK13548   153 wepdgPPRWLLLDEPTSALDlAHQHHVLRLARQLAHErGLAVIVVLHDLNlAARYADRIVLLHQGRLVADG 223
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
462-632 3.69e-21

ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.


Pssm-ID: 213185 [Multi-domain]  Cd Length: 232  Bit Score: 93.76  E-value: 3.69e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINV-RFLREII 540
Cdd:cd03218      1 LRAENLSKRYGKRK---VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMhKRARLGI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  541 GVVSQEPVLFAT-TIAENIRYGRE--NVTMDEIEKAVKEANAYDFIMKLPHKFdtlvgerGAQLSGGQKQRIAIARALVR 617
Cdd:cd03218     78 GYLPQEASIFRKlTVEENILAVLEirGLSKKEREEKLEELLEEFHITHLRKSK-------ASSLSGGERRRVEIARALAT 150
                          170
                   ....*....|....*
gi 1149123047  618 NPKILLLDEATSALD 632
Cdd:cd03218    151 NPKFLLLDEPFAGVD 165
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
1118-1324 3.81e-21

ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 98.98  E-value: 3.81e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1118 PDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLerfydplAGKVLLDGKEIKR-LNVQwlrahLGIVSQEPILFDcs 1196
Cdd:COG0488    326 GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLL-------AGELEPDSGTVKLgETVK-----IGYFDQHQEELD-- 391
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1197 iaeniaygDNSRVVsqEEIVRAA---KEANIHAFIESL---PNKYSTKVGDkgtqLSGGQKQRIAIARALVRQPHILLLD 1270
Cdd:COG0488    392 --------PDKTVL--DELRDGApggTEQEVRGYLGRFlfsGDDAFKPVGV----LSGGEKARLALAKLLLSPPNVLLLD 457
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1149123047 1271 EATSALDTESEKVVQEALDkAREGrTCIVIAH-R--LSTIqnADLIVVFQNGRVKEH 1324
Cdd:COG0488    458 EPTNHLDIETLEALEEALD-DFPG-TVLLVSHdRyfLDRV--ATRILEFEDGGVREY 510
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
1118-1333 4.65e-21

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 98.44  E-value: 4.65e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1118 PDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQ-WLRAHLGIVSQEPILF-DC 1195
Cdd:PRK11288    15 PGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTaALAAGVAIIYQELHLVpEM 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1196 SIAENIAYGD--NSR-VVSQEEIVRAAKEANIHAFIESLPNkysTKVGDkgtqLSGGQKQRIAIARALVRQPHILLLDEA 1272
Cdd:PRK11288    95 TVAENLYLGQlpHKGgIVNRRLLNYEAREQLEHLGVDIDPD---TPLKY----LSIGQRQMVEIAKALARNARVIAFDEP 167
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1149123047 1273 TSALDT-ESE---KVVQEALDkarEGRTCIVIAHRLSTI-QNADLIVVFQNGR-VKEHG-----THQQLLAQ 1333
Cdd:PRK11288   168 TSSLSArEIEqlfRVIRELRA---EGRVILYVSHRMEEIfALCDAITVFKDGRyVATFDdmaqvDRDQLVQA 236
ABC_6TM_TAP2 cd18590
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ...
216-405 4.93e-21

Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.


Pssm-ID: 350034 [Multi-domain]  Cd Length: 289  Bit Score: 95.10  E-value: 4.93e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  216 KIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQSMATFFTGFIVGFTRGWKLTLVILAISPVL 295
Cdd:cd18590     70 RLRHQLFSSLVQQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVKTLGMLGFMLSLSWQLTLLTLIEMPLT 149
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  296 GLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKRIGIKKAITANISIGAAFLL 375
Cdd:cd18590    150 AIAQKVYNTYHQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTVRAVYLLVRRVL 229
                          170       180       190
                   ....*....|....*....|....*....|
gi 1149123047  376 IYASYALAFWYGTTLVLSGEYSIGQVLTVF 405
Cdd:cd18590    230 QLGVQVLMLYCGRQLIQSGHLTTGSLVSFI 259
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
1121-1334 5.00e-21

ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.


Pssm-ID: 213258 [Multi-domain]  Cd Length: 282  Bit Score: 94.92  E-value: 5.00e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1121 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKeikrlnvqwlrahLGIVSQEPILFDCSIAEN 1200
Cdd:cd03291     51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQFSWIMPGTIKEN 117
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1201 IAYG---DNSRVVSqeeIVRAAK-EANIHAFieslPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSAL 1276
Cdd:cd03291    118 IIFGvsyDEYRYKS---VVKACQlEEDITKF----PEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYL 190
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1149123047 1277 DTESEKVVQEA-LDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQLLAQK 1334
Cdd:cd03291    191 DVFTEKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLR 249
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
1104-1277 5.81e-21

sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 96.07  E-value: 5.81e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1104 NVTFGEVVFNYPTrpDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQL---LERFydpLAGKVLLDGKEIKRLnvqwlr 1180
Cdd:PRK11650     3 GLKLQAVRKSYDG--KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMvagLERI---TSGEIWIGGRVVNEL------ 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1181 ahlgivsqEPILFDC-------------SIAENIAYGDNSRVVSQEEIVR----AAKEANIHAFIESLPNkystkvgdkg 1243
Cdd:PRK11650    72 --------EPADRDIamvfqnyalyphmSVRENMAYGLKIRGMPKAEIEErvaeAARILELEPLLDRKPR---------- 133
                          170       180       190
                   ....*....|....*....|....*....|....
gi 1149123047 1244 tQLSGGQKQRIAIARALVRQPHILLLDEATSALD 1277
Cdd:PRK11650   134 -ELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
1106-1321 6.04e-21

ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 98.18  E-value: 6.04e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1106 TFGEVVFNyptrpdipvlQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLN-VQWLRAHLG 1184
Cdd:COG3845     14 RFGGVVAN----------DDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSpRDAIALGIG 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1185 IVSQEPILFDC-SIAENIAYGDNSRVVSQEEIVRAAKEanihafIESLPNKY------STKVGDkgtqLSGGQKQRIAIA 1257
Cdd:COG3845     84 MVHQHFMLVPNlTVAENIVLGLEPTKGGRLDRKAARAR------IRELSERYgldvdpDAKVED----LSVGEQQRVEIL 153
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1149123047 1258 RALVRQPHILLLDEATSAL-DTESEKVVqEALDK-AREGRTCIVIAHRLSTI-QNADLIVVFQNGRV 1321
Cdd:COG3845    154 KALYRGARILILDEPTAVLtPQEADELF-EILRRlAAEGKSIIFITHKLREVmAIADRVTVLRRGKV 219
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
462-719 7.49e-21

ABC-type uncharacterized transport system, ATPase component [General function prediction only];


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 94.79  E-value: 7.49e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYpsrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINvrflREIIG 541
Cdd:COG4152      2 LELKGLTKRF---GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED----RRRIG 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  542 VVSQEPVLFAT-TIAENIRY-GR-ENVTMDEIEKAVKEanaydfIMKlphKFDtlVGERGA----QLSGGQKQRIAIARA 614
Cdd:COG4152     75 YLPEERGLYPKmKVGEQLVYlARlKGLSKAEAKRRADE------WLE---RLG--LGDRANkkveELSKGNQQKVQLIAA 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  615 LVRNPKILLLDEATSALDTES-EAVVQVALDKARKGRTTIVIAHRLSTV-RNADVIAGFDDGVIVEKGNHDELMKEKGIy 692
Cdd:COG4152    144 LLHDPELLILDEPFSGLDPVNvELLKDVIRELAAKGTTVIFSSHQMELVeELCDRIVIINKGRKVLSGSVDEIRRQFGR- 222
                          250       260
                   ....*....|....*....|....*..
gi 1149123047  693 fKLVTMQTAGNEVELENAADESKSEID 719
Cdd:COG4152    223 -NTLRLEADGDAGWLRALPGVTVVEED 248
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
462-674 7.69e-21

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 98.08  E-value: 7.69e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSrkeVKILKGLNLKVQSGQTVALVGNSGCGKSTtvqLMQRL-----YDPTEGMVSVDGQDIRTINVRFL 536
Cdd:PRK13549     6 LEMKNITKTFGG---VKALDNVSLKVRAGEIVSLCGENGAGKST---LMKVLsgvypHGTYEGEIIFEGEELQASNIRDT 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  537 REI-IGVVSQEPVLFAT-TIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLphKFDTLVGERGAQLSGGQKQRIAIARA 614
Cdd:PRK13549    80 ERAgIAIIHQELALVKElSVLENIFLGNEITPGGIMDYDAMYLRAQKLLAQL--KLDINPATPVGNLGLGQQQLVEIAKA 157
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1149123047  615 LVRNPKILLLDEATSALdTESEAVVQVAL--DKARKGRTTIVIAHRLSTVRN-ADVIAGFDDG 674
Cdd:PRK13549   158 LNKQARLLILDEPTASL-TESETAVLLDIirDLKAHGIACIYISHKLNEVKAiSDTICVIRDG 219
cbiO PRK13643
energy-coupling factor transporter ATPase;
462-688 9.03e-21

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 94.42  E-value: 9.03e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSRKEV--KILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTIN----VRF 535
Cdd:PRK13643     2 IKFEKVNYTYQPNSPFasRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeIKP 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  536 LREIIGVVSQEP--VLFATTIAENIRYGREN--VTMDEIEKAVKE-----ANAYDFIMKLPHkfdtlvgergaQLSGGQK 606
Cdd:PRK13643    82 VRKKVGVVFQFPesQLFEETVLKDVAFGPQNfgIPKEKAEKIAAEklemvGLADEFWEKSPF-----------ELSGGQM 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  607 QRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARK-GRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKGNHDE 684
Cdd:PRK13643   151 RRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSD 230

                   ....
gi 1149123047  685 LMKE 688
Cdd:PRK13643   231 VFQE 234
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
1111-1330 1.09e-20

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 94.38  E-value: 1.09e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1111 VFNYPTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKV---LLDGKEIKRL------------- 1174
Cdd:PRK13651    11 IFNKKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewiFKDEKNKKKTkekekvleklviq 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1175 --------NVQWLRAHLGIVSQ--EPILFDCSIAENIAYGDNSRVVSQEEIVRAAKEanihaFIE--SLPNKYSTKvgdK 1242
Cdd:PRK13651    91 ktrfkkikKIKEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSKEEAKKRAAK-----YIElvGLDESYLQR---S 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1243 GTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKA-REGRTCIVIAHRL-STIQNADLIVVFQNGR 1320
Cdd:PRK13651   163 PFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLdNVLEWTKRTIFFKDGK 242
                          250
                   ....*....|.
gi 1149123047 1321 -VKEHGTHQQL 1330
Cdd:PRK13651   243 iIKDGDTYDIL 253
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
1122-1332 1.20e-20

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 93.62  E-value: 1.20e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1122 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAG-----KVLLDGKEI-KRLNVQWLRAHLGIVSQEPILFDC 1195
Cdd:PRK14271    36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIfNYRDVLEFRRRVGMLFQRPNPFPM 115
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1196 SIAENIAYGDNSRVVSQEEIVRAAKEANIHAFieSLPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSA 1275
Cdd:PRK14271   116 SIMDNVLAGVRAHKLVPRKEFRGVAQARLTEV--GLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSA 193
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1149123047 1276 LDTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLLA 1332
Cdd:PRK14271   194 LDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLFS 251
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
1122-1328 1.30e-20

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 92.38  E-value: 1.30e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1122 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDG------KEIKRLNVQWLRAHLGIVSQE----PI 1191
Cdd:PRK11124    17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAIRELRRNVGMVFQQynlwPH 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1192 LfdcSIAENIAYGDnSRV--VSQEEIVRAAKEA----NIHAFIESLPnkystkvgdkgTQLSGGQKQRIAIARALVRQPH 1265
Cdd:PRK11124    97 L---TVQQNLIEAP-CRVlgLSKDQALARAEKLlerlRLKPYADRFP-----------LHLSGGQQQRVAIARALMMEPQ 161
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1149123047 1266 ILLLDEATSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQ 1328
Cdd:PRK11124   162 VLLFDEPTAALDPEiTAQIVSIIRELAETGITQVIVTHEVEVARKtASRVVYMENGHIVEQGDAS 226
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
1121-1327 1.37e-20

ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 443326 [Multi-domain]  Cd Length: 242  Bit Score: 92.38  E-value: 1.37e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1121 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDG------KEIKRLNVQWLRAHLGIVSQE----P 1190
Cdd:COG4161     16 QALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIRLLRQKVGMVFQQynlwP 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1191 ILfdcSIAENIAYG-----DNSRVVSQEEIVRAAKEANIHAFIESLPNkystkvgdkgtQLSGGQKQRIAIARALVRQPH 1265
Cdd:COG4161     96 HL---TVMENLIEApckvlGLSKEQAREKAMKLLARLRLTDKADRFPL-----------HLSGGQQQRVAIARALMMEPQ 161
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1149123047 1266 ILLLDEATSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTH 1327
Cdd:COG4161    162 VLLFDEPTAALDPEiTAQVVEIIRELSQTGITQVIVTHEVEFARKvASQVVYMEKGRIIEQGDA 225
urea_trans_UrtE TIGR03410
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ...
1122-1326 1.45e-20

urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 274567 [Multi-domain]  Cd Length: 230  Bit Score: 92.20  E-value: 1.45e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1122 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWlRAHLGI--VSQEPILF-DCSIA 1198
Cdd:TIGR03410   15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHE-RARAGIayVPQGREIFpRLTVE 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1199 ENIAYGDNsrvvsqeeiVRAAKEANIHAFIESLPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDT 1278
Cdd:TIGR03410   94 ENLLTGLA---------ALPRRSRKIPDEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQP 164
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1149123047 1279 ESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVFQNGRVKEHGT 1326
Cdd:TIGR03410  165 SIIKDIGRVIRRlrAEGGMAILLVEQYLDfARELADRYYVMERGRVVASGA 215
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
1123-1327 1.46e-20

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 91.86  E-value: 1.46e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1123 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLN---VQWLRAHLGIVSQEP-ILFDCSIA 1198
Cdd:PRK10908    18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKnreVPFLRRQIGMIFQDHhLLMDRTVY 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1199 ENIAYGDNSRVVSQEEIVRAAKEAnihafieslpnkySTKVG--DKG----TQLSGGQKQRIAIARALVRQPHILLLDEA 1272
Cdd:PRK10908    98 DNVAIPLIIAGASGDDIRRRVSAA-------------LDKVGllDKAknfpIQLSGGEQQRVGIARAVVNKPAVLLADEP 164
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1149123047 1273 TSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQNADL-IVVFQNGRVkeHGTH 1327
Cdd:PRK10908   165 TGNLDDAlSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYrMLTLSDGHL--HGGV 219
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
473-680 1.63e-20

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 95.68  E-value: 1.63e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  473 SRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIGVVSQEPVL-FA 551
Cdd:PRK09536    12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFE 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  552 TTIAENIRYGREN-----VTMDE-----IEKAVKEANAYDFIMKlphKFDTlvgergaqLSGGQKQRIAIARALVRNPKI 621
Cdd:PRK09536    92 FDVRQVVEMGRTPhrsrfDTWTEtdraaVERAMERTGVAQFADR---PVTS--------LSGGERQRVLLARALAQATPV 160
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1149123047  622 LLLDEATSALDTESEA-VVQVALDKARKGRTTIVIAHRLS-TVRNADVIAGFDDGVIVEKG 680
Cdd:PRK09536   161 LLLDEPTASLDINHQVrTLELVRRLVDDGKTAVAAIHDLDlAARYCDELVLLADGRVRAAG 221
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
1118-1316 1.90e-20

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 90.76  E-value: 1.90e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1118 PDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQwlrahlgiVSQEPILFDCSI 1197
Cdd:NF040873     3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQ--------RSEVPDSLPLTV 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1198 AENIAYGDNSRVVSQEEIVRAAKEANIHAF----IESLPNKystKVGDkgtqLSGGQKQRIAIARALVRQPHILLLDEAT 1273
Cdd:NF040873    75 RDLVAMGRWARRGLWRRLTRDDRAAVDDALervgLADLAGR---QLGE----LSGGQRQRALLAQGLAQEADLLLLDEPT 147
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1149123047 1274 SALDTESEKVVQEAL-DKAREGRTCIVIAHRLSTIQNADLIVVF 1316
Cdd:NF040873   148 TGLDAESRERIIALLaEEHARGATVVVVTHDLELVRRADPCVLL 191
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
1122-1321 2.04e-20

Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.


Pssm-ID: 213182 [Multi-domain]  Cd Length: 182  Bit Score: 90.18  E-value: 2.04e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1122 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNV-QWLRAHLGIVSQEP----ILFDCS 1196
Cdd:cd03215     15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPrDAIRAGIAYVPEDRkregLVLDLS 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1197 IAENIAYGDnsrvvsqeeivraakeanihafieslpnkystkvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEATSAL 1276
Cdd:cd03215     95 VAENIALSS---------------------------------------LLSGGNQQKVVLARWLARDPRVLILDEPTRGV 135
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1149123047 1277 DTES-EKVVQEALDKAREGRTCIVIahrlST-----IQNADLIVVFQNGRV 1321
Cdd:cd03215    136 DVGAkAEIYRLIRELADAGKAVLLI----SSeldelLGLCDRILVMYEGRI 182
ABC_6TM_exporter_like cd18564
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
190-414 2.61e-20

Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 350008 [Multi-domain]  Cd Length: 307  Bit Score: 93.35  E-value: 2.61e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  190 GIGAGVLVAAYIQVSFWCLAAGRQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQSMAT 269
Cdd:cd18564     62 GIALLRGLASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLT 141
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  270 FFTGFIVGFTRGWKLTLVILAISPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNK 349
Cdd:cd18564    142 LVGMLGVMFWLDWQLALIALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFAR 221
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1149123047  350 NLEEAKRIGIK-KAITANISIGAAfLLIYASYALAFWYGTTLVLSGEYSIGQvLTVFFSVLIGAFS 414
Cdd:cd18564    222 ENRKSLRAGLRaARLQALLSPVVD-VLVAVGTALVLWFGAWLVLAGRLTPGD-LLVFLAYLKNLYK 285
ABC_6TM_TmrB_like cd18541
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ...
179-407 2.65e-20

Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349985 [Multi-domain]  Cd Length: 293  Bit Score: 92.86  E-value: 2.65e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  179 EDMTRYAYYYSGIGAGVLVAAYIQVSFWcLAAGRQI-HKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIG 257
Cdd:cd18541     37 SQLLRYALLILLLALLIGIFRFLWRYLI-FGASRRIeYDLRNDLFAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALG 115
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  258 DKIGMFFQSMATFFTGFIVGFTRGWKLTLVILAISPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAF 337
Cdd:cd18541    116 PGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLVYRLGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAF 195
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  338 GGQKKELERYNKNLEEAKRIGIKKAITANISIGAAFLLIYASYALAFWYGTTLVLSGEYSIGQvLTVFFS 407
Cdd:cd18541    196 VQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLSFLIVLWYGGRLVIRGTITLGD-LVAFNS 264
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
1118-1320 2.94e-20

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 96.15  E-value: 2.94e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1118 PDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYdP---LAGKVLLDGKEIKRLNVQWL-RAHLGIVSQEPILF 1193
Cdd:PRK13549    16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PhgtYEGEIIFEGEELQASNIRDTeRAGIAIIHQELALV 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1194 -DCSIAENIAYGD---NSRVVSQEEIVRAAKE--ANIHAFIEslPNkysTKVGDkgtqLSGGQKQRIAIARALVRQPHIL 1267
Cdd:PRK13549    95 kELSVLENIFLGNeitPGGIMDYDAMYLRAQKllAQLKLDIN--PA---TPVGN----LGLGQQQLVEIAKALNKQARLL 165
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1149123047 1268 LLDEATSALdTESEKVVQEAL--DKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGR 1320
Cdd:PRK13549   166 ILDEPTASL-TESETAVLLDIirDLKAHGIACIYISHKLNEVKAiSDTICVIRDGR 220
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
466-689 4.01e-20

ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.


Pssm-ID: 213258 [Multi-domain]  Cd Length: 282  Bit Score: 92.23  E-value: 4.01e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  466 NVHFSYPSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQdirtinvrflreiIGVVSQ 545
Cdd:cd03291     39 NLFFSNLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQ 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  546 EPVLFATTIAENIRYGrenVTMDEI--EKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILL 623
Cdd:cd03291    106 FSWIMPGTIKENIIFG---VSYDEYryKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYL 182
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1149123047  624 LDEATSALD--TESEaVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGNHDELMKEK 689
Cdd:cd03291    183 LDSPFGYLDvfTEKE-IFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLR 249
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
462-688 6.02e-20

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 94.98  E-value: 6.02e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSrkeVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVR-FLREII 540
Cdd:PRK11288     5 LSFDGIGKTFPG---VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTaALAAGV 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  541 GVVSQE----PVLfatTIAENIRYGRenvtmdeiekavkeanaydfimkLPHKF-----DTLVGERGAQL---------- 601
Cdd:PRK11288    82 AIIYQElhlvPEM---TVAENLYLGQ-----------------------LPHKGgivnrRLLNYEAREQLehlgvdidpd 135
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  602 ------SGGQKQRIAIARALVRNPKILLLDEATSALDT-ESEAVVQVALDKARKGRTTIVIAHRLSTV-RNADVIAGFDD 673
Cdd:PRK11288   136 tplkylSIGQRQMVEIAKALARNARVIAFDEPTSSLSArEIEQLFRVIRELRAEGRVILYVSHRMEEIfALCDAITVFKD 215
                          250       260
                   ....*....|....*....|.
gi 1149123047  674 GVIVE------KGNHDELMKE 688
Cdd:PRK11288   216 GRYVAtfddmaQVDRDQLVQA 236
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
462-680 7.68e-20

ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213236 [Multi-domain]  Cd Length: 210  Bit Score: 89.26  E-value: 7.68e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYpsrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINvrflREIIG 541
Cdd:cd03269      1 LEVENVTKRF---GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIG 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  542 VVSQEPVLF-ATTIAENIRYGRENVTMdEIEKAVKEANAYDFIMKLPHKFDtlvgERGAQLSGGQKQRIAIARALVRNPK 620
Cdd:cd03269     74 YLPEERGLYpKMKVIDQLVYLAQLKGL-KKEEARRRIDEWLERLELSEYAN----KRVEELSKGNQQKVQFIAAVIHDPE 148
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1149123047  621 ILLLDEATSALDTES-EAVVQVALDKARKGRTTIVIAHRLSTV-RNADVIAGFDDGVIVEKG 680
Cdd:cd03269    149 LLILDEPFSGLDPVNvELLKDVIRELARAGKTVILSTHQMELVeELCDRVLLLNKGRAVLYG 210
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
462-688 7.69e-20

ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.


Pssm-ID: 213184 [Multi-domain]  Cd Length: 200  Bit Score: 89.12  E-value: 7.69e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSypsRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTtvqLMQRL-----YDPTEGMVSVDGQDIR--TINVR 534
Cdd:cd03217      1 LEIKDLHVS---VGGKEILKGVNLTIKKGEVHALMGPNGSGKST---LAKTImghpkYEVTEGEILFKGEDITdlPPEER 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  535 FlREIIGVVSQEPVLFA-TTIAENIRYGRENvtmdeiekavkeanaydfimklphkfdtlvgergaqLSGGQKQRIAIAR 613
Cdd:cd03217     75 A-RLGIFLAFQYPPEIPgVKNADFLRYVNEG------------------------------------FSGGEKKRNEILQ 117
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1149123047  614 ALVRNPKILLLDEATSALDTES-EAVVQVALDKARKGRTTIVIAH--RLSTVRNADVIAGFDDGVIVEKGNhDELMKE 688
Cdd:cd03217    118 LLLLEPDLAILDEPDSGLDIDAlRLVAEVINKLREEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGD-KELALE 194
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
484-686 8.13e-20

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 90.03  E-value: 8.13e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  484 NLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRflREIIGVVSQEPVLFA-TTIAENIRYG- 561
Cdd:PRK10771    19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQENNLFShLTVAQNIGLGl 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  562 RENVTMDEIEKAVKEANAY-----DFIMKLPhkfdtlvgergAQLSGGQKQRIAIARALVRNPKILLLDEATSALDT--E 634
Cdd:PRK10771    97 NPGLKLNAAQREKLHAIARqmgieDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEPFSALDPalR 165
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1149123047  635 SEAVVQVALDKARKGRTTIVIAHRLS-TVRNAD---VIAgfdDGVIVEKGNHDELM 686
Cdd:PRK10771   166 QEMLTLVSQVCQERQLTLLMVSHSLEdAARIAPrslVVA---DGRIAWDGPTDELL 218
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
1119-1325 8.22e-20

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 93.17  E-value: 8.22e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1119 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKeikRLN-VQWLRAHLGIVSQEPILF-DCS 1196
Cdd:PRK11000    15 DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEK---RMNdVPPAERGVGMVFQSYALYpHLS 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1197 IAENIAYGDNSRVVSQEEIVR----AAKEANIHAFIESLPNkystkvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEA 1272
Cdd:PRK11000    92 VAENMSFGLKLAGAKKEEINQrvnqVAEVLQLAHLLDRKPK-----------ALSGGQRQRVAIGRTLVAEPSVFLLDEP 160
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1149123047 1273 TSALDTESEkvVQEALDKA----REGRTCIVIAH-RLSTIQNADLIVVFQNGRVKEHG 1325
Cdd:PRK11000   161 LSNLDAALR--VQMRIEISrlhkRLGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVG 216
ABC_6TM_TmrA_like cd18544
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ...
181-407 8.80e-20

Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349988 [Multi-domain]  Cd Length: 294  Bit Score: 91.30  E-value: 8.80e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  181 MTRYAYYYSGIGAGVLVAAYIQVSFWCLAAGRQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKI 260
Cdd:cd18544     40 LLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGL 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  261 GMFFQSMATFFTGFIVGFTRGWKLTLVILAISPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQ 340
Cdd:cd18544    120 VTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATYLFRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNRE 199
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1149123047  341 KKELERYNKNLEEAKRIGIKkaitaNISIGAAF-----LLIYASYALAFWYGTTLVLSGEYSIGqVLTVFFS 407
Cdd:cd18544    200 KREFEEFDEINQEYRKANLK-----SIKLFALFrplveLLSSLALALVLWYGGGQVLSGAVTLG-VLYAFIQ 265
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
462-658 9.37e-20

ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).


Pssm-ID: 213190 [Multi-domain]  Cd Length: 166  Bit Score: 87.59  E-value: 9.37e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSRKevKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDirtiNVRFLreiig 541
Cdd:cd03223      1 IELENLSLATPDGR--VLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGE----DLLFL----- 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  542 vvSQEPVLFATTIAENIRYGRENVtmdeiekavkeanaydfimklphkfdtlvgergaqLSGGQKQRIAIARALVRNPKI 621
Cdd:cd03223     70 --PQRPYLPLGTLREQLIYPWDDV-----------------------------------LSGGEQQRLAFARLLLHKPKF 112
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1149123047  622 LLLDEATSALDTESEAVVqvaLDKARKGRTTIV-IAHR 658
Cdd:cd03223    113 VFLDEATSALDEESEDRL---YQLLKELGITVIsVGHR 147
PLN03232 PLN03232
ABC transporter C family member; Provisional
1112-1346 1.12e-19

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 96.20  E-value: 1.12e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1112 FNYPTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLdgkeikrlnvqwLRAHLGIVSQEPI 1191
Cdd:PLN03232   622 FSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVV------------IRGSVAYVPQVSW 689
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1192 LFDCSIAENIAYGDNsrvVSQEEIVRAAKEANIHAFIESLPNKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDE 1271
Cdd:PLN03232   690 IFNATVRENILFGSD---FESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDD 766
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1149123047 1272 ATSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGTHQQlLAQKGIYFSMVSVQAG 1346
Cdd:PLN03232   767 PLSALDAHvAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAE-LSKSGSLFKKLMENAG 841
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
1122-1332 1.32e-19

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 94.39  E-value: 1.32e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1122 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYdPLAGKVLLDGKEIKRLNVQWL---RAHLGIVSQEP---ILFDC 1195
Cdd:PRK15134   301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDPnssLNPRL 379
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1196 SIAENIAYGDNsrvVSQEEIVRAAKEANIHAFIEslpnkystKVG-DKGT------QLSGGQKQRIAIARALVRQPHILL 1268
Cdd:PRK15134   380 NVLQIIEEGLR---VHQPTLSAAQREQQVIAVME--------EVGlDPETrhrypaEFSGGQRQRIAIARALILKPSLII 448
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1149123047 1269 LDEATSALDteseKVVQE---ALDKAREGR---TCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLLA 1332
Cdd:PRK15134   449 LDEPTSSLD----KTVQAqilALLKSLQQKhqlAYLFISHDLHVVRAlCHQVIVLRQGEVVEQGDCERVFA 515
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
1121-1333 1.48e-19

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 94.00  E-value: 1.48e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1121 PVLQGLSLEVKKGQTLALVGSSGCGKS-TVVQLLERFYDP----LAGKVLLDGKEIKRLNVQWLRAHLG----IVSQEPI 1191
Cdd:PRK15134    23 TVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQTLRGVRGnkiaMIFQEPM 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1192 L-------FDCSIAENIA-YGDNSRVVSQEEIVRAAKEANIHafieslpnKYSTKVGDKGTQLSGGQKQRIAIARALVRQ 1263
Cdd:PRK15134   103 VslnplhtLEKQLYEVLSlHRGMRREAARGEILNCLDRVGIR--------QAAKRLTDYPHQLSGGERQRVMIAMALLTR 174
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1149123047 1264 PHILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTI-QNADLIVVFQNGRVKEHGTHQQLLAQ 1333
Cdd:PRK15134   175 PELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVrKLADRVAVMQNGRCVEQNRAATLFSA 247
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
1119-1320 1.87e-19

D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 131681 [Multi-domain]  Cd Length: 500  Bit Score: 93.74  E-value: 1.87e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1119 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFY--DPLAGKVLLDGKEIKRLNVQWL-RAHLGIVSQEPILF-D 1194
Cdd:TIGR02633   13 GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSPLKASNIRDTeRAGIVIIHQELTLVpE 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1195 CSIAENIAYGD----NSRVVSQEEIVRAAKEANIHAFIESLPNkySTKVGDKGtqlsGGQKQRIAIARALVRQPHILLLD 1270
Cdd:TIGR02633   93 LSVAENIFLGNeitlPGGRMAYNAMYLRAKNLLRELQLDADNV--TRPVGDYG----GGQQQLVEIAKALNKQARLLILD 166
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1149123047 1271 EATSAL-DTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGR 1320
Cdd:TIGR02633  167 EPSSSLtEKETEILLDIIRDLKAHGVACVYISHKLNEVKAvCDTICVIRDGQ 218
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
1119-1334 2.33e-19

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 91.05  E-value: 2.33e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1119 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRlNVQWLRAHLGIVSQepilFD---- 1194
Cdd:PRK13536    53 DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIGVVPQ----FDnldl 127
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1195 -CSIAEN-IAYGDNSRVVSQEeivraaKEANIHAFIE--SLPNKYSTKVGDkgtqLSGGQKQRIAIARALVRQPHILLLD 1270
Cdd:PRK13536   128 eFTVRENlLVFGRYFGMSTRE------IEAVIPSLLEfaRLESKADARVSD----LSGGMKRRLTLARALINDPQLLILD 197
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1149123047 1271 EATSALDTESEKVVQEALDK--AReGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLLAQK 1334
Cdd:PRK13536   198 EPTTGLDPHARHLIWERLRSllAR-GKTILLTTHFMEEAERlCDRLCVLEAGRKIAEGRPHALIDEH 263
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
470-666 2.54e-19

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 87.29  E-value: 2.54e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  470 SYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGqdirTINVRFLREIIGVVSQEPVl 549
Cdd:NF040873     1 GYGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG----GARVAYVPQRSEVPDSLPL- 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  550 fatTIAENIRYGR-------ENVTMDEiEKAVKEAnaydfIMKLphKFDTLVGERGAQLSGGQKQRIAIARALVRNPKIL 622
Cdd:NF040873    73 ---TVRDLVAMGRwarrglwRRLTRDD-RAAVDDA-----LERV--GLADLAGRQLGELSGGQRQRALLAQGLAQEADLL 141
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1149123047  623 LLDEATSALDTESEAVVQVAL-DKARKGRTTIVIAHRLSTVRNAD 666
Cdd:NF040873   142 LLDEPTTGLDAESRERIIALLaEEHARGATVVVVTHDLELVRRAD 186
cbiO PRK13645
energy-coupling factor transporter ATPase;
460-695 2.79e-19

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 90.07  E-value: 2.79e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  460 GNLEFRNVHFSYPSRK--EVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDI-----RTIN 532
Cdd:PRK13645     5 KDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpanlkKIKE 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  533 VRFLREIIGVVSQEP--VLFATTIAENIRYGRENVTMDEiEKAVKEANAYDFIMKLPHKFdtlVGERGAQLSGGQKQRIA 610
Cdd:PRK13645    85 VKRLRKEIGLVFQFPeyQLFQETIEKDIAFGPVNLGENK-QEAYKKVPELLKLVQLPEDY---VKRSPFELSGGQKRRVA 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  611 IARALVRNPKILLLDEATSALDTESEAVVQVALDKARK--GRTTIVIAHRLSTV-RNADVIAGFDDGVIVEKGNHDELMK 687
Cdd:PRK13645   161 LAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKeyKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGSPFEIFS 240

                   ....*...
gi 1149123047  688 EKGIYFKL 695
Cdd:PRK13645   241 NQELLTKI 248
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
462-680 2.95e-19

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 93.77  E-value: 2.95e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSR--------KEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTIN- 532
Cdd:PRK10261   314 LQVRNLVTRFPLRsgllnrvtREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSp 393
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  533 --VRFLREIIGVVSQEPvlFAT---------TIAENIRY--------GRENVTMDEIEKAVKEANAYDFimklPHKFdtl 593
Cdd:PRK10261   394 gkLQALRRDIQFIFQDP--YASldprqtvgdSIMEPLRVhgllpgkaAAARVAWLLERVGLLPEHAWRY----PHEF--- 464
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  594 vgergaqlSGGQKQRIAIARALVRNPKILLLDEATSALDTESEA-VVQVALDKARK-GRTTIVIAHRLSTV-RNADVIAG 670
Cdd:PRK10261   465 --------SGGQRQRICIARALALNPKVIIADEAVSALDVSIRGqIINLLLDLQRDfGIAYLFISHDMAVVeRISHRVAV 536
                          250
                   ....*....|
gi 1149123047  671 FDDGVIVEKG 680
Cdd:PRK10261   537 MYLGQIVEIG 546
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
1121-1271 3.04e-19

ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440752 [Multi-domain]  Cd Length: 240  Bit Score: 88.55  E-value: 3.04e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1121 PVLQGLSLEVKKGQTLALVGSSGCGKSTVvqllerFY------DPLAGKVLLDGKEIKRLNVqWLRAHLGI--VSQEPIL 1192
Cdd:COG1137     17 TVVKDVSLEVNQGEIVGLLGPNGAGKTTT------FYmivglvKPDSGRIFLDGEDITHLPM-HKRARLGIgyLPQEASI 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1193 F-DCSIAENI-AygdnsrVVSQEEIVRAAKEANIHAFIE--SLpnkysTKVGD-KGTQLSGGQKQRIAIARALVRQPHIL 1267
Cdd:COG1137     90 FrKLTVEDNIlA------VLELRKLSKKEREERLEELLEefGI-----THLRKsKAYSLSGGERRRVEIARALATNPKFI 158

                   ....
gi 1149123047 1268 LLDE 1271
Cdd:COG1137    159 LLDE 162
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
462-632 3.83e-19

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 88.58  E-value: 3.83e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTInvrflREIIG 541
Cdd:PRK11247    13 LLLNAVSKRYGERT---VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEA-----REDTR 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  542 VVSQEPVLFA-TTIAENIRYGRENVTMDEIEKAVKEANAYDfimklphkfdtLVGERGAQLSGGQKQRIAIARALVRNPK 620
Cdd:PRK11247    85 LMFQDARLLPwKKVIDNVGLGLKGQWRDAALQALAAVGLAD-----------RANEWPAALSGGQKQRVALARALIHRPG 153
                          170
                   ....*....|..
gi 1149123047  621 ILLLDEATSALD 632
Cdd:PRK11247   154 LLLLDEPLGALD 165
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
476-688 3.87e-19

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 89.76  E-value: 3.87e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  476 EVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEG---------------------MVSVDGQDIRTINVR 534
Cdd:PRK13651    19 ELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGtiewifkdeknkkktkekekvLEKLVIQKTRFKKIK 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  535 FLREI---IGVVSQ--EPVLFATTIAENIRYGRENVTMDEiEKAVKEANAYDFIMKLPHKFDtlvgERGA-QLSGGQKQR 608
Cdd:PRK13651    99 KIKEIrrrVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSK-EEAKKRAAKYIELVGLDESYL----QRSPfELSGGQKRR 173
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  609 IAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARK-GRTTIVIAHRLSTV--RNADVIAgFDDGVIVEKGNHDEL 685
Cdd:PRK13651   174 VALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKqGKTIILVTHDLDNVleWTKRTIF-FKDGKIIKDGDTYDI 252

                   ...
gi 1149123047  686 MKE 688
Cdd:PRK13651   253 LSD 255
cbiO PRK13646
energy-coupling factor transporter ATPase;
1105-1334 4.35e-19

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 89.07  E-value: 4.35e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1105 VTFGEVVFNYP--TRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEI----KRLNVQW 1178
Cdd:PRK13646     3 IRFDNVSYTYQkgTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktKDKYIRP 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1179 LRAHLGIVSQ--EPILFDCSIAENIAYGDNSRVVSQEEIvraaKEaniHAFIESLPNKYSTKVGDKGT-QLSGGQKQRIA 1255
Cdd:PRK13646    83 VRKRIGMVFQfpESQLFEDTVEREIIFGPKNFKMNLDEV----KN---YAHRLLMDLGFSRDVMSQSPfQMSGGQMRKIA 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1256 IARALVRQPHILLLDEATSALDTESEKVVQEALDKAR--EGRTCIVIAHRLSTI-QNADLIVVFQNGRVKEHGTHQQLLA 1332
Cdd:PRK13646   156 IVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFK 235

                   ..
gi 1149123047 1333 QK 1334
Cdd:PRK13646   236 DK 237
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
1120-1323 4.67e-19

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 87.53  E-value: 4.67e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1120 IPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQW---LRA-HLGIVSQEPILFDC 1195
Cdd:PRK10584    23 LSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEArakLRAkHVGFVFQSFMLIPT 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1196 SIA-ENIAY-----GDNSRvVSQEEIVRAAKEANIHAFIESLPnkystkvgdkgTQLSGGQKQRIAIARALVRQPHILLL 1269
Cdd:PRK10584   103 LNAlENVELpallrGESSR-QSRNGAKALLEQLGLGKRLDHLP-----------AQLSGGEQQRVALARAFNGRPDVLFA 170
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1149123047 1270 DEATSALDTES-EKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIVVFQNGRVKE 1323
Cdd:PRK10584   171 DEPTGNLDRQTgDKIADLLFSLNREhGTTLILVTHDLQLAARCDRRLRLVNGQLQE 226
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
454-655 4.86e-19

ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.


Pssm-ID: 213234 [Multi-domain]  Cd Length: 236  Bit Score: 87.77  E-value: 4.86e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  454 KPDNIKGNLEfrnvHFSYPSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINV 533
Cdd:cd03267     15 KEPGLIGSLK----SLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRK 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  534 RFLREiIGVV--SQEPVLFATTIAENIRYGRE--NVTMDEIEKAVKEANAydfIMKLPHKFDTLVgergAQLSGGQKQRI 609
Cdd:cd03267     91 KFLRR-IGVVfgQKTQLWWDLPVIDSFYLLAAiyDLPPARFKKRLDELSE---LLDLEELLDTPV----RQLSLGQRMRA 162
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1149123047  610 AIARALVRNPKILLLDEATSALDTESEAVVQVALDKARKGRTTIVI 655
Cdd:cd03267    163 EIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVL 208
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
462-689 5.37e-19

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 89.89  E-value: 5.37e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTiNVRFLREIIG 541
Cdd:PRK13536    42 IDLAGVSKSYGDKA---VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIG 117
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  542 VVSQEPVL-FATTIAEN-IRYGRE-NVTMDEIEKAVkeANAYDFiMKLPHKFDTLVgergAQLSGGQKQRIAIARALVRN 618
Cdd:PRK13536   118 VVPQFDNLdLEFTVRENlLVFGRYfGMSTREIEAVI--PSLLEF-ARLESKADARV----SDLSGGMKRRLTLARALIND 190
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1149123047  619 PKILLLDEATSALDTESEAVVQVALDK-ARKGRTTIVIAHRLSTV-RNADVIAGFDDGVIVEKGNHDELMKEK 689
Cdd:PRK13536   191 PQLLILDEPTTGLDPHARHLIWERLRSlLARGKTILLTTHFMEEAeRLCDRLCVLEAGRKIAEGRPHALIDEH 263
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
476-657 7.66e-19

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 87.14  E-value: 7.66e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  476 EVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVR---FLR-EIIGVVSQEPVLFA 551
Cdd:PRK10584    22 ELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEaraKLRaKHVGFVFQSFMLIP 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  552 TTIAenirygRENVTMDEIEKAVKEANAYDFIMKLPHKFDtlVGER----GAQLSGGQKQRIAIARALVRNPKILLLDEA 627
Cdd:PRK10584   102 TLNA------LENVELPALLRGESSRQSRNGAKALLEQLG--LGKRldhlPAQLSGGEQQRVALARAFNGRPDVLFADEP 173
                          170       180       190
                   ....*....|....*....|....*....|..
gi 1149123047  628 TSALDTES-EAVVQVALDKARKGRTT-IVIAH 657
Cdd:PRK10584   174 TGNLDRQTgDKIADLLFSLNREHGTTlILVTH 205
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
1122-1326 8.32e-19

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 87.18  E-value: 8.32e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1122 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQW---LRAH-LGIVSQ-EPILFDCS 1196
Cdd:PRK11629    24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeLRNQkLGFIYQfHHLLPDFT 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1197 IAENIAYGDNSRVVSQEEIVRAAKEANIHAFIESlpnkystKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSAL 1276
Cdd:PRK11629   104 ALENVAMPLLIGKKKPAEINSRALEMLAAVGLEH-------RANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNL 176
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1149123047 1277 DTESEKVVQEALDK--AREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEHGT 1326
Cdd:PRK11629   177 DARNADSIFQLLGElnRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAELS 228
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
462-684 8.53e-19

ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 91.66  E-value: 8.53e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVdGQdirtiNVRflreiIG 541
Cdd:COG0488    316 LELEGLSKSYGDKT---LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GE-----TVK-----IG 381
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  542 VVSQEPVLFAT--TIAENIRYGRENVTmdeiekavkEANAYDFIMKL---PHKFDTLVGErgaqLSGGQKQRIAIARALV 616
Cdd:COG0488    382 YFDQHQEELDPdkTVLDELRDGAPGGT---------EQEVRGYLGRFlfsGDDAFKPVGV----LSGGEKARLALAKLLL 448
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1149123047  617 RNPKILLLDEATSALDTESEAVVQVALDkARKGrTTIVIAH-R--LSTVrnADVIAGFDDGVIVEK-GNHDE 684
Cdd:COG0488    449 SPPNVLLLDEPTNHLDIETLEALEEALD-DFPG-TVLLVSHdRyfLDRV--ATRILEFEDGGVREYpGGYDD 516
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
462-657 1.02e-18

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 88.71  E-value: 1.02e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYpsrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTiNVRFLREIIG 541
Cdd:PRK13537     8 IDFRNVEKRY---GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVG 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  542 VVSQ----EPVLfatTIAENIR-YGRE-NVTMDEIEKAVkeANAYDFiMKLPHKFDTLVGErgaqLSGGQKQRIAIARAL 615
Cdd:PRK13537    84 VVPQfdnlDPDF---TVRENLLvFGRYfGLSAAAARALV--PPLLEF-AKLENKADAKVGE----LSGGMKRRLTLARAL 153
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1149123047  616 VRNPKILLLDEATSALDTESEAVVQVALDK--ARkGRTTIVIAH 657
Cdd:PRK13537   154 VNDPDVLVLDEPTTGLDPQARHLMWERLRSllAR-GKTILLTTH 196
SapF COG4167
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
1112-1333 1.07e-18

ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];


Pssm-ID: 443328 [Multi-domain]  Cd Length: 265  Bit Score: 87.59  E-value: 1.07e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1112 FNYPT----RPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVS 1187
Cdd:COG4167     14 FKYRTglfrRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKYRCKHIRMIF 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1188 QEPilfdcsiaeNIAYGDNSRVVSQ-EEIVR-------AAKEANIHAFIEslpnkystKVG-------DKGTQLSGGQKQ 1252
Cdd:COG4167     94 QDP---------NTSLNPRLNIGQIlEEPLRlntdltaEEREERIFATLR--------LVGllpehanFYPHMLSSGQKQ 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1253 RIAIARALVRQPHILLLDEATSALD--TESEKV-----VQEaldkaREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEH 1324
Cdd:COG4167    157 RVALARALILQPKIIIADEALAALDmsVRSQIInlmleLQE-----KLGISYIYVSQHLGIVKHiSDKVLVMHQGEVVEY 231

                   ....*....
gi 1149123047 1325 GTHQQLLAQ 1333
Cdd:COG4167    232 GKTAEVFAN 240
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
462-626 1.47e-18

ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440752 [Multi-domain]  Cd Length: 240  Bit Score: 86.62  E-value: 1.47e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRT--INVRfLREI 539
Cdd:COG1137      4 LEAENLVKSYGKRT---VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHlpMHKR-ARLG 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  540 IGVVSQEPVLFAT-TIAENIRYGRENVTMDEIEKAvkeanaydfimklpHKFDTLVGE---------RGAQLSGGQKQRI 609
Cdd:COG1137     80 IGYLPQEASIFRKlTVEDNILAVLELRKLSKKERE--------------ERLEELLEEfgithlrksKAYSLSGGERRRV 145
                          170
                   ....*....|....*..
gi 1149123047  610 AIARALVRNPKILLLDE 626
Cdd:COG1137    146 EIARALATNPKFILLDE 162
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
483-680 1.51e-18

retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]


Pssm-ID: 130324 [Multi-domain]  Cd Length: 2272  Bit Score: 92.38  E-value: 1.51e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  483 LNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTiNVRFLREIIGVVSQEPVLFA-TTIAENIRYg 561
Cdd:TIGR01257  949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFHhLTVAEHILF- 1026
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  562 RENVTMDEIEKAVKEANAYDFIMKLPHKFDtlvgERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQV 641
Cdd:TIGR01257 1027 YAQLKGRSWEEAQLEMEAMLEDTGLHHKRN----EEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWD 1102
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1149123047  642 ALDKARKGRTTIVIAHRLStvrNADVIAgfDDGVIVEKG 680
Cdd:TIGR01257 1103 LLLKYRSGRTIIMSTHHMD---EADLLG--DRIAIISQG 1136
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
1122-1332 1.53e-18

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 87.94  E-value: 1.53e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1122 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRlNVQWLRAHLGIVSQ----EPilfDCSI 1197
Cdd:PRK13537    22 VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVGVVPQfdnlDP---DFTV 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1198 AENIaygdnsRVVSQEEIVRAAK-EANIHAFIE--SLPNKYSTKVGDkgtqLSGGQKQRIAIARALVRQPHILLLDEATS 1274
Cdd:PRK13537    98 RENL------LVFGRYFGLSAAAaRALVPPLLEfaKLENKADAKVGE----LSGGMKRRLTLARALVNDPDVLVLDEPTT 167
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1149123047 1275 ALDTESEKVVQEALDK--AReGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLLA 1332
Cdd:PRK13537   168 GLDPQARHLMWERLRSllAR-GKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHALIE 227
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
462-657 1.76e-18

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 86.68  E-value: 1.76e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFlreiiG 541
Cdd:PRK11248     2 LQISHLYADYGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER-----G 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  542 VVSQ-EPVLFATTIAENIRYGREnvtMDEIEKAVKEANAYDFIMKlphkfdtlVGERGA------QLSGGQKQRIAIARA 614
Cdd:PRK11248    74 VVFQnEGLLPWRNVQDNVAFGLQ---LAGVEKMQRLEIAHQMLKK--------VGLEGAekryiwQLSGGQRQRVGIARA 142
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1149123047  615 LVRNPKILLLDEATSALDTESEAVVQVALDK--ARKGRTTIVIAH 657
Cdd:PRK11248   143 LAANPQLLLLDEPFGALDAFTREQMQTLLLKlwQETGKQVLLITH 187
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
462-688 1.99e-18

methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]


Pssm-ID: 132313 [Multi-domain]  Cd Length: 520  Bit Score: 90.63  E-value: 1.99e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPS--RKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVS-------VDGQDIRTIN 532
Cdd:TIGR03269  280 IKVRNVSKRYISvdRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrvgdewVDMTKPGPDG 359
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  533 VRFLREIIGVVSQEPVLFA-TTIAENIRygrENVTM---DEI--EKAV--------KEANAYDFIMKLPHkfdtlvgerg 598
Cdd:TIGR03269  360 RGRAKRYIGILHQEYDLYPhRTVLDNLT---EAIGLelpDELarMKAVitlkmvgfDEEKAEEILDKYPD---------- 426
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  599 aQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARK--GRTTIVIAHRLSTVRN-ADVIAGFDDGV 675
Cdd:TIGR03269  427 -ELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDvCDRAALMRDGK 505
                          250
                   ....*....|...
gi 1149123047  676 IVEKGNHDELMKE 688
Cdd:TIGR03269  506 IVKIGDPEEIVEE 518
ABC_6TM_ABCB8_like cd18574
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ...
155-400 2.04e-18

Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.


Pssm-ID: 350018 [Multi-domain]  Cd Length: 295  Bit Score: 87.22  E-value: 2.04e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  155 LEDLMSNITNRSDINDTGFFMNLEEDMTRYAYYYSGigAGVLVAAYIqvSFWCLAAGRQIHKIRKQFFHAIMRQEIGWFD 234
Cdd:cd18574     19 LGDLVNVISRSLKETNGDFIEDLKKPALKLLGLYLL--QSLLTFAYI--SLLSVVGERVAARLRNDLFSSLLRQDIAFFD 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  235 VHDVGELNTRLTDDVSK--------INEGIgdkigmffQSMATFFTGFIVGFTRGWKLTLVILAISPVLGLSAAVWAKIL 306
Cdd:cd18574     95 THRTGELVNRLTADVQEfkssfkqcVSQGL--------RSVTQTVGCVVSLYLISPKLTLLLLVIVPVVVLVGTLYGSFL 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  307 SSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKR--------IGIKKAITaNISIGAAFLLIYa 378
Cdd:cd18574    167 RKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYEEEVEKAAKlneklglgIGIFQGLS-NLALNGIVLGVL- 244
                          250       260
                   ....*....|....*....|..
gi 1149123047  379 syalafWYGTTLVLSGEYSIGQ 400
Cdd:cd18574    245 ------YYGGSLVSRGELTAGD 260
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
469-691 2.12e-18

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 86.98  E-value: 2.12e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  469 FSYpsrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQ--DIRTINVRFLREIIGVVSQE 546
Cdd:PRK13638     9 FRY---QDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQVATVFQD 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  547 P--VLFATTIAENIRYGREN--VTMDEIEKAVKEANaydfimklphkfdTLVGERGAQ------LSGGQKQRIAIARALV 616
Cdd:PRK13638    86 PeqQIFYTDIDSDIAFSLRNlgVPEAEITRRVDEAL-------------TLVDAQHFRhqpiqcLSHGQKKRVAIAGALV 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  617 RNPKILLLDEATSALDTESEA-VVQVALDKARKGRTTIVIAHRLSTV----------RNADVIAGFDDGVIVEKGnhdEL 685
Cdd:PRK13638   153 LQARYLLLDEPTAGLDPAGRTqMIAIIRRIVAQGNHVIISSHDIDLIyeisdavyvlRQGQILTHGAPGEVFACT---EA 229

                   ....*.
gi 1149123047  686 MKEKGI 691
Cdd:PRK13638   230 MEQAGL 235
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
465-687 2.23e-18

Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 86.77  E-value: 2.23e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  465 RNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVR-FLREIIGVV 543
Cdd:PRK10575    15 RNVSFRVPGRT---LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKaFARKVAYLP 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  544 SQEPVLFATTIAENI------------RYGRENvtmdeiEKAVKEANAYDFIMKLPHKfdtLVGergaQLSGGQKQRIAI 611
Cdd:PRK10575    92 QQLPAAEGMTVRELVaigrypwhgalgRFGAAD------REKVEEAISLVGLKPLAHR---LVD----SLSGGERQRAWI 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  612 ARALVRNPKILLLDEATSALD----TESEAVVQvALDKARkGRTTIVIAHRLS-TVRNADVIAGFDDGVIVEKGNHDELM 686
Cdd:PRK10575   159 AMLVAQDSRCLLLDEPTSALDiahqVDVLALVH-RLSQER-GLTVIAVLHDINmAARYCDYLVALRGGEMIAQGTPAELM 236

                   .
gi 1149123047  687 K 687
Cdd:PRK10575   237 R 237
PvdE COG4615
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...
827-1323 2.74e-18

ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];


Pssm-ID: 443659 [Multi-domain]  Cd Length: 547  Bit Score: 90.24  E-value: 2.74e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  827 LLFLALGIISFITFFLQGFTFGKAGEILTKRLRYMVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIgSRLAVI 906
Cdd:COG4615     52 LLFAGLLVLLLLSRLASQLLLTRLGQHAVARLRLRLSRRILAAPLERLE--RIGAARLLAALTEDVRTISQAF-VRLPEL 128
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  907 TQNIANlgtgIIISFIY-GWQLTLLLLAIVPIIAIAGVVEMKMLSgqalKDKKELEGSGKIATEAIENFRTVVSLTQEQK 985
Cdd:COG4615    129 LQSVAL----VLGCLAYlAWLSPPLFLLTLVLLGLGVAGYRLLVR----RARRHLRRAREAEDRLFKHFRALLEGFKELK 200
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  986 F-----EHMYAQSLQVP---YRNSLRKAH-IFGITFSFTQAMMYFSYAGCFrfgaYLVAHKLMSFEDVLLVFSAVV-FGA 1055
Cdd:COG4615    201 LnrrrrRAFFDEDLQPTaerYRDLRIRADtIFALANNWGNLLFFALIGLIL----FLLPALGWADPAVLSGFVLVLlFLR 276
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1056 MAVGQVSSFAPDYAKAKISAAHIimiiEKTPL-IDSYSTEGLMPNTLEGNVTFGE-----VVFNYPTRPDIP--VLQGLS 1127
Cdd:COG4615    277 GPLSQLVGALPTLSRANVALRKI----EELELaLAAAEPAAADAAAPPAPADFQTlelrgVTYRYPGEDGDEgfTLGPID 352
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1128 LEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEPILFDcsiaeniaygdns 1207
Cdd:COG4615    353 LTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFD------------- 419
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1208 RVVSQEEIVRAAKeanIHAFIESLpnKYSTKVGDKG-----TQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEK 1282
Cdd:COG4615    420 RLLGLDGEADPAR---ARELLERL--ELDHKVSVEDgrfstTDLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEFRR 494
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|....
gi 1149123047 1283 VVQEAL---DKAReGRTCIVIAHRLSTIQNADLIVVFQNGRVKE 1323
Cdd:COG4615    495 VFYTELlpeLKAR-GKTVIAISHDDRYFDLADRVLKMDYGKLVE 537
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
1121-1321 3.07e-18

ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 89.69  E-value: 3.07e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1121 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNV-QWLRAHLGIVS----QEPILFDC 1195
Cdd:COG1129    266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPrDAIRAGIAYVPedrkGEGLVLDL 345
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1196 SIAENI---AYGDNSR--VVSQEEIVRAAKEanihaFIESLpnkySTKVGDKGT---QLSGGQKQRIAIARALVRQPHIL 1267
Cdd:COG1129    346 SIRENItlaSLDRLSRggLLDRRRERALAEE-----YIKRL----RIKTPSPEQpvgNLSGGNQQKVVLAKWLATDPKVL 416
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1149123047 1268 LLDEATSALD--TESE--KVVQEAldkAREGRTCIVIahrlST-----IQNADLIVVFQNGRV 1321
Cdd:COG1129    417 ILDEPTRGIDvgAKAEiyRLIREL---AAEGKAVIVI----SSelpelLGLSDRILVMREGRI 472
ABC_6TM_Tm288_like cd18547
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ...
781-1064 3.60e-18

Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349991 [Multi-domain]  Cd Length: 298  Bit Score: 86.69  E-value: 3.60e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  781 FVVGVFCAIINGGLQPAFAIIFSKIIGVFTRIDDPETKRQNSNLFSLLFLALGI--ISFITFFLQGFTFGKAGEILTKRL 858
Cdd:cd18547      1 LILVIILAIISTLLSVLGPYLLGKAIDLIIEGLGGGGGVDFSGLLRILLLLLGLylLSALFSYLQNRLMARVSQRTVYDL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  859 RYMVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIGSRLAVITQNIANLGTGIIISFIYGWQLTLLLLAIVPII 938
Cdd:cd18547     81 RKDLFEKLQRLPLSYFD--THSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLS 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  939 AIAgvveMKMLSGQALKD-KKELEGSGKI---ATEAIENFRTVVSLTQE----QKFEHMYAQslqvpYRNSLRKAHIF-G 1009
Cdd:cd18547    159 LLV----TKFIAKRSQKYfRKQQKALGELngyIEEMISGQKVVKAFNREeeaiEEFDEINEE-----LYKASFKAQFYsG 229
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1149123047 1010 ITFSFTQAMMYFSYAGCFRFGAYLvahklmsfedvllvfsaVVFGAMAVGQVSSF 1064
Cdd:cd18547    230 LLMPIMNFINNLGYVLVAVVGGLL-----------------VINGALTVGVIQAF 267
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
462-691 3.64e-18

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 89.72  E-value: 3.64e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSrkeVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREI-I 540
Cdd:PRK15439    12 LCARSISKQYSG---VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLgI 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  541 GVVSQEPVLFAT-TIAENIRYG--RENVTMDEIEKAVKEANAYdfiMKLPHKFDTL-VGERgaqlsggqkQRIAIARALV 616
Cdd:PRK15439    89 YLVPQEPLLFPNlSVKENILFGlpKRQASMQKMKQLLAALGCQ---LDLDSSAGSLeVADR---------QIVEILRGLM 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1149123047  617 RNPKILLLDEATSALD-TESEAVVQVALDKARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKGNHDELMKEKGI 691
Cdd:PRK15439   157 RDSRILILDEPTASLTpAETERLFSRIRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADLSTDDII 233
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
1122-1321 4.35e-18

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 85.50  E-value: 4.35e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1122 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDP-----LAGKVLL-DGKEIKRLNVQWLRahlgivsqepILFDC 1195
Cdd:PRK11247    27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPsagelLAGTAPLaEAREDTRLMFQDAR----------LLPWK 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1196 SIAENIAYG--DNSRVVSQE--EIVRAAKEANihafieslpnkystkvgDKGTQLSGGQKQRIAIARALVRQPHILLLDE 1271
Cdd:PRK11247    97 KVIDNVGLGlkGQWRDAALQalAAVGLADRAN-----------------EWPAALSGGQKQRVALARALIHRPGLLLLDE 159
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1149123047 1272 ATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVFQNGRV 1321
Cdd:PRK11247   160 PLGALDALTRIEMQDLIESlwQQHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
479-660 4.47e-18

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 84.87  E-value: 4.47e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  479 ILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREI----IGVVSQEPVLFATTI 554
Cdd:PRK11629    24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELrnqkLGFIYQFHHLLPDFT 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  555 AenirygRENVTMDEI--EKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALD 632
Cdd:PRK11629   104 A------LENVAMPLLigKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLD 177
                          170       180       190
                   ....*....|....*....|....*....|
gi 1149123047  633 TE-SEAVVQVALD-KARKGRTTIVIAHRLS 660
Cdd:PRK11629   178 ARnADSIFQLLGElNRLQGTAFLVVTHDLQ 207
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
1104-1333 4.54e-18

ABC-type uncharacterized transport system, ATPase component [General function prediction only];


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 86.32  E-value: 4.54e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1104 NVT--FGEVVfnyptrpdipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNvqwlRA 1181
Cdd:COG4152      6 GLTkrFGDKT----------AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED----RR 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1182 HLGIVSQEPILF-DCSIAENIAY-----GdnsrvVSQEEIVRAAKEanihaFIE--SLPNKYSTKVGDkgtqLSGGQKQR 1253
Cdd:COG4152     72 RIGYLPEERGLYpKMKVGEQLVYlarlkG-----LSKAEAKRRADE-----WLErlGLGDRANKKVEE----LSKGNQQK 137
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1254 IAIARALVRQPHILLLDEATSALDTES-EKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLL 1331
Cdd:COG4152    138 VQLIAALLHDPELLILDEPFSGLDPVNvELLKDVIRELAAKGTTVIFSSHQMELVEElCDRIVIINKGRKVLSGSVDEIR 217

                   ..
gi 1149123047 1332 AQ 1333
Cdd:COG4152    218 RQ 219
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
1125-1330 4.65e-18

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 87.07  E-value: 4.65e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1125 GLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLN-VQWL--RAHLGIVSQEPILF---DCSIA 1198
Cdd:PRK15079    39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKdDEWRavRSDIQMIFQDPLASlnpRMTIG 118
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1199 ENIAygDNSRV----VSQEEIVRAAKEANIH-AFIESLPNKYSTkvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEAT 1273
Cdd:PRK15079   119 EIIA--EPLRTyhpkLSRQEVKDRVKAMMLKvGLLPNLINRYPH-------EFSGGQCQRIGIARALILEPKLIICDEPV 189
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1274 SALDTESE-KVVQEALDKARE-GRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQL 1330
Cdd:PRK15079   190 SALDVSIQaQVVNLLQQLQREmGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV 249
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
474-656 4.78e-18

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 84.16  E-value: 4.78e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  474 RKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIGvvSQEPVLFATT 553
Cdd:PRK13539    12 RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLG--HRNAMKPALT 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  554 IAENIRYGRE--NVTMDEIEKAVKeanaydfIMKLPHKFDTlvgeRGAQLSGGQKQRIAIARALVRNPKILLLDEATSAL 631
Cdd:PRK13539    90 VAENLEFWAAflGGEELDIAAALE-------AVGLAPLAHL----PFGYLSAGQKRRVALARLLVSNRPIWILDEPTAAL 158
                          170       180
                   ....*....|....*....|....*
gi 1149123047  632 DTESEAVVQvALDKARKGRTTIVIA 656
Cdd:PRK13539   159 DAAAVALFA-ELIRAHLAQGGIVIA 182
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
1114-1302 5.13e-18

ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 88.97  E-value: 5.13e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1114 YPTRPdipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGkeikrlnvqwlRAHLGIVSQEPILF 1193
Cdd:COG0488      8 FGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-----------GLRIGYLPQEPPLD 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1194 D-CSIAENIAYGDNSRVVSQEEIVRA-----------AKEANIHAFIESL-------------------PNKYSTKVGDk 1242
Cdd:COG0488     74 DdLTVLDTVLDGDAELRALEAELEELeaklaepdedlERLAELQEEFEALggweaearaeeilsglgfpEEDLDRPVSE- 152
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1149123047 1243 gtqLSGGQKQRIAIARALVRQPHILLLDEATSALDTESekvVQ--EALDKAREGrTCIVIAH 1302
Cdd:COG0488    153 ---LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES---IEwlEEFLKNYPG-TVLVVSH 207
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
1119-1321 5.29e-18

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 89.78  E-value: 5.29e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1119 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWL----RAHLGIVSQE-PILF 1193
Cdd:PRK10535    20 QVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrREHFGFIFQRyHLLS 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1194 DCSIAENIaygDNSRVVSQEEivRAAKEANIHAFIESLpnKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEAT 1273
Cdd:PRK10535   100 HLTAAQNV---EVPAVYAGLE--RKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPT 172
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1149123047 1274 SALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIVVFQNGRV 1321
Cdd:PRK10535   173 GALDSHSGEEVMAILHQLRDrGHTVIIVTHDPQVAAQAERVIEIRDGEI 221
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
1122-1288 5.47e-18

Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.


Pssm-ID: 213198 [Multi-domain]  Cd Length: 201  Bit Score: 83.70  E-value: 5.47e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1122 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEPILFDCSIAENI 1201
Cdd:cd03231     15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENL 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1202 AY--GDNSRvvsqEEIVRAAKEANIHAFiESLPnkystkvgdkGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTE 1279
Cdd:cd03231     95 RFwhADHSD----EQVEEALARVGLNGF-EDRP----------VAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKA 159

                   ....*....
gi 1149123047 1280 SEKVVQEAL 1288
Cdd:cd03231    160 GVARFAEAM 168
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
1119-1325 5.74e-18

ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.


Pssm-ID: 213184 [Multi-domain]  Cd Length: 200  Bit Score: 83.73  E-value: 5.74e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1119 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERF--YDPLAGKVLLDGKEIKRLNVQwLRAHLGI--VSQEPILFD 1194
Cdd:cd03217     12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPE-ERARLGIflAFQYPPEIP 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1195 csiaeniayGdnsrvVSQEEIVRAAKEAnihafieslpnkystkvgdkgtqLSGGQKQRIAIARALVRQPHILLLDEATS 1274
Cdd:cd03217     91 ---------G-----VKNADFLRYVNEG-----------------------FSGGEKKRNEILQLLLLEPDLAILDEPDS 133
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1149123047 1275 ALDTESEKVVQEALDKAR-EGRTCIVIAH--RLSTIQNADLIVVFQNGRVKEHG 1325
Cdd:cd03217    134 GLDIDALRLVAEVINKLReEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSG 187
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
1112-1325 6.08e-18

ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.


Pssm-ID: 213187 [Multi-domain]  Cd Length: 224  Bit Score: 84.12  E-value: 6.08e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1112 FNYPTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKeikrlnVQW-LRAHLGIVSQ-- 1188
Cdd:cd03220     27 GRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR------VSSlLGLGGGFNPElt 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1189 --EPILFDCSIaeniaYGdnsrvVSQEEIvrAAKEANIHAFIEsLPNKYSTKVGdkgtQLSGGQKQRIAIARALVRQPHI 1266
Cdd:cd03220    101 grENIYLNGRL-----LG-----LSRKEI--DEKIDEIIEFSE-LGDFIDLPVK----TYSSGMKARLAFAIATALEPDI 163
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1149123047 1267 LLLDEATSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTI-QNADLIVVFQNGRVKEHG 1325
Cdd:cd03220    164 LLIDEVLAVGDAAfQEKCQRRLRELLKQGKTVILVSHDPSSIkRLCDRALVLEKGKIRFDG 224
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
1121-1326 6.76e-18

retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]


Pssm-ID: 130324 [Multi-domain]  Cd Length: 2272  Bit Score: 90.46  E-value: 6.76e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1121 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRlNVQWLRAHLGIVSQEPILFD-CSIAE 1199
Cdd:TIGR01257  944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFHhLTVAE 1022
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1200 NIAYGDNSRVVSQEEivraaKEANIHAFIESlpNKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTE 1279
Cdd:TIGR01257 1023 HILFYAQLKGRSWEE-----AQLEMEAMLED--TGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPY 1095
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1149123047 1280 SEKVVQEALDKAREGRTCIVIAHRLStiqNADL----IVVFQNGRVKEHGT 1326
Cdd:TIGR01257 1096 SRRSIWDLLLKYRSGRTIIMSTHHMD---EADLlgdrIAIISQGRLYCSGT 1143
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
1122-1331 1.05e-17

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 84.65  E-value: 1.05e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1122 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEPIL-FDCSIAEN 1200
Cdd:PRK10253    22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTpGDITVQEL 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1201 IAYGdnsRVVSQEEIVRAAKEaNIHAFIESLPNKYSTKVGDKGTQ-LSGGQKQRIAIARALVRQPHILLLDEATSALDTE 1279
Cdd:PRK10253   102 VARG---RYPHQPLFTRWRKE-DEEAVTKAMQATGITHLADQSVDtLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDIS 177
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1149123047 1280 SEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVFQNGRVKEHGTHQQLL 1331
Cdd:PRK10253   178 HQIDLLELLSElnREKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIV 232
ABC_6TM_bac_exporter_ABCB8_10_like cd18575
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ...
824-1062 1.13e-17

Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.


Pssm-ID: 350019 [Multi-domain]  Cd Length: 289  Bit Score: 85.23  E-value: 1.13e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  824 LFSLLFLALGIISFITFFLqgftFGKAGEILTKRLRYMVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIGSRL 903
Cdd:cd18575     41 LLLAVALVLALASALRFYL----VSWLGERVVADLRKAVFAHLLRLSPSFFE--TTRTGEVLSRLTTDTTLIQTVVGSSL 114
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  904 AVITQNIANLGTGIIISFIYGWQLTLLLLAIVPIIAIAGVV---EMKMLSGQAlKDKkeLEGSGKIATEAIENFRTVVSL 980
Cdd:cd18575    115 SIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILfgrRVRRLSRAS-QDR--LADLSAFAEETLSAIKTVQAF 191
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  981 TQEQKFEHMYAQSLQVPYRNSLRKAHIFGITFSFTQAMMYFSYAGCFRFGAYLVAHKLMSFEDVL-LVFSAvVFGAMAVG 1059
Cdd:cd18575    192 TREDAERQRFATAVEAAFAAALRRIRARALLTALVIFLVFGAIVFVLWLGAHDVLAGRMSAGELSqFVFYA-VLAAGSVG 270

                   ...
gi 1149123047 1060 QVS 1062
Cdd:cd18575    271 ALS 273
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
1116-1301 1.46e-17

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 82.61  E-value: 1.46e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1116 TRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQ-EPILfd 1194
Cdd:PRK13539    11 VRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLGHRNAmKPAL-- 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1195 cSIAENIAYGDNSRVVSQEEIVRAAKEANIHAfIESLPNKYstkvgdkgtqLSGGQKQRIAIARALVRQPHILLLDEATS 1274
Cdd:PRK13539    89 -TVAENLEFWAAFLGGEELDIAAALEAVGLAP-LAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPTA 156
                          170       180
                   ....*....|....*....|....*..
gi 1149123047 1275 ALDTESEKVVQEALdKAREGRTCIVIA 1301
Cdd:PRK13539   157 ALDAAAVALFAELI-RAHLAQGGIVIA 182
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
1122-1326 1.49e-17

ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 83.59  E-value: 1.49e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1122 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKeikrlnVQWLrahLGI-VSQEPILfdcSIAEN 1200
Cdd:COG1134     41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR------VSAL---LELgAGFHPEL---TGREN 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1201 I-----AYGdnsrvVSQEEIvrAAKEANIHAFIE-----SLPNK-YSTkvgdkgtqlsgGQKQRIAIARALVRQPHILLL 1269
Cdd:COG1134    109 IylngrLLG-----LSRKEI--DEKFDEIVEFAElgdfiDQPVKtYSS-----------GMRARLAFAVATAVDPDILLV 170
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1149123047 1270 DEATSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGT 1326
Cdd:COG1134    171 DEVLAVGDAAfQKKCLARIRELRESGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGD 229
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
1123-1330 1.71e-17

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 83.91  E-value: 1.71e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1123 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFY--DPLAG-KVLLDGKEIKRL-----NVQWLRAHLGIVSQEPILFD 1194
Cdd:PRK09984    20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgDKSAGsHIELLGRTVQREgrlarDIRKSRANTGYIFQQFNLVN 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1195 -CSIAENIAYGDNSRVVSQEEIVRAAKEANIHAFIESLpnkysTKVG------DKGTQLSGGQKQRIAIARALVRQPHIL 1267
Cdd:PRK09984   100 rLSVLENVLIGALGSTPFWRTCFSWFTREQKQRALQAL-----TRVGmvhfahQRVSTLSGGQQQRVAIARALMQQAKVI 174
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1149123047 1268 LLDEATSALDTESEKVVQEALD--KAREGRTCIVIAHRLS-TIQNADLIVVFQNGRVKEHGTHQQL 1330
Cdd:PRK09984   175 LADEPIASLDPESARIVMDTLRdiNQNDGITVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQF 240
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
1116-1303 2.09e-17

ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).


Pssm-ID: 213190 [Multi-domain]  Cd Length: 166  Bit Score: 81.05  E-value: 2.09e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1116 TRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYdPLAGkvlldGKeIKRLnvqwLRAHLGIVSQEPILFDC 1195
Cdd:cd03223     10 TPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLW-PWGS-----GR-IGMP----EGEDLLFLPQRPYLPLG 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1196 SIAENIAYgdnsrvvsqeeivraakeanihafieslPnkystkvgdKGTQLSGGQKQRIAIARALVRQPHILLLDEATSA 1275
Cdd:cd03223     79 TLREQLIY----------------------------P---------WDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSA 121
                          170       180
                   ....*....|....*....|....*...
gi 1149123047 1276 LDTESEKVVQEALDKarEGRTCIVIAHR 1303
Cdd:cd03223    122 LDEESEDRLYQLLKE--LGITVISVGHR 147
ABC_6TM_TmrB_like cd18541
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ...
781-1040 2.82e-17

Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349985 [Multi-domain]  Cd Length: 293  Bit Score: 84.00  E-value: 2.82e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  781 FVVGVFCAIINGGLQpafaIIFSKIIGVFT-RIDDPETKRQNSNLFSLLFLALGIISFITFFLQGFTFGKAGEILTKRLR 859
Cdd:cd18541      1 YLLGILFLILVDLLQ----LLIPRIIGRAIdALTAGTLTASQLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLR 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  860 YMVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIGSRLAVITQNIANLGTGIIISFIYGWQLTLLLLAIVPIIA 939
Cdd:cd18541     77 NDLFAHLLTLSPSFYQ--KNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLA 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  940 IAGVVEMKMLSGQALKDKKELegsGKIATEAIENF---RTVVSLTQEQKFEHMYAQSLQVPYRNSLRKAHIFGITFSFTQ 1016
Cdd:cd18541    155 LLVYRLGKKIHKRFRKVQEAF---SDLSDRVQESFsgiRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIG 231
                          250       260
                   ....*....|....*....|....
gi 1149123047 1017 AMMYFSYAGCFRFGAYLVAHKLMS 1040
Cdd:cd18541    232 LLIGLSFLIVLWYGGRLVIRGTIT 255
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
1120-1333 2.92e-17

methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]


Pssm-ID: 132313 [Multi-domain]  Cd Length: 520  Bit Score: 86.78  E-value: 2.92e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1120 IPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLdgkeikRLNVQWL-----------RA--HLGIV 1186
Cdd:TIGR03269  297 VKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNV------RVGDEWVdmtkpgpdgrgRAkrYIGIL 370
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1187 SQEPILF-DCSIAENIaygdnSRVVSQEEIVRAAKEANIHAF-IESLPNKYSTKVGDKGT-QLSGGQKQRIAIARALVRQ 1263
Cdd:TIGR03269  371 HQEYDLYpHRTVLDNL-----TEAIGLELPDELARMKAVITLkMVGFDEEKAEEILDKYPdELSEGERHRVALAQVLIKE 445
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1149123047 1264 PHILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLLAQ 1333
Cdd:TIGR03269  446 PRIVILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIVEE 518
CeuD COG4604
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ...
1121-1326 3.03e-17

ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];


Pssm-ID: 443654 [Multi-domain]  Cd Length: 252  Bit Score: 82.82  E-value: 3.03e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1121 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEPILfdcsiaen 1200
Cdd:COG4604     15 VVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILRQENHI-------- 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1201 iaygdNSRVVSQE-------------------EIVRAAkeanIHAF-IESLPNKYSTkvgdkgtQLSGGQKQRIAIARAL 1260
Cdd:COG4604     87 -----NSRLTVRElvafgrfpyskgrltaedrEIIDEA----IAYLdLEDLADRYLD-------ELSGGQRQRAFIAMVL 150
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1149123047 1261 VRQPHILLLDEATSALD----TESEKVVQEAldkARE-GRTCIVIAHRLstiqN-----ADLIVVFQNGRVKEHGT 1326
Cdd:COG4604    151 AQDTDYVLLDEPLNNLDmkhsVQMMKLLRRL---ADElGKTVVIVLHDI----NfascyADHIVAMKDGRVVAQGT 219
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
444-681 3.11e-17

The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 87.02  E-value: 3.11e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  444 SIDSYSKSGHKPDNIKGNLEFRNVHFSYPSRKEVK-ILKGLNLKVQSGQTVALVGNSGCGKSTTVQ-LMQRLYDPTE--G 519
Cdd:TIGR00955    4 SWRNSDVFGRVAQDGSWKQLVSRLRGCFCRERPRKhLLKNVSGVAKPGELLAVMGSSGAGKTTLMNaLAFRSPKGVKgsG 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  520 MVSVDGqdiRTINVRFLREIIGVVSQEPVLFAT-TIAENI------RYGReNVTMDEIEKAVKEanaydFI--MKLPHKF 590
Cdd:TIGR00955   84 SVLLNG---MPIDAKEMRAISAYVQQDDLFIPTlTVREHLmfqahlRMPR-RVTKKEKRERVDE-----VLqaLGLRKCA 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  591 DTLVGERGAQ--LSGGQKQRIAIARALVRNPKILLLDEATSALDTESEA-VVQVALDKARKGRTTIVIAHRLStvrnADV 667
Cdd:TIGR00955  155 NTRIGVPGRVkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYsVVQVLKGLAQKGKTIICTIHQPS----SEL 230
                          250
                   ....*....|....
gi 1149123047  668 IAGFDDGVIVEKGN 681
Cdd:TIGR00955  231 FELFDKIILMAEGR 244
ABC_6TM_exporter_like cd18563
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
217-407 3.21e-17

Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 350007 [Multi-domain]  Cd Length: 296  Bit Score: 83.71  E-value: 3.21e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  217 IRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQSMATFFTGFIVGFTRGWKLTLVILAISPVLG 296
Cdd:cd18563     78 LRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVV 157
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  297 -LSAAVWAKILSSFTdKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKRIGIKKAITANISIGAAFLL 375
Cdd:cd18563    158 wGSYFFWKKIRRLFH-RQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFPLLTFL 236
                          170       180       190
                   ....*....|....*....|....*....|..
gi 1149123047  376 IYASYALAFWYGTTLVLSGEYSIGqVLTVFFS 407
Cdd:cd18563    237 TSLGTLIVWYFGGRQVLSGTMTLG-TLVAFLS 267
cbiO PRK13645
energy-coupling factor transporter ATPase;
1103-1333 3.67e-17

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 83.52  E-value: 3.67e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1103 GNVTFGEVVFNYPTRP--DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEI-----KRLN 1175
Cdd:PRK13645     5 KDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpanlkKIKE 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1176 VQWLRAHLGIVSQEP--ILFDCSIAENIAYGDNSRVVSQEEIVRAAKEAnihAFIESLPNKYSTKvgdKGTQLSGGQKQR 1253
Cdd:PRK13645    85 VKRLRKEIGLVFQFPeyQLFQETIEKDIAFGPVNLGENKQEAYKKVPEL---LKLVQLPEDYVKR---SPFELSGGQKRR 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1254 IAIARALVRQPHILLLDEATSALDTESEK---VVQEALDKaREGRTCIVIAHRLSTI-QNADLIVVFQNGRVKEHG---- 1325
Cdd:PRK13645   159 VALAGIIAMDGNTLVLDEPTGGLDPKGEEdfiNLFERLNK-EYKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGspfe 237
                          250
                   ....*....|
gi 1149123047 1326 --THQQLLAQ 1333
Cdd:PRK13645   238 ifSNQELLTK 247
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
475-709 4.89e-17

methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]


Pssm-ID: 132313 [Multi-domain]  Cd Length: 520  Bit Score: 86.01  E-value: 4.89e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  475 KEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRL--YDPTEGMV----------------SVDGQDI-------- 528
Cdd:TIGR03269   11 DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgyverpSKVGEPCpvcggtle 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  529 ----------RTINVRFLREIigvvsqePVLFATTIAeniRYGRENV------TMDEIEKAVKEA--NAYDFI--MKLPH 588
Cdd:TIGR03269   91 peevdfwnlsDKLRRRIRKRI-------AIMLQRTFA---LYGDDTVldnvleALEEIGYEGKEAvgRAVDLIemVQLSH 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  589 KFDTLVGErgaqLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARK--GRTTIVIAHRLSTVRN-A 665
Cdd:TIGR03269  161 RITHIARD----LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKasGISMVLTSHWPEVIEDlS 236
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1149123047  666 DVIAGFDDGVIVEKGNHDELMKekgIYFKLVTMQTAGNEVELEN 709
Cdd:TIGR03269  237 DKAIWLENGEIKEEGTPDEVVA---VFMEGVSEVEKECEVEVGE 277
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
480-657 6.02e-17

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 81.46  E-value: 6.02e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  480 LKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDI---RTINVRFLREIIGVVSQE---------- 546
Cdd:PRK10908    18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlKNREVPFLRRQIGMIFQDhhllmdrtvy 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  547 -----PVLFATTIAENIRYgRENVTMDEIEKAVKEANaydfimkLPhkfdtlvgergAQLSGGQKQRIAIARALVRNPKI 621
Cdd:PRK10908    98 dnvaiPLIIAGASGDDIRR-RVSAALDKVGLLDKAKN-------FP-----------IQLSGGEQQRVGIARAVVNKPAV 158
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1149123047  622 LLLDEATSALDTE-SEAVVQVALDKARKGRTTIVIAH 657
Cdd:PRK10908   159 LLADEPTGNLDDAlSEGILRLFEEFNRVGVTVLMATH 195
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
1123-1330 6.31e-17

Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213232 [Multi-domain]  Cd Length: 220  Bit Score: 81.26  E-value: 6.31e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1123 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRlNVQWLRAHLGIVSQEPILFDCSIA-ENI 1201
Cdd:cd03265     16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLSVDDELTGwENL 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1202 A-----YGdnsrvVSQEEivRAAKEANIHAFIEslpnkystkVGDKGTQL----SGGQKQRIAIARALVRQPHILLLDEA 1272
Cdd:cd03265     95 YiharlYG-----VPGAE--RRERIDELLDFVG---------LLEAADRLvktySGGMRRRLEIARSLVHRPEVLFLDEP 158
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1149123047 1273 TSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTI-QNADLIVVFQNGRVKEHGTHQQL 1330
Cdd:cd03265    159 TIGLDPQTRAHVWEYIEKlkEEFGMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPEEL 219
ABC_6TM_ABCB9_like cd18784
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ...
817-1040 6.36e-17

Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit.


Pssm-ID: 350057 [Multi-domain]  Cd Length: 289  Bit Score: 82.74  E-value: 6.36e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  817 TKRQNSNLFSLLFLALGIISFITFFLQG-----FTFGKAGeiLTKRLRYMVFRSMLRQDVSWFDdpKNTTGALTTRLAND 891
Cdd:cd18784     27 VIEKSQDKFSRAIIIMGLLAIASSVAAGirgglFTLAMAR--LNIRIRNLLFRSIVSQEIGFFD--TVKTGDITSRLTSD 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  892 AAQVKGAIGSRLAVITQNIANLGTGIIISFIYGWQLTLLLLAIVPIIAIAGVVEMKMLSGQALKDKKELEGSGKIATEAI 971
Cdd:cd18784    103 TTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYYKKLSKAVQDSLAKANEVAEETI 182
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  972 ENFRTVVSLTQEQKFEHMYAQSLQVPYRNSLRKAHIFGiTFSFTQAMMYFS-YAGCFRFGAYLVAHKLMS 1040
Cdd:cd18784    183 SSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEALAYG-GYVWSNELTELAlTVSTLYYGGHLVITGQIS 251
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
462-657 6.62e-17

ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.


Pssm-ID: 213188 [Multi-domain]  Cd Length: 144  Bit Score: 79.03  E-value: 6.62e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVdGQDIRtinvrflreiIG 541
Cdd:cd03221      1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW-GSTVK----------IG 66
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  542 VVsqepvlfattiaenirygrenvtmdeiekavkeanaydfimklphkfdtlvgergAQLSGGQKQRIAIARALVRNPKI 621
Cdd:cd03221     67 YF-------------------------------------------------------EQLSGGEKMRLALAKLLLENPNL 91
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1149123047  622 LLLDEATSALDTESEAVVQVALdKARKGrTTIVIAH 657
Cdd:cd03221     92 LLLDEPTNHLDLESIEALEEAL-KEYPG-TVILVSH 125
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
462-688 7.02e-17

ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 81.67  E-value: 7.02e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYP-------------------SRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVS 522
Cdd:COG1134      5 IEVENVSKSYRlyhepsrslkelllrrrrtRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  523 VDGqdirtiNVRFLREIIGVVSQEpvlfaTTIAENIR-----YGrenVTMDEIEKAVKEANAY----DFImklphkfDTL 593
Cdd:COG1134     85 VNG------RVSALLELGAGFHPE-----LTGRENIYlngrlLG---LSRKEIDEKFDEIVEFaelgDFI-------DQP 143
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  594 VGergaQLSGGQKQRIAIARALVRNPKILLLDEATSALDTE----SEAVVQvalDKARKGRTTIVIAHRLSTVRN-ADVI 668
Cdd:COG1134    144 VK----TYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAfqkkCLARIR---ELRESGRTVIFVSHSMGAVRRlCDRA 216
                          250       260
                   ....*....|....*....|
gi 1149123047  669 AGFDDGVIVEKGNHDELMKE 688
Cdd:COG1134    217 IWLEKGRLVMDGDPEEVIAA 236
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
449-680 7.64e-17

ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.


Pssm-ID: 213187 [Multi-domain]  Cd Length: 224  Bit Score: 81.04  E-value: 7.64e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  449 SKSGHKPDNIKGNLEFRNVHFSYPSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQD- 527
Cdd:cd03220      7 SKSYPTYKGGSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVs 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  528 -IRTINVRFLREIIGVvsqepvlfattiaENIR-YGRE-NVTMDEIEKavKEANAYDFiMKLPHKFDTLVGErgaqLSGG 604
Cdd:cd03220     87 sLLGLGGGFNPELTGR-------------ENIYlNGRLlGLSRKEIDE--KIDEIIEF-SELGDFIDLPVKT----YSSG 146
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1149123047  605 QKQRIAIARALVRNPKILLLDEATSALDTE-SEAVVQVALDKARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKG 680
Cdd:cd03220    147 MKARLAFAIATALEPDILLIDEVLAVGDAAfQEKCQRRLRELLKQGKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
1125-1330 9.55e-17

leucine/isoleucine/valine transporter ATP-binding subunit; Provisional


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 81.57  E-value: 9.55e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1125 GLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLrAHLGIVS--QEPILF-DCSIAENI 1201
Cdd:PRK11300    23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQI-ARMGVVRtfQHVRLFrEMTVIENL 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1202 aygdnsrVVSQEEIV---------------RAAKEANIHAF-------IESLPNKystkvgDKGTqLSGGQKQRIAIARA 1259
Cdd:PRK11300   102 -------LVAQHQQLktglfsgllktpafrRAESEALDRAAtwlervgLLEHANR------QAGN-LAYGQQRRLEIARC 167
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1149123047 1260 LVRQPHILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQL 1330
Cdd:PRK11300   168 MVTQPEILMLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEI 241
ABC_6TM_Tm288_like cd18547
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ...
158-407 1.14e-16

Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349991 [Multi-domain]  Cd Length: 298  Bit Score: 82.07  E-value: 1.14e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  158 LMSNITNR-SDINDTGFFMNLEEdMTRYAYYYSGIGAGVLVAAYIQvSFWCLAAGRQI-HKIRKQFFHAIMRQEIGWFDV 235
Cdd:cd18547     21 LLGKAIDLiIEGLGGGGGVDFSG-LLRILLLLLGLYLLSALFSYLQ-NRLMARVSQRTvYDLRKDLFEKLQRLPLSYFDT 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  236 HDVGELNTRLTDDVSKINEGIGDKIGMFFQSMATFFTGFIVGFTRGWKLTLVILAISPVLGLSAAVWAKILSSFTDKELL 315
Cdd:cd18547     99 HSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLLVTKFIAKRSQKYFRKQQK 178
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  316 AYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKRIGIKKAITANISIGAAFLLIYASYALAFWYGTTLVLSGE 395
Cdd:cd18547    179 ALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFKAQFYSGLLMPIMNFINNLGYVLVAVVGGLLVINGA 258
                          250
                   ....*....|..
gi 1149123047  396 YSIGqVLTVFFS 407
Cdd:cd18547    259 LTVG-VIQAFLQ 269
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
1117-1301 1.41e-16

heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]


Pssm-ID: 273491 [Multi-domain]  Cd Length: 198  Bit Score: 79.71  E-value: 1.41e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1117 RPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQEPILFDCS 1196
Cdd:TIGR01189   10 RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELS 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1197 IAENIAY-----GDNSRVVSQeeivrAAKEANIHAFiESLPnkystkvgdkGTQLSGGQKQRIAIARALVRQPHILLLDE 1271
Cdd:TIGR01189   90 ALENLHFwaaihGGAQRTIED-----ALAAVGLTGF-EDLP----------AAQLSAGQQRRLALARLWLSRRPLWILDE 153
                          170       180       190
                   ....*....|....*....|....*....|
gi 1149123047 1272 ATSALDTESEKVVQEALDkAREGRTCIVIA 1301
Cdd:TIGR01189  154 PTTALDKAGVALLAGLLR-AHLARGGIVLL 182
GguA NF040905
sugar ABC transporter ATP-binding protein;
462-678 1.41e-16

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 84.46  E-value: 1.41e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSrkeVKILKGLNLKVQSGQTVALVGNSGCGKSTtvqLMQRL-----YDPTEGMVSVDGQ-----DIRTi 531
Cdd:NF040905     2 LEMRGITKTFPG---VKALDDVNLSVREGEIHALCGENGAGKST---LMKVLsgvypHGSYEGEILFDGEvcrfkDIRD- 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  532 nvrflREIIGVV--SQE----PVLfatTIAENIRYGRENVTMDEI--EKAVKEANAYDFIMKLPHKFDTLVGERGAqlsg 603
Cdd:NF040905    75 -----SEALGIViiHQElaliPYL---SIAENIFLGNERAKRGVIdwNETNRRARELLAKVGLDESPDTLVTDIGV---- 142
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1149123047  604 GQKQRIAIARALVRNPKILLLDEATSAL-DTESEAVVQVALDKARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVE 678
Cdd:NF040905   143 GKQQLVEIAKALSKDVKLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIRRvADSITVLRDGRTIE 219
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
1120-1321 1.42e-16

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 84.72  E-value: 1.42e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1120 IPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVqwLRAH-LGI--VSQEPILF-DC 1195
Cdd:PRK15439    24 VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTP--AKAHqLGIylVPQEPLLFpNL 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1196 SIAENIAYGDNSRVVSQEEIVRAAKEANIHAFIESLPNkySTKVGDkgtqlsggqKQRIAIARALVRQPHILLLDEATSA 1275
Cdd:PRK15439   102 SVKENILFGLPKRQASMQKMKQLLAALGCQLDLDSSAG--SLEVAD---------RQIVEILRGLMRDSRILILDEPTAS 170
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1149123047 1276 LD-TESEKV---VQEALDKareGRTCIVIAHRLSTI-QNADLIVVFQNGRV 1321
Cdd:PRK15439   171 LTpAETERLfsrIRELLAQ---GVGIVFISHKLPEIrQLADRISVMRDGTI 218
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
462-686 1.68e-16

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 80.99  E-value: 1.68e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVH--FSYPS----RKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDG---------- 525
Cdd:PRK15112     5 LEVRNLSktFRYRTgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDhplhfgdysy 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  526 --QDIRTI-----NVRFLREIIGVVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYdfimklPHkfdtlvgerg 598
Cdd:PRK15112    85 rsQRIRMIfqdpsTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLLPDHASYY------PH---------- 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  599 aQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEA-VVQVALD-KARKGRTTIVIAHRLSTVRN-ADVIAGFDDGV 675
Cdd:PRK15112   149 -MLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSqLINLMLElQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGE 227
                          250
                   ....*....|.
gi 1149123047  676 IVEKGNHDELM 686
Cdd:PRK15112   228 VVERGSTADVL 238
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
479-686 2.21e-16

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 80.80  E-value: 2.21e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  479 ILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIGVVSQEPVLFA-TTIAEN 557
Cdd:PRK10253    22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGdITVQEL 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  558 IRYGRE------NVTMDEIEKAVKEANAYDFIMKLP-HKFDTlvgergaqLSGGQKQRIAIARALVRNPKILLLDEATSA 630
Cdd:PRK10253   102 VARGRYphqplfTRWRKEDEEAVTKAMQATGITHLAdQSVDT--------LSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1149123047  631 LDTESEA-VVQVALDKAR-KGRTTIVIAHRLS-TVRNADVIAGFDDGVIVEKGNHDELM 686
Cdd:PRK10253   174 LDISHQIdLLELLSELNReKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIV 232
ABC_6TM_TAP1 cd18589
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ...
143-403 2.56e-16

Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.


Pssm-ID: 350033 [Multi-domain]  Cd Length: 289  Bit Score: 80.98  E-value: 2.56e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  143 GEMTDIFANAGNLEDLMSNITnrsdindtgfFMNLeedmtryayyysgIGAGVLVAAYIQVSFWCLAAGRQIHKIRKQFF 222
Cdd:cd18589     20 GRMTDWIMNKDAPEAFTAAIT----------VMSL-------------LTIASAVSEFVCDLIYNITMSRIHSRLQGLVF 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  223 HAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQSMATFFTGFIVGFTRGWKLTLVILAISPVLGLSAAVW 302
Cdd:cd18589     77 AAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLTALGLPLLLLVPKFV 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  303 AKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKRIGIKKAITANISIGAAFLLIYASYAL 382
Cdd:cd18589    157 GKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEEGEAQRYRQRLQKTYRLNKKEAAAYAVSMWTSSFSGLALKVG 236
                          250       260
                   ....*....|....*....|.
gi 1149123047  383 AFWYGTTLVLSGEYSIGQVLT 403
Cdd:cd18589    237 ILYYGGQLVTAGTVSSGDLVT 257
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
1121-1320 3.11e-16

ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.


Pssm-ID: 213188 [Multi-domain]  Cd Length: 144  Bit Score: 77.10  E-value: 3.11e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1121 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLerfydplAGKvlldgkeikrlnvqwLRAHLGIVSQEPILfdcsiaeN 1200
Cdd:cd03221     14 LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLI-------AGE---------------LEPDEGIVTWGSTV-------K 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1201 IAYgdnsrvvsqeeivraakeanihafiesLPnkystkvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEATSALDTES 1280
Cdd:cd03221     65 IGY---------------------------FE------------QLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLES 105
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1149123047 1281 EKVVQEALdKAREGrTCIVIAHRLSTIQN-ADLIVVFQNGR 1320
Cdd:cd03221    106 IEALEEAL-KEYPG-TVILVSHDRYFLDQvATKIIELEDGK 144
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
1116-1330 3.86e-16

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 80.19  E-value: 3.86e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1116 TRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWL---RAHLGIVSQEPIL 1192
Cdd:PRK11831    16 TRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRKRMSMLFQSGAL 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1193 F-DCSIAENIAYGDNSRVVSQEEIVRAAKEANIHAfieslpnkystkVGDKG------TQLSGGQKQRIAIARALVRQPH 1265
Cdd:PRK11831    96 FtDMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEA------------VGLRGaaklmpSELSGGMARRAALARAIALEPD 163
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1149123047 1266 ILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQL 1330
Cdd:PRK11831   164 LIMFDEPFVGQDPITMGVLVKLISELNSalGVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQAL 231
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
1117-1330 4.30e-16

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 83.37  E-value: 4.30e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1117 RPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLR--------------AH 1182
Cdd:PRK10261    26 QQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRQVIElseqsaaqmrhvrgAD 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1183 LGIVSQEPI-----LFDC--SIAENIAYGDNsrvVSQEEIVRAAKEANIHAFI---ESLPNKYStkvgdkgTQLSGGQKQ 1252
Cdd:PRK10261   106 MAMIFQEPMtslnpVFTVgeQIAESIRLHQG---ASREEAMVEAKRMLDQVRIpeaQTILSRYP-------HQLSGGMRQ 175
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1253 RIAIARALVRQPHILLLDEATSALDTESE-------KVVQEALDKAregrtCIVIAHRLSTIQN-ADLIVVFQNGRVKEH 1324
Cdd:PRK10261   176 RVMIAMALSCRPAVLIADEPTTALDVTIQaqilqliKVLQKEMSMG-----VIFITHDMGVVAEiADRVLVMYQGEAVET 250

                   ....*.
gi 1149123047 1325 GTHQQL 1330
Cdd:PRK10261   251 GSVEQI 256
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
473-637 5.87e-16

Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.


Pssm-ID: 213198 [Multi-domain]  Cd Length: 201  Bit Score: 77.92  E-value: 5.87e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  473 SRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIGVVSQEPVLFAT 552
Cdd:cd03231      9 ERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTL 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  553 TIAENIRYGRENVTMDEIEKAVKEANAYDFimklphkFDTLVgergAQLSGGQKQRIAIARALVRNPKILLLDEATSALD 632
Cdd:cd03231     89 SVLENLRFWHADHSDEQVEEALARVGLNGF-------EDRPV----AQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157

                   ....*
gi 1149123047  633 TESEA 637
Cdd:cd03231    158 KAGVA 162
PvdE COG4615
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...
185-626 7.17e-16

ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];


Pssm-ID: 443659 [Multi-domain]  Cd Length: 547  Bit Score: 82.54  E-value: 7.17e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  185 AYYYSGIGAGVLVAAYIQvsfwclaagRQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVskinegigDKIGMFF 264
Cdd:COG4615     60 LLLLSRLASQLLLTRLGQ---------HAVARLRLRLSRRILAAPLERLERIGAARLLAALTEDV--------RTISQAF 122
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  265 QSMATFFTGFIVGFtrgwkLTLVILA-ISPVLGLSAAVWAkILSSFTDKELLAYAKAG----AVAEEVL-AAIRTVIafG 338
Cdd:COG4615    123 VRLPELLQSVALVL-----GCLAYLAwLSPPLFLLTLVLL-GLGVAGYRLLVRRARRHlrraREAEDRLfKHFRALL--E 194
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  339 GQKkEL----ER----YNKNLE---EAKRIGIKKAITANISIGA-AFLLIYASYALAFWYGTTLV-LSGEYSIGQVLTVF 405
Cdd:COG4615    195 GFK-ELklnrRRrrafFDEDLQptaERYRDLRIRADTIFALANNwGNLLFFALIGLILFLLPALGwADPAVLSGFVLVLL 273
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  406 FsvLIGAfsVGQASPSIEAFANARgAAYEifKIIDNKPSIDSYSKSGHKPDNIKGN-----LEFRNVHFSYPSRKEVK-- 478
Cdd:COG4615    274 F--LRGP--LSQLVGALPTLSRAN-VALR--KIEELELALAAAEPAAADAAAPPAPadfqtLELRGVTYRYPGEDGDEgf 346
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  479 ILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIGVVSQEPVLFATTiaeni 558
Cdd:COG4615    347 TLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFDRL----- 421
                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1149123047  559 rYGRENVTMDEiekavkEANAYDFIMKLPHK-------FDTLvgergaQLSGGQKQRIAIARALVRNPKILLLDE 626
Cdd:COG4615    422 -LGLDGEADPA------RARELLERLELDHKvsvedgrFSTT------DLSQGQRKRLALLVALLEDRPILVFDE 483
PRK10522 PRK10522
multidrug transporter membrane component/ATP-binding component; Provisional
1091-1333 9.15e-16

multidrug transporter membrane component/ATP-binding component; Provisional


Pssm-ID: 236707 [Multi-domain]  Cd Length: 547  Bit Score: 82.33  E-value: 9.15e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1091 YSTEGLMPNTLEG--NVTFGEVVFNYPTR-----PdipvlqgLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGK 1163
Cdd:PRK10522   307 YKAEFPRPQAFPDwqTLELRNVTFAYQDNgfsvgP-------INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGE 379
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1164 VLLDGKEIKRLNVQWLRAHLGIVSQEPILFDcsiaeniaygdnsRVVSQEEivRAAKEANIHAFIESLPNKYSTKVGD-- 1241
Cdd:PRK10522   380 ILLDGKPVTAEQPEDYRKLFSAVFTDFHLFD-------------QLLGPEG--KPANPALVEKWLERLKMAHKLELEDgr 444
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1242 -KGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVV-QEALDKARE-GRTCIVIAHRLSTIQNADLIVVFQN 1318
Cdd:PRK10522   445 iSNLKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFyQVLLPLLQEmGKTIFAISHDDHYFIHADRLLEMRN 524
                          250
                   ....*....|....*.
gi 1149123047 1319 GRVKE-HGTHQQLLAQ 1333
Cdd:PRK10522   525 GQLSElTGEERDAASR 540
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
477-674 9.99e-16

D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 131681 [Multi-domain]  Cd Length: 500  Bit Score: 81.79  E-value: 9.99e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  477 VKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLY--DPTEGMVSVDGQDIRTINVRFL-REIIGVVSQEPVLFAT- 552
Cdd:TIGR02633   14 VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSPLKASNIRDTeRAGIVIIHQELTLVPEl 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  553 TIAENIRYGRE----NVTMDEIEkAVKEANAYDFIMKLPHKFDTL-VGERGaqlsGGQKQRIAIARALVRNPKILLLDEA 627
Cdd:TIGR02633   94 SVAENIFLGNEitlpGGRMAYNA-MYLRAKNLLRELQLDADNVTRpVGDYG----GGQQQLVEIAKALNKQARLLILDEP 168
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1149123047  628 TSAL-DTESEAVVQVALDKARKGRTTIVIAHRLSTVRN-ADVIAGFDDG 674
Cdd:TIGR02633  169 SSSLtEKETEILLDIIRDLKAHGVACVYISHKLNEVKAvCDTICVIRDG 217
GguA NF040905
sugar ABC transporter ATP-binding protein;
1116-1323 1.20e-15

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 81.37  E-value: 1.20e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1116 TRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYdP---LAGKVLLDGKEIKRLNvqwLRA--HLGIV--SQ 1188
Cdd:NF040905    10 TFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PhgsYEGEILFDGEVCRFKD---IRDseALGIViiHQ 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1189 E----PILfdcSIAENIAYGdNSR----VVSQEEIVRAAKEANIHAFIESLPNkysTKVGDKGTqlsgGQKQRIAIARAL 1260
Cdd:NF040905    86 ElaliPYL---SIAENIFLG-NERakrgVIDWNETNRRARELLAKVGLDESPD---TLVTDIGV----GKQQLVEIAKAL 154
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1149123047 1261 VRQPHILLLDEATSAL-DTESEKVVQEALDKAREGRTCIVIAHRLSTI-QNADLIVVFQNGRVKE 1323
Cdd:NF040905   155 SKDVKLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIrRVADSITVLRDGRTIE 219
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
1120-1336 1.26e-15

high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 78.00  E-value: 1.26e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1120 IPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIkrlnVQW-----LRAHLGIVSQEPILFD 1194
Cdd:PRK11614    18 IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDI----TDWqtakiMREAVAIVPEGRRVFS 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1195 -CSIAENIAYGD--NSRVVSQEEIVRAakeanihafIESLPNKYSTKVGDKGTqLSGGQKQRIAIARALVRQPHILLLDE 1271
Cdd:PRK11614    94 rMTVEENLAMGGffAERDQFQERIKWV---------YELFPRLHERRIQRAGT-MSGGEQQMLAIGRALMSQPRLLLLDE 163
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1272 ATSALdteSEKVVQEALDKAR----EGRTCIVIAHRLS-TIQNADLIVVFQNGRVKEHGTHQQLLAQKGI 1336
Cdd:PRK11614   164 PSLGL---APIIIQQIFDTIEqlreQGMTIFLVEQNANqALKLADRGYVLENGHVVLEDTGDALLANEAV 230
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
463-842 1.36e-15

Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 82.85  E-value: 1.36e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  463 EFRNVHFSYPSRKEVK-ILKGLNLKVQSGQTVALVGNSGCGKSTTVQ-LMQRLydpTEGMVSvdgQDIRTINVRFLRE-- 538
Cdd:TIGR00956  761 HWRNLTYEVKIKKEKRvILNNVDGWVKPGTLTALMGASGAGKTTLLNvLAERV---TTGVIT---GGDRLVNGRPLDSsf 834
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  539 --IIGVVSQEPVLFAT-TIAENIRYGRENVTMDEIEKavKEANAY-DFIMKL---PHKFDTLVGERGAQLSGGQKQRIAI 611
Cdd:TIGR00956  835 qrSIGYVQQQDLHLPTsTVRESLRFSAYLRQPKSVSK--SEKMEYvEEVIKLlemESYADAVVGVPGEGLNVEQRKRLTI 912
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  612 ARALVRNPKILL-LDEATSALDTESEAVVQVALDK-ARKGRTTIVIAHRLStvrnADVIAGFDDGVIVEKGNHDELMKEK 689
Cdd:TIGR00956  913 GVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKlADHGQAILCTIHQPS----AILFEEFDRLLLLQKGGQTVYFGDL 988
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  690 GI-------YFK---LVTMQTAGNEVE--LE--NAADESKSEIDALEMSSNDSRSSLIRKRSTRRSVRGSQAQDrkLSTK 755
Cdd:TIGR00956  989 GEnshtiinYFEkhgAPKCPEDANPAEwmLEviGAAPGAHANQDYHEVWRNSSEYQAVKNELDRLEAELSKAED--DNDP 1066
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  756 EALDESIPP-------------VSFWRIMKLNlteWPYFVVGVFCAIING-----------GLQPAFAIIFSKIIGVFTR 811
Cdd:TIGR00956 1067 DALSKYAASlwyqfklvlwrtfQQYWRTPDYL---YSKFFLTIFAALFIGftffkvgtslqGLQNQMFAVFMATVLFNPL 1143
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|...
gi 1149123047  812 I-----------DDPETKRQNSNLFS-LLFLALGIISFITFFL 842
Cdd:TIGR00956 1144 IqqylppfvaqrDLYEVRERPSRTFSwLAFIAAQITVEIPYNL 1186
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
466-677 1.43e-15

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 79.77  E-value: 1.43e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  466 NVHFSYPSrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTV-QLMQRLYDP--TEGMVSVDGQDIRTINVRFLREI--- 539
Cdd:PRK09473    19 RVTFSTPD-GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAfALMGLLAANgrIGGSATFNGREILNLPEKELNKLrae 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  540 -IGVVSQEPVlfaTTIAENIRYG-------------------RENVTMDEiekAVKEANAYDFIMKLPHKFdtlvgerga 599
Cdd:PRK09473    98 qISMIFQDPM---TSLNPYMRVGeqlmevlmlhkgmskaeafEESVRMLD---AVKMPEARKRMKMYPHEF--------- 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  600 qlSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARKGRTT--IVIAHRLStvrnadVIAGFDDGVIV 677
Cdd:PRK09473   163 --SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaiIMITHDLG------VVAGICDKVLV 234
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
477-680 1.51e-15

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 81.37  E-value: 1.51e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  477 VKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREI-IGVVSQE-PVLFATTI 554
Cdd:PRK09700    18 VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLgIGIIYQElSVIDELTV 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  555 AENIRYGRE------NVTMDEIEKAVKEANAYDFIMKLPHKFDTLVGErgaqLSGGQKQRIAIARALVRNPKILLLDEAT 628
Cdd:PRK09700    98 LENLYIGRHltkkvcGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVAN----LSISHKQMLEIAKTLMLDAKVIIMDEPT 173
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1149123047  629 SALDTESEAVVQVALDKARK-GRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKG 680
Cdd:PRK09700   174 SSLTNKEVDYLFLIMNQLRKeGTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSG 227
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
1119-1332 1.57e-15

methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]


Pssm-ID: 132313 [Multi-domain]  Cd Length: 520  Bit Score: 81.39  E-value: 1.57e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1119 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERF--YDPLAGKVLLD---GKEIKRLNVQwlrAHLG--------- 1184
Cdd:TIGR03269   12 GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHvalCEKCGYVERP---SKVGepcpvcggt 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1185 IVSQEPILFDCS------IAENIA---------YGDNSRVV----SQEEIVRAAKEANIHA--FIESLpnKYSTKVGDKG 1243
Cdd:TIGR03269   89 LEPEEVDFWNLSdklrrrIRKRIAimlqrtfalYGDDTVLDnvleALEEIGYEGKEAVGRAvdLIEMV--QLSHRITHIA 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1244 TQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKA--REGRTCIVIAHRLSTIQN-ADLIVVFQNGR 1320
Cdd:TIGR03269  167 RDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvkASGISMVLTSHWPEVIEDlSDKAIWLENGE 246
                          250
                   ....*....|..
gi 1149123047 1321 VKEHGTHQQLLA 1332
Cdd:TIGR03269  247 IKEEGTPDEVVA 258
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
1117-1331 1.80e-15

The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 81.63  E-value: 1.80e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1117 RPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLErFYDP----LAGKVLLDGKeikRLNVQWLRAHLGIVSQEPIL 1192
Cdd:TIGR00955   35 RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPkgvkGSGSVLLNGM---PIDAKEMRAISAYVQQDDLF 110
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1193 FDCSIA-ENIAYgdNSRVVSQEEIVRAAKEANIHAFIE--SLPNKYSTKVGDKGTQ--LSGGQKQRIAIARALVRQPHIL 1267
Cdd:TIGR00955  111 IPTLTVrEHLMF--QAHLRMPRRVTKKEKRERVDEVLQalGLRKCANTRIGVPGRVkgLSGGERKRLAFASELLTDPPLL 188
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1149123047 1268 LLDEATSALDTES-EKVVQEALDKAREGRTCIVIAHRLST--IQNADLIVVFQNGRVKEHGTHQQLL 1331
Cdd:TIGR00955  189 FCDEPTSGLDSFMaYSVVQVLKGLAQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQAV 255
ABC_6TM_TAP2 cd18590
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ...
812-1018 2.28e-15

Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.


Pssm-ID: 350034 [Multi-domain]  Cd Length: 289  Bit Score: 78.15  E-value: 2.28e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  812 IDDPETKRQNSNLFSLLFLaLGIISFITFFLQG-----FTFgkAGEILTKRLRYMVFRSMLRQDVSWFDdpKNTTGALTT 886
Cdd:cd18590     23 IDILGGEYQHNAFTSAIGL-MCLFSLGSSLSAGlrgglFMC--TLSRLNLRLRHQLFSSLVQQDIGFFE--KTKTGDLTS 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  887 RLANDAAQVKGAIGSRLAVITQN-IANLGTgiiISFIYG--WQLTLLLLAIVPIIAIAgvveMKMLSGQALKDKKELEGS 963
Cdd:cd18590     98 RLSTDTTLMSRSVALNANVLLRSlVKTLGM---LGFMLSlsWQLTLLTLIEMPLTAIA----QKVYNTYHQKLSQAVQDS 170
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1149123047  964 ----GKIATEAIENFRTVVSLTQEQKFEHMYAQSLQVPYRNSLRKAHIFGITFSFTQAM 1018
Cdd:cd18590    171 iakaGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTVRAVYLLVRRVL 229
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
462-631 2.94e-15

high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 76.84  E-value: 2.94e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYpsrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTI-NVRFLREII 540
Cdd:PRK11614     6 LSFDKVSAHY---GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWqTAKIMREAV 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  541 GVVSQEPVLFA-TTIAENIRYGRENVTMDEIEKAVKEAnaYDFIMKLPHKfdtlVGERGAQLSGGQKQRIAIARALVRNP 619
Cdd:PRK11614    83 AIVPEGRRVFSrMTVEENLAMGGFFAERDQFQERIKWV--YELFPRLHER----RIQRAGTMSGGEQQMLAIGRALMSQP 156
                          170
                   ....*....|..
gi 1149123047  620 KILLLDEATSAL 631
Cdd:PRK11614   157 RLLLLDEPSLGL 168
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
462-685 3.34e-15

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 80.13  E-value: 3.34e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSRKEVK-ILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYdPT------EGMVSVDGQDIRTINVR 534
Cdd:PRK15134     6 LAIENLSVAFRQQQTVRtVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLL-PSppvvypSGDIRFHGESLLHASEQ 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  535 FLREI----IGVVSQEPVLFAT---TIAENI-------RYGRENVTMDE---------IEKAVKEANAYdfimklPHkfd 591
Cdd:PRK15134    85 TLRGVrgnkIAMIFQEPMVSLNplhTLEKQLyevlslhRGMRREAARGEilncldrvgIRQAAKRLTDY------PH--- 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  592 tlvgergaQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARK--GRTTIVIAHRLSTVRN-ADVI 668
Cdd:PRK15134   156 --------QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKlADRV 227
                          250
                   ....*....|....*..
gi 1149123047  669 AGFDDGVIVEKGNHDEL 685
Cdd:PRK15134   228 AVMQNGRCVEQNRAATL 244
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
1118-1319 4.42e-15

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 79.66  E-value: 4.42e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1118 PDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIK----RLNVQwlrAHLGIVSQEPILF 1193
Cdd:PRK10762    15 PGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfngpKSSQE---AGIGIIHQELNLI 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1194 D-CSIAENIAYGdnsrvvsqEEIVRA---------AKEANihAFIESLPNKYSTK--VGDkgtqLSGGQKQRIAIARALV 1261
Cdd:PRK10762    92 PqLTIAENIFLG--------REFVNRfgridwkkmYAEAD--KLLARLNLRFSSDklVGE----LSIGEQQMVEIAKVLS 157
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1149123047 1262 RQPHILLLDEATSAL-DTESE---KVVQEALDkarEGRTCIVIAHRLSTI-QNADLIVVFQNG 1319
Cdd:PRK10762   158 FESKVIIMDEPTDALtDTETEslfRVIRELKS---QGRGIVYISHRLKEIfEICDDVTVFRDG 217
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
473-656 5.28e-15

heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]


Pssm-ID: 273491 [Multi-domain]  Cd Length: 198  Bit Score: 75.09  E-value: 5.28e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  473 SRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIGVVSQEPVLFAT 552
Cdd:TIGR01189    9 SRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPEL 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  553 TIAENIRYGRE--NVTMDEIEKAVKEANaydfimkLPHKFDTLVgergAQLSGGQKQRIAIARALVRNPKILLLDEATSA 630
Cdd:TIGR01189   89 SALENLHFWAAihGGAQRTIEDALAAVG-------LTGFEDLPA----AQLSAGQQRRLALARLWLSRRPLWILDEPTTA 157
                          170       180
                   ....*....|....*....|....*.
gi 1149123047  631 LDTESEAVVQVALDkARKGRTTIVIA 656
Cdd:TIGR01189  158 LDKAGVALLAGLLR-AHLARGGIVLL 182
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
472-708 5.62e-15

ABC-type uncharacterized transport system, ATPase component [General function prediction only];


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 77.82  E-value: 5.62e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  472 PSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIiGVV----SQ-- 545
Cdd:COG4586     30 REYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFARRI-GVVfgqrSQlw 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  546 --EPVLfattiaENIRYGRE--NVTMDEIEKAVKEanaYDFIMKLPHKFDTLVgeRgaQLSGGQKQRIAIARALVRNPKI 621
Cdd:COG4586    109 wdLPAI------DSFRLLKAiyRIPDAEYKKRLDE---LVELLDLGELLDTPV--R--QLSLGQRMRCELAAALLHRPKI 175
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  622 LLLDEATSALDTESEAVVQVALDK--ARKGRTTIVIAHRLSTV----RNADVIagfDDGVIVEKGNHDELmKEKGIYFKL 695
Cdd:COG4586    176 LFLDEPTIGLDVVSKEAIREFLKEynRERGTTILLTSHDMDDIealcDRVIVI---DHGRIIYDGSLEEL-KERFGPYKT 251
                          250
                   ....*....|...
gi 1149123047  696 VTMQTAGNEVELE 708
Cdd:COG4586    252 IVLELAEPVPPLE 264
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
466-685 5.74e-15

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 79.90  E-value: 5.74e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  466 NVHFSYpSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTIN--VRFLREI---- 539
Cdd:PRK10261    19 NIAFMQ-EQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSrqVIELSEQsaaq 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  540 --------IGVVSQEPV-----LFAT--TIAENIRYgRENVTMDEiekAVKEANAYDFIMKLPHKfDTLVGERGAQLSGG 604
Cdd:PRK10261    98 mrhvrgadMAMIFQEPMtslnpVFTVgeQIAESIRL-HQGASREE---AMVEAKRMLDQVRIPEA-QTILSRYPHQLSGG 172
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  605 QKQRIAIARALVRNPKILLLDEATSALDTESEA----VVQVALDKARKGrtTIVIAHRLSTVRN-ADVIAGFDDGVIVEK 679
Cdd:PRK10261   173 MRQRVMIAMALSCRPAVLIADEPTTALDVTIQAqilqLIKVLQKEMSMG--VIFITHDMGVVAEiADRVLVMYQGEAVET 250

                   ....*.
gi 1149123047  680 GNHDEL 685
Cdd:PRK10261   251 GSVEQI 256
ycf16 CHL00131
sulfate ABC transporter protein; Validated
1119-1326 5.82e-15

sulfate ABC transporter protein; Validated


Pssm-ID: 214372 [Multi-domain]  Cd Length: 252  Bit Score: 76.22  E-value: 5.82e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1119 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERF--YDPLAGKVLLDGKEIKRLNVQwLRAHLGI----------- 1185
Cdd:CHL00131    19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEPE-ERAHLGIflafqypieip 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1186 -VSQEPILfdcsiaeNIAYgdNSRVVSQEEivraaKEANIHAFIESLPNKySTKVGDKGTQL--------SGGQKQRIAI 1256
Cdd:CHL00131    98 gVSNADFL-------RLAY--NSKRKFQGL-----PELDPLEFLEIINEK-LKLVGMDPSFLsrnvnegfSGGEKKRNEI 162
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1149123047 1257 ARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIV-IAH--RLSTIQNADLIVVFQNGRVKEHGT 1326
Cdd:CHL00131   163 LQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIIlITHyqRLLDYIKPDYVHVMQNGKIIKTGD 235
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
479-685 6.13e-15

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 76.67  E-value: 6.13e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  479 ILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGM-----VSVDGQDIRTI-NVRFLREIIGVVSQEPVLFAT 552
Cdd:PRK14271    36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYrysgdVLLGGRSIFNYrDVLEFRRRVGMLFQRPNPFPM 115
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  553 TIAENIRYG-RENVTMDEIE-KAVKEANAYDfiMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSA 630
Cdd:PRK14271   116 SIMDNVLAGvRAHKLVPRKEfRGVAQARLTE--VGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSA 193
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1149123047  631 LDTESEAVVQVALDKARKGRTTIVIAHRLS-TVRNADVIAGFDDGVIVEKGNHDEL 685
Cdd:PRK14271   194 LDPTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQL 249
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
1105-1321 6.21e-15

ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 79.30  E-value: 6.21e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1105 VTFGEVVF-----NYPTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL--ERfyDPLAGKVLLDGKEIKRLNVQ 1177
Cdd:COG3845    251 AEPGEVVLevenlSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALagLR--PPASGSIRLDGEDITGLSPR 328
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1178 WLRAH-LGIVSQEP-----ILfDCSIAENIAYGDnsrvVSQEEIVRAA--KEANIHAFIESLPNKYSTKVGDKGT---QL 1246
Cdd:COG3845    329 ERRRLgVAYIPEDRlgrglVP-DMSVAENLILGR----YRRPPFSRGGflDRKAIRAFAEELIEEFDVRTPGPDTparSL 403
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1149123047 1247 SGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAR-EGRTCIVIAHRLSTIQN-ADLIVVFQNGRV 1321
Cdd:COG3845    404 SGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRdAGAAVLLISEDLDEILAlSDRIAVMYEGRI 480
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
1111-1325 7.06e-15

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 79.51  E-value: 7.06e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1111 VFNYPTRpDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLN---VQWLRAHLGIVS 1187
Cdd:PRK10261   329 LLNRVTR-EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIF 407
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1188 QEPI-------LFDCSIAE-----NIAYGD--NSRVVSQEEIVRAAKEaniHAFieSLPNKYstkvgdkgtqlSGGQKQR 1253
Cdd:PRK10261   408 QDPYasldprqTVGDSIMEplrvhGLLPGKaaAARVAWLLERVGLLPE---HAW--RYPHEF-----------SGGQRQR 471
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1149123047 1254 IAIARALVRQPHILLLDEATSALDTE-SEKVVQEALDKARE-GRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHG 1325
Cdd:PRK10261   472 ICIARALALNPKVIIADEAVSALDVSiRGQIINLLLDLQRDfGIAYLFISHDMAVVERiSHRVAVMYLGQIVEIG 546
ABC_6TM_PCAT1_LagD_like cd18570
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ...
216-413 1.36e-14

Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.


Pssm-ID: 350014 [Multi-domain]  Cd Length: 294  Bit Score: 75.95  E-value: 1.36e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  216 KIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDdVSKINEGIGDKIGMFFQSMATFFTGFIVGFTRGWKLTLVILAISPVL 295
Cdd:cd18570     76 RLILGYFKHLLKLPLSFFETRKTGEIISRFND-ANKIREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPLY 154
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  296 GLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKRIGIKKAITANISIGAAFLL 375
Cdd:cd18570    155 ILIILLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLI 234
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1149123047  376 IYASYALAFWYGTTLVLSGEYSIGQVLTvfFSVLIGAF 413
Cdd:cd18570    235 SLIGSLLILWIGSYLVIKGQLSLGQLIA--FNALLGYF 270
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
475-632 1.67e-14

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 74.54  E-value: 1.67e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  475 KEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRF-LREIIGVVSQEPVLFAT- 552
Cdd:PRK10895    14 KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHArARRGIGYLPQEASIFRRl 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  553 TIAENIrygrenVTMDEIEKAVKEANAYDFIMKLPHKFDT--LVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSA 630
Cdd:PRK10895    94 SVYDNL------MAVLQIRDDLSAEQREDRANELMEEFHIehLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAG 167

                   ..
gi 1149123047  631 LD 632
Cdd:PRK10895   168 VD 169
ABCG_PDR_domain2 cd03232
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...
462-680 2.38e-14

Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213199 [Multi-domain]  Cd Length: 192  Bit Score: 73.05  E-value: 2.38e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSRKEVK-ILKGLNLKVQSGQTVALVGNSGCGKSTTVQ-LMQRLYDPT-EGMVSVDGqdiRTINVRFLRe 538
Cdd:cd03232      4 LTWKNLNYTVPVKGGKRqLLNNISGYVKPGTLTALMGESGAGKTTLLDvLAGRKTAGViTGEILING---RPLDKNFQR- 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  539 IIGVVSQEPVLFAT-TIAENIRygrenvtmdeiekavkeanaydFIMKLphkfdtlvgeRGaqLSGGQKQRIAIARALVR 617
Cdd:cd03232     80 STGYVEQQDVHSPNlTVREALR----------------------FSALL----------RG--LSVEQRKRLTIGVELAA 125
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1149123047  618 NPKILLLDEATSALDTESEAVVQVALDK-ARKGRTTIVIAHRLStvrnADVIAGFDDGVIVEKG 680
Cdd:cd03232    126 KPSILFLDEPTSGLDSQAAYNIVRFLKKlADSGQAILCTIHQPS----ASIFEKFDRLLLLKRG 185
ABC_6TM_Tm287_like cd18548
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ...
157-413 2.50e-14

Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349992 [Multi-domain]  Cd Length: 292  Bit Score: 75.13  E-value: 2.50e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  157 DLMSNIT-------NRSDINDTGFFMnleedmtryayyySGIGAGVLVAAYIQVSFWCLAAGRQIHKIRKQFFHAIMRqe 229
Cdd:cd18548     20 TLMADIIdegiangDLSYILRTGLLM-------------LLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFEKIQS-- 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  230 igwFDVHDVGE-----LNTRLTDDVSKINEGIGDKIGMFFQSMATFFTGFIVGFTRGWKLTLVILAISPVLGLSAAVWAK 304
Cdd:cd18548     85 ---FSFAEIDKfgtssLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPILALVVFLIMK 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  305 ILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKRIGIKKAITANISIGAAFLLIYASYALAF 384
Cdd:cd18548    162 KAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPLMMLIMNLAIVAIL 241
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1149123047  385 WYGTTLVLSGEYSIGQV-------LTVFFSVLIGAF 413
Cdd:cd18548    242 WFGGHLINAGSLQVGDLvafinylMQILMSLMMLSM 277
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
1112-1332 2.60e-14

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 74.83  E-value: 2.60e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1112 FNYPT----RPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVS 1187
Cdd:PRK15112    14 FRYRTgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIF 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1188 QEPI-----------LFDCSIAENIAYGDNSRvvsQEEIVRAAKEANI---HAfieslpNKYSTkvgdkgtQLSGGQKQR 1253
Cdd:PRK15112    94 QDPStslnprqrisqILDFPLRLNTDLEPEQR---EKQIIETLRQVGLlpdHA------SYYPH-------MLAPGQKQR 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1254 IAIARALVRQPHILLLDEATSALD-TESEKVVQEALD-KAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQL 1330
Cdd:PRK15112   158 LGLARALILRPKVIIADEALASLDmSMRSQLINLMLElQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADV 237

                   ..
gi 1149123047 1331 LA 1332
Cdd:PRK15112   238 LA 239
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
1118-1325 3.68e-14

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 73.97  E-value: 3.68e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1118 PDIPVLQGLSLEVKKGQTLALVGSSGCGKS----TVVQLLERFYDPLAGKVLLDGKEIKrlnVQWLRA-HLGIVSQEP-- 1190
Cdd:PRK10418    14 AAQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVA---PCALRGrKIATIMQNPrs 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1191 ------ILFDCSIAENIAYGDNSRVVSQEEIVRAAKEANIHAFIESLPnkystkvgdkgTQLSGGQKQRIAIARALVRQP 1264
Cdd:PRK10418    91 afnplhTMHTHARETCLALGKPADDATLTAALEAVGLENAARVLKLYP-----------FEMSGGMLQRMMIALALLCEA 159
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1149123047 1265 HILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHG 1325
Cdd:PRK10418   160 PFIIADEPTTDLDVVAQARILDLLESivQKRALGMLLVTHDMGVVARlADDVAVMSHGRIVEQG 223
ABC_6TM_exporter_like cd18550
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
214-411 5.84e-14

Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349994 [Multi-domain]  Cd Length: 294  Bit Score: 74.06  E-value: 5.84e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  214 IHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQSMATFFTGFIVGFTRGWKLTLVILAISP 293
Cdd:cd18550     71 MYDLRVQLYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLP 150
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  294 VLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAA--IRTVIAFGGQKKELERYNKNLEEAKRIGIKKAITANISIGA 371
Cdd:cd18550    151 LFVLPTRRVGRRRRKLTREQQEKLAELNSIMQETLSVsgALLVKLFGREDDEAARFARRSRELRDLGVRQALAGRWFFAA 230
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1149123047  372 AFLLIYASYALAFWYGTTLVLSGEYSIGQVltVFFSVLIG 411
Cdd:cd18550    231 LGLFTAIGPALVYWVGGLLVIGGGLTIGTL--VAFTALLG 268
ABC_6TM_YknV_like cd18545
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ...
181-405 6.93e-14

Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349989 [Multi-domain]  Cd Length: 293  Bit Score: 74.04  E-value: 6.93e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  181 MTRYAYYYSGIGAGVLVAAYIQVSFWCLAAGRQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKI 260
Cdd:cd18545     39 LLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGL 118
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  261 GMFFQSMATFFTGFIVGFTRGWKLTLVILAISPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQ 340
Cdd:cd18545    119 INLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVVFLLRRRARKAWQRVRKKISNLNAYLHESISGIRVIQSFARE 198
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1149123047  341 KKELERYNKNLEEAKRIGIkKAITANISIGAAFLLIYA-SYALAFWYGTTLVLSGEYSIGqVLTVF 405
Cdd:cd18545    199 DENEEIFDELNRENRKANM-RAVRLNALFWPLVELISAlGTALVYWYGGKLVLGGAITVG-VLVAF 262
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
1123-1331 7.07e-14

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 73.04  E-value: 7.07e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1123 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWL----RAHL-----GIVSQEP--- 1190
Cdd:PRK11701    22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseaeRRRLlrtewGFVHQHPrdg 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1191 ILFDCSIAENIA----------YGD----NSRVVSQEEIVRAAkeanihafIESLPnkystkvgdkgTQLSGGQKQRIAI 1256
Cdd:PRK11701   102 LRMQVSAGGNIGerlmavgarhYGDiratAGDWLERVEIDAAR--------IDDLP-----------TTFSGGMQQRLQI 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1257 ARALVRQPHILLLDEATSALDTEsekvVQ-EALDKARE-----GRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQ 1329
Cdd:PRK11701   163 ARNLVTHPRLVFMDEPTGGLDVS----VQaRLLDLLRGlvrelGLAVVIVTHDLAVARLlAHRLLVMKQGRVVESGLTDQ 238

                   ..
gi 1149123047 1330 LL 1331
Cdd:PRK11701   239 VL 240
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
483-688 7.75e-14

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 72.66  E-value: 7.75e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  483 LNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYdPTEGMVSVDGQDIRTINVRFLREIIGVVSQE-PVLFATTIAENI-RY 560
Cdd:PRK03695    15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRAYLSQQqTPPFAMPVFQYLtLH 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  561 GRENVTMDEIEKAVKE-ANAYDFIMKLPhkfdTLVGergaQLSGGQKQRIAIARALVR-----NP--KILLLDEATSALD 632
Cdd:PRK03695    94 QPDKTRTEAVASALNEvAEALGLDDKLG----RSVN----QLSGGEWQRVRLAAVVLQvwpdiNPagQLLLLDEPMNSLD 165
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1149123047  633 TESeavvQVALDK-----ARKGRTTIVIAHRLS-TVRNADVIAGFDDGVIVEKGNHDELMKE 688
Cdd:PRK03695   166 VAQ----QAALDRllselCQQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVLTP 223
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
1117-1302 7.93e-14

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 71.76  E-value: 7.93e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1117 RPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRL------NVQWLRAHLGIVS--- 1187
Cdd:PRK13538    11 RDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQrdeyhqDLLYLGHQPGIKTelt 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1188 -QEPILFDCSIAeniaygdnsRVVSQEEIVRAAKEANIHAFiESLPNKystkvgdkgtQLSGGQKQRIAIARALVRQPHI 1266
Cdd:PRK13538    91 aLENLRFYQRLH---------GPGDDEALWEALAQVGLAGF-EDVPVR----------QLSAGQQRRVALARLWLTRAPL 150
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1149123047 1267 LLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAH 1302
Cdd:PRK13538   151 WILDEPFTAIDKQGVARLEALLAQhAEQGGMVILTTH 187
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
1123-1319 8.38e-14

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 75.59  E-value: 8.38e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1123 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQwLRAHLG--IVSQEPILFD-CSIAE 1199
Cdd:PRK09700    21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHK-LAAQLGigIIYQELSVIDeLTVLE 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1200 NIAYGDN-SRVVSQEEIVRAAK---EANIHAFIESLPNKYSTKVGDkgtqLSGGQKQRIAIARALVRQPHILLLDEATSA 1275
Cdd:PRK09700   100 NLYIGRHlTKKVCGVNIIDWREmrvRAAMMLLRVGLKVDLDEKVAN----LSISHKQMLEIAKTLMLDAKVIIMDEPTSS 175
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1149123047 1276 L-DTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVFQNG 1319
Cdd:PRK09700   176 LtNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRiCDRYTVMKDG 221
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
473-689 9.25e-14

ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 71.91  E-value: 9.25e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  473 SRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLY--DPTEGMVSVDGQDIrtinvrflreiigvvSQEpvlf 550
Cdd:COG2401     39 RVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQF---------------GRE---- 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  551 aTTIAENIryGRENVTMDEIE--KAVKEANAYDFIMKLPHkfdtlvgergaqLSGGQKQRIAIARALVRNPKILLLDEAT 628
Cdd:COG2401    100 -ASLIDAI--GRKGDFKDAVEllNAVGLSDAVLWLRRFKE------------LSTGQKFRFRLALLLAERPKLLVIDEFC 164
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1149123047  629 SALDTESEAVVQVALDK-ARKGRTTIVIA-HRlstvrnADVIAGFDDGVIVEKGnHDELMKEK 689
Cdd:COG2401    165 SHLDRQTAKRVARNLQKlARRAGITLVVAtHH------YDVIDDLQPDLLIFVG-YGGVPEEK 220
ABC_6TM_ABCB8_like cd18574
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ...
837-995 1.08e-13

Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.


Pssm-ID: 350018 [Multi-domain]  Cd Length: 295  Bit Score: 73.35  E-value: 1.08e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  837 FITFFLQG-FTF------GKAGEILTKRLRYMVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIGSrlaVITQN 909
Cdd:cd18574     49 LGLYLLQSlLTFayisllSVVGERVAARLRNDLFSSLLRQDIAFFD--THRTGELVNRLTADVQEFKSSFKQ---CVSQG 123
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  910 IANLG--TGIIISFIY-GWQLTLLLLAIVPIIAIAGVV---EMKMLSGQAlkdKKELEGSGKIATEAIENFRTVVSLTQE 983
Cdd:cd18574    124 LRSVTqtVGCVVSLYLiSPKLTLLLLVIVPVVVLVGTLygsFLRKLSRRA---QAQVAKATGVADEALGNIRTVRAFAME 200
                          170
                   ....*....|..
gi 1149123047  984 QKFEHMYAQSLQ 995
Cdd:cd18574    201 DRELELYEEEVE 212
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
489-681 1.08e-13

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 69.71  E-value: 1.08e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047   489 SGQTVALVGNSGCGKSTTVQ-LMQRLYDPTEGMVSVDGQDIRTINVRFLREIIgvvsqepvlfattiaenirygrenvtm 567
Cdd:smart00382    1 PGEVILIVGPPGSGKTTLARaLARELGPPGGGVIYIDGEDILEEVLDQLLLII--------------------------- 53
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047   568 deiekavkeanaydfimklphkfdtlVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALD--- 644
Cdd:smart00382   54 --------------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrl 107
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|.
gi 1149123047   645 ----KARKGRTTIVIAHRLSTVRNADVIAGFDDGVIVEKGN 681
Cdd:smart00382  108 llllKSEKNLTVILTTNDEKDLGPALLRRRFDRRIVLLLIL 148
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
483-632 1.20e-13

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 74.14  E-value: 1.20e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  483 LNLKVQ-----SGQTvALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQ---DI-RTINVRFLREIIGVVSQEPVLFA-T 552
Cdd:PRK11144    13 LCLTVNltlpaQGIT-AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAeKGICLPPEKRRIGYVFQDARLFPhY 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  553 TIAENIRYGrenvtMDEIEKAvkeanaydfimklphKFDTLVGERG---------AQLSGGQKQRIAIARALVRNPKILL 623
Cdd:PRK11144    92 KVRGNLRYG-----MAKSMVA---------------QFDKIVALLGieplldrypGSLSGGEKQRVAIGRALLTAPELLL 151

                   ....*....
gi 1149123047  624 LDEATSALD 632
Cdd:PRK11144   152 MDEPLASLD 160
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
480-674 1.47e-13

Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.


Pssm-ID: 213182 [Multi-domain]  Cd Length: 182  Bit Score: 70.54  E-value: 1.47e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  480 LKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREI-IGVVSQEPV---LFAT-TI 554
Cdd:cd03215     16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVPEDRKregLVLDlSV 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  555 AENIrygrenvtmdeiekavkeanaydfimklphkfdTLvgerGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTE 634
Cdd:cd03215     96 AENI---------------------------------AL----SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVG 138
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1149123047  635 S-EAVVQVALDKARKGRTTIVIAHRLSTV-RNADVIAGFDDG 674
Cdd:cd03215    139 AkAEIYRLIRELADAGKAVLLISSELDELlGLCDRILVMYEG 180
hmuV PRK13547
heme ABC transporter ATP-binding protein;
466-687 1.67e-13

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 72.55  E-value: 1.67e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  466 NVHFSYPSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQ-LMQRLYDPTE-------GMVSVDGQDIRTINVRFLR 537
Cdd:PRK13547     3 TADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKaLAGDLTGGGAprgarvtGDVTLNGEPLAAIDAPRLA 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  538 EIIGVVSQ--EPVlFATTIAENIRYGR----------ENVTMDEIEKAVKEANAydfimklphkfDTLVGERGAQLSGGQ 605
Cdd:PRK13547    83 RLRAVLPQaaQPA-FAFSAREIVLLGRypharragalTHRDGEIAWQALALAGA-----------TALVGRDVTTLSGGE 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  606 KQRIAIARAL---------VRNPKILLLDEATSALDTES-----EAVVQVALDkARKGRTTIVIAHRLSTvRNADVIAGF 671
Cdd:PRK13547   151 LARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHqhrllDTVRRLARD-WNLGVLAIVHDPNLAA-RHADRIAML 228
                          250
                   ....*....|....*.
gi 1149123047  672 DDGVIVEKGNHDELMK 687
Cdd:PRK13547   229 ADGAIVAHGAPADVLT 244
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
452-685 1.71e-13

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 72.11  E-value: 1.71e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  452 GHKPDNIkgnLEFRNVHFSypsRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTI 531
Cdd:PRK11831     1 EQSVANL---VDMRGVSFT---RGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAM 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  532 NVRFL---REIIGVVSQEPVLFA-TTIAENIRYG-RENVTMDE--IEKAVkeanaydfIMKLphkfdTLVGERGA----- 599
Cdd:PRK11831    75 SRSRLytvRKRMSMLFQSGALFTdMNVFDNVAYPlREHTQLPAplLHSTV--------MMKL-----EAVGLRGAaklmp 141
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  600 -QLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARK--GRTTIVIAHR----LSTVRNADVIAgfd 672
Cdd:PRK11831   142 sELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSalGVTCVVVSHDvpevLSIADHAYIVA--- 218
                          250
                   ....*....|...
gi 1149123047  673 DGVIVEKGNHDEL 685
Cdd:PRK11831   219 DKKIVAHGSAQAL 231
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
465-643 3.71e-13

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 70.91  E-value: 3.71e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  465 RNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQdirtinvrfLReiIGVVS 544
Cdd:PRK09544     8 ENVSVSFGQRR---VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK---------LR--IGYVP 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  545 QEPVLFAT---TIAENIRYgRENVTMDEIEKAVKEANAYDFIMKLPHKfdtlvgergaqLSGGQKQRIAIARALVRNPKI 621
Cdd:PRK09544    74 QKLYLDTTlplTVNRFLRL-RPGTKKEDILPALKRVQAGHLIDAPMQK-----------LSGGETQRVLLARALLNRPQL 141
                          170       180
                   ....*....|....*....|..
gi 1149123047  622 LLLDEATSALDTESeavvQVAL 643
Cdd:PRK09544   142 LVLDEPTQGVDVNG----QVAL 159
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
1096-1331 3.74e-13

Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 71.36  E-value: 3.74e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1096 LMPNTLEGNVTFG--EVVFNYPTRPdipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKR 1173
Cdd:PRK10575     1 MQEYTNHSDTTFAlrNVSFRVPGRT---LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLES 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1174 LNVQWLRAHLGIVSQE-PILFDCSIAENIA------------YGDNSRVVSQEEIVRAAKEANIHAFIESlpnkystkvg 1240
Cdd:PRK10575    78 WSSKAFARKVAYLPQQlPAAEGMTVRELVAigrypwhgalgrFGAADREKVEEAISLVGLKPLAHRLVDS---------- 147
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1241 dkgtqLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAhRLSTIQNA----DLIVVF 1316
Cdd:PRK10575   148 -----LSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIA-VLHDINMAarycDYLVAL 221
                          250
                   ....*....|....*
gi 1149123047 1317 QNGRVKEHGTHQQLL 1331
Cdd:PRK10575   222 RGGEMIAQGTPAELM 236
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
1121-1321 4.75e-13

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 73.23  E-value: 4.75e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1121 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLN-----------VQWLRAHLGIVSQE 1189
Cdd:PRK10982   262 PSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNaneainhgfalVTEERRSTGIYAYL 341
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1190 PILFDCSIAENIAYGDNSRVVSQEEIvraakEANIHAFIESLPNK---YSTKVGdkgtQLSGGQKQRIAIARALVRQPHI 1266
Cdd:PRK10982   342 DIGFNSLISNIRNYKNKVGLLDNSRM-----KSDTQWVIDSMRVKtpgHRTQIG----SLSGGNQQKVIIGRWLLTQPEI 412
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1149123047 1267 LLLDEATSALDTESE-KVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRV 1321
Cdd:PRK10982   413 LMLDEPTRGIDVGAKfEIYQLIAELAKKDKGIIIISSEMPELLGiTDRILVMSNGLV 469
ABCG_PDR_domain2 cd03232
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...
1123-1319 5.20e-13

Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213199 [Multi-domain]  Cd Length: 192  Bit Score: 69.19  E-value: 5.20e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1123 LQGLSLEVKKGQTLALVGSSGCGKSTvvqLLerfyDPLA---------GKVLLDGKEIKrlnvQWLRAHLGIVSQEPILF 1193
Cdd:cd03232     23 LNNISGYVKPGTLTALMGESGAGKTT---LL----DVLAgrktagvitGEILINGRPLD----KNFQRSTGYVEQQDVHS 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1194 DCSIaeniaygdnsrvvsqeeiVRaakeanihafiESLpnKYSTKVGDkgtqLSGGQKQRIAIARALVRQPHILLLDEAT 1273
Cdd:cd03232     92 PNLT------------------VR-----------EAL--RFSALLRG----LSVEQRKRLTIGVELAAKPSILFLDEPT 136
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1149123047 1274 SALDTESEKVVQEALDK-AREGRTCIVIAHRLS--TIQNADLIVVFQNG 1319
Cdd:cd03232    137 SGLDSQAAYNIVRFLKKlADSGQAILCTIHQPSasIFEKFDRLLLLKRG 185
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
1115-1321 6.82e-13

ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.


Pssm-ID: 213234 [Multi-domain]  Cd Length: 236  Bit Score: 69.67  E-value: 6.82e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1115 PTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGkeikrlNVQW-----LRAHLGIV--S 1187
Cdd:cd03267     29 RKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG------LVPWkrrkkFLRRIGVVfgQ 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1188 QEPILFDCSIAENIAYgdnSRVVSQEEIVRAAKeaNIHAFIESLPnkySTKVGDKGT-QLSGGQKQRIAIARALVRQPHI 1266
Cdd:cd03267    103 KTQLWWDLPVIDSFYL---LAAIYDLPPARFKK--RLDELSELLD---LEELLDTPVrQLSLGQRMRAEIAAALLHEPEI 174
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1149123047 1267 LLLDEATSALDTESEKVVQEALDKAREGR--TCIVIAHRLSTIQN-ADLIVVFQNGRV 1321
Cdd:cd03267    175 LFLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEAlARRVLVIDKGRL 232
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
479-685 7.28e-13

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 70.11  E-value: 7.28e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  479 ILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDP----TEGMVSVDGQDIRTINVRflREIIGVVSQEP------- 547
Cdd:PRK10418    18 LVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPCALR--GRKIATIMQNPrsafnpl 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  548 VLFATTIAENIR-YGRE--NVTMDEIEKAVKEANAyDFIMKLpHKFdtlvgergaQLSGGQKQRIAIARALVRNPKILLL 624
Cdd:PRK10418    96 HTMHTHARETCLaLGKPadDATLTAALEAVGLENA-ARVLKL-YPF---------EMSGGMLQRMMIALALLCEAPFIIA 164
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1149123047  625 DEATSALDTESEAVVQVALDK--ARKGRTTIVIAHRLSTV-RNADVIAGFDDGVIVEKGNHDEL 685
Cdd:PRK10418   165 DEPTTDLDVVAQARILDLLESivQKRALGMLLVTHDMGVVaRLADDVAVMSHGRIVEQGDVETL 228
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
1106-1332 8.34e-13

D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 131681 [Multi-domain]  Cd Length: 500  Bit Score: 72.55  E-value: 8.34e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1106 TFGEVVFN-------YPTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD-PLAGKVLLDGKEIK-RLNV 1176
Cdd:TIGR02633  252 EIGDVILEarnltcwDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGKPVDiRNPA 331
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1177 QWLRAHLGIVSQEP----ILFDCSIAENIAYGDNSRVVSQEEIVRAAKEANIHAFIESLPNKYSTKVGDKGtQLSGGQKQ 1252
Cdd:TIGR02633  332 QAIRAGIAMVPEDRkrhgIVPILGVGKNITLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLPIG-RLSGGNQQ 410
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1253 RIAIARALVRQPHILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVK----EHG- 1325
Cdd:TIGR02633  411 KAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQlAQEGVAIIVVSSELAEVLGlSDRVLVIGEGKLKgdfvNHAl 490

                   ....*..
gi 1149123047 1326 THQQLLA 1332
Cdd:TIGR02633  491 TQEQVLA 497
PRK10522 PRK10522
multidrug transporter membrane component/ATP-binding component; Provisional
462-678 1.01e-12

multidrug transporter membrane component/ATP-binding component; Provisional


Pssm-ID: 236707 [Multi-domain]  Cd Length: 547  Bit Score: 72.31  E-value: 1.01e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSRKEVkiLKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIG 541
Cdd:PRK10522   323 LELRNVTFAYQDNGFS--VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFS 400
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  542 VVSQEPVLFATTIaeniryGRENvtmdeieKAVKEANAYDFI--MKLPHKFdTLVGERGA--QLSGGQKQRIAIARALVR 617
Cdd:PRK10522   401 AVFTDFHLFDQLL------GPEG-------KPANPALVEKWLerLKMAHKL-ELEDGRISnlKLSKGQKKRLALLLALAE 466
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1149123047  618 NPKILLLDEATSALDTESEAVV-QVALDKAR-KGRTTIVIAHRLSTVRNADVIAGFDDGVIVE 678
Cdd:PRK10522   467 ERDILLLDEWAADQDPHFRREFyQVLLPLLQeMGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
462-657 1.01e-12

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 68.68  E-value: 1.01e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSypsRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREII- 540
Cdd:PRK13538     2 LEARNLACE---RDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLy 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  541 -----GVvsqEPVLfatTIAENIRY---GRENVTMDEIEKAVKEANAYDFiMKLPhkfdtlvgerGAQLSGGQKQRIAIA 612
Cdd:PRK13538    79 lghqpGI---KTEL---TALENLRFyqrLHGPGDDEALWEALAQVGLAGF-EDVP----------VRQLSAGQQRRVALA 141
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1149123047  613 RALVRNPKILLLDEATSALDTESEAVVQVALDK-ARKGRTTIVIAH 657
Cdd:PRK13538   142 RLWLTRAPLWILDEPFTAIDKQGVARLEALLAQhAEQGGMVILTTH 187
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
462-677 1.03e-12

ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 72.37  E-value: 1.03e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVhfSYPSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREI-I 540
Cdd:COG3845    258 LEVENL--SVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgV 335
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  541 GVVSQEPVLFAT----TIAENI---RYGRENVT------MDEIEKAVKEanaydfIMKlphKFD-------TLVGergaQ 600
Cdd:COG3845    336 AYIPEDRLGRGLvpdmSVAENLilgRYRRPPFSrggfldRKAIRAFAEE------LIE---EFDvrtpgpdTPAR----S 402
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1149123047  601 LSGGQKQRIAIARALVRNPKILLLDEATSALDTES-EAVVQVALDKARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIV 677
Cdd:COG3845    403 LSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAiEFIHQRLLELRDAGAAVLLISEDLDEILAlSDRIAVMYEGRIV 481
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
1126-1325 1.23e-12

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 71.06  E-value: 1.23e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1126 LSLEVK-----KGQTlALVGSSGCGKSTVVQLLERFYDP------LAGKVLLDGKeiKRLNVQWLRAHLGIVSQEPILF- 1193
Cdd:PRK11144    13 LCLTVNltlpaQGIT-AIFGRSGAGKTSLINAISGLTRPqkgrivLNGRVLFDAE--KGICLPPEKRRIGYVFQDARLFp 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1194 DCSIAENIAYGDNSRVVSQ-EEIVRAAKeanihafIESLPNKY-STkvgdkgtqLSGGQKQRIAIARALVRQPHILLLDE 1271
Cdd:PRK11144    90 HYKVRGNLRYGMAKSMVAQfDKIVALLG-------IEPLLDRYpGS--------LSGGEKQRVAIGRALLTAPELLLMDE 154
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1149123047 1272 ATSALDTESEKVVQEALDK-AREGRTCIV-IAHRLSTI-QNADLIVVFQNGRVKEHG 1325
Cdd:PRK11144   155 PLASLDLPRKRELLPYLERlAREINIPILyVSHSLDEIlRLADRVVVLEQGKVKAFG 211
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
1122-1336 1.32e-12

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 69.15  E-value: 1.32e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1122 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQwLRAHLGI--VSQEPILFD-CSIA 1198
Cdd:PRK10895    18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLH-ARARRGIgyLPQEASIFRrLSVY 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1199 ENI-AYGDNSRVVSQEEIVRAAKEANIHAFIESLPNKYstkvgdkGTQLSGGQKQRIAIARALVRQPHILLLDEATSALD 1277
Cdd:PRK10895    97 DNLmAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSM-------GQSLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1149123047 1278 TESEKVVQEALDKARE-GRTCIVIAHRL-STIQNADLIVVFQNGRVKEHGTHQQLLAQKGI 1336
Cdd:PRK10895   170 PISVIDIKRIIEHLRDsGLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQDEHV 230
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
464-656 1.32e-12

First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213200 [Multi-domain]  Cd Length: 202  Bit Score: 68.06  E-value: 1.32e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  464 FRNVHF-SYPSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTtvqLMQRL------YDPTEGMVSVDGQDIRTINVRFL 536
Cdd:cd03233      6 WRNISFtTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCST---LLKALanrtegNVSVEGDIHYNGIPYKEFAEKYP 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  537 REIIgVVSQEPVLFAT-TIAEnirygrenvTMDeiekAVKEANAYDFImklphkfdtlvgeRGaqLSGGQKQRIAIARAL 615
Cdd:cd03233     83 GEII-YVSEEDVHFPTlTVRE---------TLD----FALRCKGNEFV-------------RG--ISGGERKRVSIAEAL 133
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1149123047  616 VRNPKILLLDEATSALDTESE-AVVQVALDKARKGRTTIVIA 656
Cdd:cd03233    134 VSRASVLCWDNSTRGLDSSTAlEILKCIRTMADVLKTTTFVS 175
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
1121-1303 1.92e-12

ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 68.06  E-value: 1.92e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1121 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFY--DPLAGKVLLDGKEIKRlnvqwlrahlgivsqepilfDCSIA 1198
Cdd:COG2401     44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQFGR--------------------EASLI 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1199 ENIA-YGDNSRVVsqeEIVRAAKEANIHAFIEslpnKYStkvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEATSALD 1277
Cdd:COG2401    104 DAIGrKGDFKDAV---ELLNAVGLSDAVLWLR----RFK--------ELSTGQKFRFRLALLLAERPKLLVIDEFCSHLD 168
                          170       180
                   ....*....|....*....|....*...
gi 1149123047 1278 TESEKVVQEALDKA--REGRTCIVIAHR 1303
Cdd:COG2401    169 RQTAKRVARNLQKLarRAGITLVVATHH 196
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
478-689 3.28e-12

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 68.50  E-value: 3.28e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  478 KILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLY--DPTEG--------MVSVDGQDIRtiNVRFLREIIGVVSQEP 547
Cdd:PRK09984    18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgDKSAGshiellgrTVQREGRLAR--DIRKSRANTGYIFQQF 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  548 VLF-ATTIAENIRYGRENVT------MDEIEKAVKEaNAYDFIMK--LPHkfdtLVGERGAQLSGGQKQRIAIARALVRN 618
Cdd:PRK09984    96 NLVnRLSVLENVLIGALGSTpfwrtcFSWFTREQKQ-RALQALTRvgMVH----FAHQRVSTLSGGQQQRVAIARALMQQ 170
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1149123047  619 PKILLLDEATSALDTESEAVVQVALDKARK--GRTTIVIAHRLS-TVRNADVIAGFDDGVIVEKGNHDELMKEK 689
Cdd:PRK09984   171 AKVILADEPIASLDPESARIVMDTLRDINQndGITVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQFDNER 244
sufC PRK09580
cysteine desulfurase ATPase component; Reviewed
462-682 4.87e-12

cysteine desulfurase ATPase component; Reviewed


Pssm-ID: 181965 [Multi-domain]  Cd Length: 248  Bit Score: 67.51  E-value: 4.87e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYpsrKEVKILKGLNLKVQSGQTVALVGNSGCGKST-TVQLMQRL-YDPTEGMVSVDGQDIRTIN------- 532
Cdd:PRK09580     2 LSIKDLHVSV---EDKAILRGLNLEVRPGEVHAIMGPNGSGKSTlSATLAGREdYEVTGGTVEFKGKDLLELSpedrage 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  533 -----VRFLREIIGVVSQepvLFATTIAENIRYGRENVTMDEIEKAvkeanayDFI------MKLPHkfDTLVGERGAQL 601
Cdd:PRK09580    79 gifmaFQYPVEIPGVSNQ---FFLQTALNAVRSYRGQEPLDRFDFQ-------DLMeekialLKMPE--DLLTRSVNVGF 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  602 SGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARKG-RTTIVIAH--RLSTVRNADVIAGFDDGVIVE 678
Cdd:PRK09580   147 SGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGkRSFIIVTHyqRILDYIKPDYVHVLYQGRIVK 226

                   ....
gi 1149123047  679 KGNH 682
Cdd:PRK09580   227 SGDF 230
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
1108-1332 5.14e-12

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 69.96  E-value: 5.14e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1108 GEVVF---NY----PTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYdPLA--GKVLLDGKEIK-RLNVQ 1177
Cdd:PRK13549   256 GEVILevrNLtawdPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAY-PGRweGEIFIDGKPVKiRNPQQ 334
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1178 WLRAHLGIVSQEP----ILFDCSIAENIAYGDNSRVVSQEEIVRAAKEANIHAFIESLPNKYST---KVGdkgtQLSGGQ 1250
Cdd:PRK13549   335 AIAQGIAMVPEDRkrdgIVPVMGVGKNITLAALDRFTGGSRIDDAAELKTILESIQRLKVKTASpelAIA----RLSGGN 410
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1251 KQRIAIARALVRQPHILLLDEATSALDT----ESEKVVQEAldkAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVK--- 1322
Cdd:PRK13549   411 QQKAVLAKCLLLNPKILILDEPTRGIDVgakyEIYKLINQL---VQQGVAIIVISSELPEVLGlSDRVLVMHEGKLKgdl 487
                          250
                   ....*....|..
gi 1149123047 1323 --EHGTHQQLLA 1332
Cdd:PRK13549   488 inHNLTQEQVME 499
ABC_6TM_Tm287_like cd18548
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ...
827-1078 5.28e-12

Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349992 [Multi-domain]  Cd Length: 292  Bit Score: 68.19  E-value: 5.28e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  827 LLFLALGIISFITFFLQGFTFGKAGEILTKRLRYMVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAI--GSRLA 904
Cdd:cd18548     43 LLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFEKIQSFSFAEID--KFGTSSLITRLTNDVTQVQNFVmmLLRML 120
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  905 VITqnIANLGTGIIISFIYGWQLTLLLLAIVPIIAIAGVVEMKMLSGQALKDKKELEGSGKIATEAIENFRTVVSLTQE- 983
Cdd:cd18548    121 VRA--PIMLIGAIIMAFRINPKLALILLVAIPILALVVFLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREd 198
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  984 ---QKFEHMyAQSLqvpYRNSLRKAHIFGITFSFTQAMMYFSYAGCFRFGAYLVAHKLMSFEDV-------LLVFSAVVF 1053
Cdd:cd18548    199 yeeERFDKA-NDDL---TDTSLKAGRLMALLNPLMMLIMNLAIVAILWFGGHLINAGSLQVGDLvafinylMQILMSLMM 274
                          250       260
                   ....*....|....*....|....*
gi 1149123047 1054 GAMAVGQVSsfapdyaKAKISAAHI 1078
Cdd:cd18548    275 LSMVFVMLP-------RASASAKRI 292
ABC_6TM_exporter_like cd18565
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
197-415 6.22e-12

Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 350009 [Multi-domain]  Cd Length: 313  Bit Score: 68.36  E-value: 6.22e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  197 VAAYIQVSFWCLAAGRQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQSMATFFTGFIV 276
Cdd:cd18565     69 LFQYLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAI 148
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  277 GFTRGWKLTLVILAISPVLGLSAAVWAKILSSftdKELLAYAKAGAVA---EEVLAAIRTVIAFGGQKKELERynknLEE 353
Cdd:cd18565    149 LFYLNWQLALVALLPVPLIIAGTYWFQRRIEP---RYRAVREAVGDLNarlENNLSGIAVIKAFTAEDFERER----VAD 221
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1149123047  354 AKRIGIKKAITAnISIGAAF-----LLIYASYALAFWYGTTLVLSGEYSIGQVLTVffsvliGAFSV 415
Cdd:cd18565    222 ASEEYRDANWRA-IRLRAAFfpvirLVAGAGFVATFVVGGYWVLDGPPLFTGTLTV------GTLVT 281
ABC_6TM_Rv0194_D1_like cd18543
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ...
191-409 9.62e-12

Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349987 [Multi-domain]  Cd Length: 291  Bit Score: 67.51  E-value: 9.62e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  191 IGAGVLVAAYIQvsfWCLAAGRQI----------HKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGdKI 260
Cdd:cd18543     41 LVLLLLALGVAE---AVLSFLRRYlagrlslgveHDLRTDLFAHLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLA-FG 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  261 GMFFQSMATFFTGFIVGFTRGWKLTLVILAISPVLGLSAAVWAKILSSFTdkeLLAYAKAGAVA---EEVLAAIRTVIAF 337
Cdd:cd18543    117 PFLLGNLLTLVVGLVVMLVLSPPLALVALASLPPLVLVARRFRRRYFPAS---RRAQDQAGDLAtvvEESVTGIRVVKAF 193
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1149123047  338 GGQKKELERYNKNLEEAKRIGIKKA-ITANISigAAFLLI-YASYALAFWYGTTLVLSGEYSIGQvLTVFFSVL 409
Cdd:cd18543    194 GRERRELDRFEAAARRLRATRLRAArLRARFW--PLLEALpELGLAAVLALGGWLVANGSLTLGT-LVAFSAYL 264
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
461-688 1.04e-11

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 67.84  E-value: 1.04e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  461 NLEFRNVHFSyPSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYD-PTEGM---VSVDGQDIRTINVRFL 536
Cdd:PRK11022     5 NVDKLSVHFG-DESAPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyPGRVMaekLEFNGQDLQRISEKER 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  537 REIIG----VVSQEPVlfaTTIaeNIRYGRENVTMDEIE------KAVKEANAYDFImklphkfdTLVG-----ER---- 597
Cdd:PRK11022    84 RNLVGaevaMIFQDPM---TSL--NPCYTVGFQIMEAIKvhqggnKKTRRQRAIDLL--------NQVGipdpaSRldvy 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  598 GAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEA-VVQVALD-KARKGRTTIVIAHRLSTV-RNADVIAGFDDG 674
Cdd:PRK11022   151 PHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAqIIELLLElQQKENMALVLITHDLALVaEAAHKIIVMYAG 230
                          250
                   ....*....|....
gi 1149123047  675 VIVEKGNHDELMKE 688
Cdd:PRK11022   231 QVVETGKAHDIFRA 244
hmuV PRK13547
heme ABC transporter ATP-binding protein;
1122-1326 1.28e-11

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 66.77  E-value: 1.28e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1122 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLE-RFYDPLA-------GKVLLDGKEIKRLNVQWL---RAHLGIVSQEP 1190
Cdd:PRK13547    16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGGAprgarvtGDVTLNGEPLAAIDAPRLarlRAVLPQAAQPA 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1191 ILFdcSIAENIAYGDNSRVVSQEEIVRAAKEANIHAFIESlpnKYSTKVGDKGTQLSGGQKQRIAIARAL---------V 1261
Cdd:PRK13547    96 FAF--SAREIVLLGRYPHARRAGALTHRDGEIAWQALALA---GATALVGRDVTTLSGGELARVQFARVLaqlwpphdaA 170
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1149123047 1262 RQPHILLLDEATSALD-TESEKVVQEALDKAREGRT-CIVIAHRLS-TIQNADLIVVFQNGRVKEHGT 1326
Cdd:PRK13547   171 QPPRYLLLDEPTAALDlAHQHRLLDTVRRLARDWNLgVLAIVHDPNlAARHADRIAMLADGAIVAHGA 238
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
470-657 1.65e-11

ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.


Pssm-ID: 274744 [Multi-domain]  Cd Length: 552  Bit Score: 68.42  E-value: 1.65e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  470 SYPSRKEvkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGmVSVDGQDIRtinvrflreiIGVVSQEPVL 549
Cdd:TIGR03719   13 VVPPKKE--ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNG-EARPQPGIK----------VGYLPQEPQL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  550 FAT-TIAENI-------------------RYGRENVTMD-------EIEKAVKEANAYDFIMKLPHKFDTLVGERG---- 598
Cdd:TIGR03719   80 DPTkTVRENVeegvaeikdaldrfneisaKYAEPDADFDklaaeqaELQEIIDAADAWDLDSQLEIAMDALRCPPWdadv 159
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1149123047  599 AQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALdKARKGrTTIVIAH 657
Cdd:TIGR03719  160 TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHL-QEYPG-TVVAVTH 216
ycf16 CHL00131
sulfate ABC transporter protein; Validated
462-688 2.11e-11

sulfate ABC transporter protein; Validated


Pssm-ID: 214372 [Multi-domain]  Cd Length: 252  Bit Score: 65.82  E-value: 2.11e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYpsrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLM--QRLYDPTEGMVSVDGQDIRTINVR----- 534
Cdd:CHL00131     8 LEIKNLHASV---NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIagHPAYKILEGDILFKGESILDLEPEerahl 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  535 --FLR-----EIIGVVSQEpvlFATTIAENIRYGRENVTMDEIEkavkeanAYDFIM-KLPhkfdtLVGERGAQL----- 601
Cdd:CHL00131    85 giFLAfqypiEIPGVSNAD---FLRLAYNSKRKFQGLPELDPLE-------FLEIINeKLK-----LVGMDPSFLsrnvn 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  602 ---SGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDK-ARKGRTTIVIAH--RLSTVRNADVIAGFDDGV 675
Cdd:CHL00131   150 egfSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKlMTSENSIILITHyqRLLDYIKPDYVHVMQNGK 229
                          250
                   ....*....|...
gi 1149123047  676 IVEKGNhDELMKE 688
Cdd:CHL00131   230 IIKTGD-AELAKE 241
ABC_6TM_YwjA_like cd18549
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ...
191-413 2.21e-11

Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar proteins; This group represents the six-transmembrane helical domain of an uncharacterized ABC transporter YwjA from Bacillus subtilis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349993 [Multi-domain]  Cd Length: 295  Bit Score: 66.32  E-value: 2.21e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  191 IGAGVLVAAYI-------QVSFWCLAAGRQI-HKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINE----GIGD 258
Cdd:cd18549     43 IIGAILLALYIlrtllnyFVTYWGHVMGARIeTDMRRDLFEHLQKLSFSFFDNNKTGQLMSRITNDLFDISElahhGPED 122
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  259 kigmFFQSMATFFTGFIVGFTRGWKLTLVILAISPVLglsaAVWA-----KILSSFTDkellAYAKAG---AVAEEVLAA 330
Cdd:cd18549    123 ----LFISIITIIGSFIILLTINVPLTLIVFALLPLM----IIFTiyfnkKMKKAFRR----VREKIGeinAQLEDSLSG 190
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  331 IRTVIAFGGQKKELERY---NKNLEEAKRIGIkKAITANISIGAAFLLIYasYALAFWYGTTLVLSGEYSIGQVLTvfFS 407
Cdd:cd18549    191 IRVVKAFANEEYEIEKFdegNDRFLESKKKAY-KAMAYFFSGMNFFTNLL--NLVVLVAGGYFIIKGEITLGDLVA--FL 265

                   ....*.
gi 1149123047  408 VLIGAF 413
Cdd:cd18549    266 LYVNVF 271
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
462-680 3.51e-11

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 65.33  E-value: 3.51e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSRKEvkiLKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINV-------- 533
Cdd:PRK11701     7 LSVRGLTKLYGPRKG---CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLyalseaer 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  534 RFL-REIIGVVSQEP-------VLFATTIAENI------RYGRENVT----MDEIEKAVkeanayDFIMKLPHKFdtlvg 595
Cdd:PRK11701    84 RRLlRTEWGFVHQHPrdglrmqVSAGGNIGERLmavgarHYGDIRATagdwLERVEIDA------ARIDDLPTTF----- 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  596 ergaqlSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVqvaLDKARK-----GRTTIVIAHRLSTVRN-ADVIA 669
Cdd:PRK11701   153 ------SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARL---LDLLRGlvrelGLAVVIVTHDLAVARLlAHRLL 223
                          250
                   ....*....|.
gi 1149123047  670 GFDDGVIVEKG 680
Cdd:PRK11701   224 VMKQGRVVESG 234
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
480-662 3.65e-11

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 65.29  E-value: 3.65e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  480 LKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRtinvRFLRE-IIGVVSQE-------PVLFA 551
Cdd:PRK15056    23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR----QALQKnLVAYVPQSeevdwsfPVLVE 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  552 TTIAENiRYGreNVTMDEIEKA-----VKEANAYDFIMKLPHKfdtLVGErgaqLSGGQKQRIAIARALVRNPKILLLDE 626
Cdd:PRK15056    99 DVVMMG-RYG--HMGWLRRAKKrdrqiVTAALARVDMVEFRHR---QIGE----LSGGQKKRVFLARAIAQQGQVILLDE 168
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1149123047  627 ATSALDTESEAVVQVALDKAR-KGRTTIVIAHRLSTV 662
Cdd:PRK15056   169 PFTGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSV 205
ABC_6TM_exporter_like cd18778
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
193-432 3.69e-11

Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 350051 [Multi-domain]  Cd Length: 293  Bit Score: 65.64  E-value: 3.69e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  193 AGVLVAAYI-QVSFWCL-------AAGRQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFF 264
Cdd:cd18778     43 ALLLLGAYLlRALLNFLriylnhvAEQKVVADLRSDLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGI 122
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  265 QSMATFFTGFIVGFTRGWKLTLVILAISPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKEL 344
Cdd:cd18778    123 TNVLTLVGVAIILFSINPKLALLTLIPIPFLALGAWLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEA 202
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  345 ERYNKNLEEAKRIGIKKAITANISIGAAFLLIYASYALAFWYGTTLVLSGEYSIGQVltVFFSVLIGAF--SVGQASPSI 422
Cdd:cd18778    203 KRFEALSRRYRKAQLRAMKLWAIFHPLMEFLTSLGTVLVLGFGGRLVLAGELTIGDL--VAFLLYLGLFyePITSLHGLN 280
                          250
                   ....*....|
gi 1149123047  423 EAFANARGAA 432
Cdd:cd18778    281 EMLQRALAGA 290
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
1132-1316 4.12e-11

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 62.39  E-value: 4.12e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  1132 KGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVlldgkeikrlnvqwlrahlgivsqepILFDCSIAENIAYGDNSRVVs 1211
Cdd:smart00382    1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV--------------------------IYIDGEDILEEVLDQLLLII- 53
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  1212 qeeivraakeanihafieslpnkystkVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALD-- 1289
Cdd:smart00382   54 ---------------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElr 106
                           170       180       190
                    ....*....|....*....|....*....|..
gi 1149123047  1290 -----KAREGRTCIVIAHRLSTIQNADLIVVF 1316
Cdd:smart00382  107 lllllKSEKNLTVILTTNDEKDLGPALLRRRF 138
ABC_6TM_Rv0194_D1_like cd18543
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ...
781-1065 4.18e-11

Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349987 [Multi-domain]  Cd Length: 291  Bit Score: 65.58  E-value: 4.18e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  781 FVVGVFCAIINGGLQPAFAIIFSKIIgvftriDDPETKRQNSNL--FSLLFLALGIISFITFFLQGFTFGKAGEILTKRL 858
Cdd:cd18543      1 LILALLAALLATLAGLAIPLLTRRAI------DGPIAHGDRSALwpLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDL 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  859 RYMVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIgSRLAVITQNIANLGTGIIISFIYGWQLTLLLLAIVPII 938
Cdd:cd18543     75 RTDLFAHLQRLDGAFHD--RWQSGQLLSRATSDLSLVQRFL-AFGPFLLGNLLTLVVGLVVMLVLSPPLALVALASLPPL 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  939 AIAGVVEMKMLSGQALKDKkelEGSGKIATEAIEN---FRTVVSLTQE----QKFEHMyAQSLqvpYRNSLRKAHIFGIT 1011
Cdd:cd18543    152 VLVARRFRRRYFPASRRAQ---DQAGDLATVVEESvtgIRVVKAFGRErrelDRFEAA-ARRL---RATRLRAARLRARF 224
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1149123047 1012 FSFTQAMMYFSYAGCFRFGAYLVAHKLMSFEDvLLVFSAVVfgAMAVGQVSSFA 1065
Cdd:cd18543    225 WPLLEALPELGLAAVLALGGWLVANGSLTLGT-LVAFSAYL--TMLVWPVRMLG 275
ABC_6TM_PCAT1_LagD_like cd18570
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ...
785-1075 4.31e-11

Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.


Pssm-ID: 350014 [Multi-domain]  Cd Length: 294  Bit Score: 65.54  E-value: 4.31e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  785 VFCAIINGGLQPAFAIiFSKIIgvftrIDD--PETKRQNSNLFSLLFLALGIISFITFFLQGFTFGKAGEILTKRLRYMV 862
Cdd:cd18570      8 LLLSLLITLLGIAGSF-FFQIL-----IDDiiPSGDINLLNIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILGY 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  863 FRSMLRQDVSWFDdpKNTTGALTTRLaNDAAQVKGAIGSrlAVITQnIANLGTGIIIS---FIYGWQLTLLLLAIVPIIA 939
Cdd:cd18570     82 FKHLLKLPLSFFE--TRKTGEIISRF-NDANKIREAISS--TTISL-FLDLLMVIISGiilFFYNWKLFLITLLIIPLYI 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  940 IAGVVEMKMLSGqalKDKKELEGSGKIATEAIENFR---TVVSLTQEQKFehmyAQSLQVPYRNSLRKAHIFGITF---- 1012
Cdd:cd18570    156 LIILLFNKPFKK---KNREVMESNAELNSYLIESLKgieTIKSLNAEEQF----LKKIEKKFSKLLKKSFKLGKLSnlqs 228
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1149123047 1013 SFTQAMMYFSYAGCFRFGAYLVAHKLMSFEDvLLVFSAVVFGAM-AVGQVSSFAPDYAKAKISA 1075
Cdd:cd18570    229 SIKGLISLIGSLLILWIGSYLVIKGQLSLGQ-LIAFNALLGYFLgPIENLINLQPKIQEAKVAA 291
3a01203 TIGR00954
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...
1122-1305 5.74e-11

Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 273360 [Multi-domain]  Cd Length: 659  Bit Score: 67.08  E-value: 5.74e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1122 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYdPLAGKVLLDGKEIKrlnvqwlrahLGIVSQEPILFDCSIAENI 1201
Cdd:TIGR00954  467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELW-PVYGGRLTKPAKGK----------LFYVPQRPYMTLGTLRDQI 535
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1202 AYGDNS-----RVVSQEEIVRAAKEANIHAFIESlpNKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSAL 1276
Cdd:TIGR00954  536 IYPDSSedmkrRGLSDKDLEQILDNVQLTHILER--EGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAV 613
                          170       180
                   ....*....|....*....|....*....
gi 1149123047 1277 DTESEKVVQEALDKAreGRTCIVIAHRLS 1305
Cdd:TIGR00954  614 SVDVEGYMYRLCREF--GITLFSVSHRKS 640
PLN03211 PLN03211
ABC transporter G-25; Provisional
1122-1344 6.16e-11

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 66.83  E-value: 6.16e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1122 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLE-RFY-DPLAGKVLLDGKEIKRlnvQWLRaHLGIVSQEPILF-DCSIA 1198
Cdd:PLN03211    83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgRIQgNNFTGTILANNRKPTK---QILK-RTGFVTQDDILYpHLTVR 158
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1199 ENIAYGDNSRV---VSQEEIVRAAkEANIHAFieSLPNKYSTKVGDKGTQ-LSGGQKQRIAIARALVRQPHILLLDEATS 1274
Cdd:PLN03211   159 ETLVFCSLLRLpksLTKQEKILVA-ESVISEL--GLTKCENTIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDEPTS 235
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1149123047 1275 ALD-TESEKVVQEALDKAREGRTCIVIAHRLST--IQNADLIVVFQNGRVKEHGTHQQLLAqkgiYFSMVSVQ 1344
Cdd:PLN03211   236 GLDaTAAYRLVLTLGSLAQKGKTIVTSMHQPSSrvYQMFDSVLVLSEGRCLFFGKGSDAMA----YFESVGFS 304
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
1119-1333 6.48e-11

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 65.52  E-value: 6.48e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1119 DIPVLQGLSLEVKKGQTLALVGSSGCGKS-TVVQLLERFYDP--LAGKVLLDGKEI-----KRLNVqwLRA-HLGIVSQE 1189
Cdd:PRK09473    28 DVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANgrIGGSATFNGREIlnlpeKELNK--LRAeQISMIFQD 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1190 PIlfdCSIAENIAYGDN-----------SRVVSQEEIVR---AAKEANIHAFIESLPNKYStkvgdkgtqlsGGQKQRIA 1255
Cdd:PRK09473   106 PM---TSLNPYMRVGEQlmevlmlhkgmSKAEAFEESVRmldAVKMPEARKRMKMYPHEFS-----------GGMRQRVM 171
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1256 IARALVRQPHILLLDEATSALDTESEKVVQEALDK-AREGRTCIV-IAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLLA 1332
Cdd:PRK09473   172 IAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNElKREFNTAIImITHDLGVVAGiCDKVLVMYAGRTMEYGNARDVFY 251

                   .
gi 1149123047 1333 Q 1333
Cdd:PRK09473   252 Q 252
ABC_6TM_exporter_like cd18563
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
812-1040 7.56e-11

Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 350007 [Multi-domain]  Cd Length: 296  Bit Score: 64.84  E-value: 7.56e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  812 IDD---PETKRQNSNLFSLLFLALGIISFITFFLQ---GFTFGKAGEILTKRLRYMVFRSMLRQDVSWFDdpKNTTGALT 885
Cdd:cd18563     26 IDDvliQLGPGGNTSLLLLLVLGLAGAYVLSALLGilrGRLLARLGERITADLRRDLYEHLQRLSLSFFD--KRQTGSLM 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  886 TRLANDAAQVKGAIGSRLAVITQNIANL-GTGIIIsFIYGWQLTLLLLAIVPIIAIAGVVEMKMLSGQALK-DKKELEGS 963
Cdd:cd18563    104 SRVTSDTDRLQDFLSDGLPDFLTNILMIiGIGVVL-FSLNWKLALLVLIPVPLVVWGSYFFWKKIRRLFHRqWRRWSRLN 182
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  964 GKIAtEAIENFRTVVSLTQEQKFEHMYAQSLQVPYRNSLRkahIFGITFSFTQAMMYFSYAGCF---RFGAYLVAHKLMS 1040
Cdd:cd18563    183 SVLN-DTLPGIRVVKAFGQEKREIKRFDEANQELLDANIR---AEKLWATFFPLLTFLTSLGTLivwYFGGRQVLSGTMT 258
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
1119-1314 8.12e-11

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 66.51  E-value: 8.12e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1119 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLerfydplAGKVLLDGKEI---KRLNVQWL-----RAHLGIVsqep 1190
Cdd:PRK11147    15 DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKIL-------NGEVLLDDGRIiyeQDLIVARLqqdppRNVEGTV---- 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1191 ilFDcSIAENIA--------YGDNSRVVSQEE----IVRAAK-------------EANIHAFIESL---PNKystkvgdK 1242
Cdd:PRK11147    84 --YD-FVAEGIEeqaeylkrYHDISHLVETDPseknLNELAKlqeqldhhnlwqlENRINEVLAQLgldPDA-------A 153
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1149123047 1243 GTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALdKAREGrTCIVIAHRLSTIQN-ADLIV 1314
Cdd:PRK11147   154 LSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFL-KTFQG-SIIFISHDRSFIRNmATRIV 224
sufC PRK09580
cysteine desulfurase ATPase component; Reviewed
1119-1333 9.61e-11

cysteine desulfurase ATPase component; Reviewed


Pssm-ID: 181965 [Multi-domain]  Cd Length: 248  Bit Score: 63.66  E-value: 9.61e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1119 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL--ERFYDPLAGKVLLDGKEIKRLNVQwLRAHLGI--VSQEPI--- 1191
Cdd:PRK09580    13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSPE-DRAGEGIfmAFQYPVeip 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1192 ------LFDCSIAENIAYGDnsrvvsQEEIVRAAKEANIHAFIESL--PNKYSTKVGDKGtqLSGGQKQRIAIARALVRQ 1263
Cdd:PRK09580    92 gvsnqfFLQTALNAVRSYRG------QEPLDRFDFQDLMEEKIALLkmPEDLLTRSVNVG--FSGGEKKRNDILQMAVLE 163
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1149123047 1264 PHILLLDEATSALDTESEKVVQEALDKAREG-RTCIVIAH--RLSTIQNADLIVVFQNGRVKEHGTH---QQLLAQ 1333
Cdd:PRK09580   164 PELCILDESDSGLDIDALKIVADGVNSLRDGkRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDFtlvKQLEEQ 239
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
462-666 9.83e-11

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127 [Multi-domain]  Cd Length: 200  Bit Score: 62.66  E-value: 9.83e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYpsrKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIIG 541
Cdd:PRK13540     2 LDVIELDFDY---HDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCF 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  542 VVSQEPVLFATTIAEN----IRYGRENVTMDEIEKavkeanaydfIMKLPHKFDTLVGergaQLSGGQKQRIAIARALVR 617
Cdd:PRK13540    79 VGHRSGINPYLTLRENclydIHFSPGAVGITELCR----------LFSLEHLIDYPCG----LLSSGQKRQVALLRLWMS 144
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1149123047  618 NPKILLLDEATSALDTESEAVVQVALDKAR-KGRTTIVIAHRLSTVRNAD 666
Cdd:PRK13540   145 KAKLWLLDEPLVALDELSLLTIITKIQEHRaKGGAVLLTSHQDLPLNKAD 194
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
1122-1304 1.11e-10

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 63.59  E-value: 1.11e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1122 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKeikrlnvqwLRahLGIVSQEpILFDCSIAENI 1201
Cdd:PRK09544    19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK---------LR--IGYVPQK-LYLDTTLPLTV 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1202 aygdnSRV------VSQEEIVRAAKEANIHAFIESLPNKystkvgdkgtqLSGGQKQRIAIARALVRQPHILLLDEATSA 1275
Cdd:PRK09544    87 -----NRFlrlrpgTKKEDILPALKRVQAGHLIDAPMQK-----------LSGGETQRVLLARALLNRPQLLVLDEPTQG 150
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1149123047 1276 LDTESEKVVQEALDKAREGRTCIV--IAHRL 1304
Cdd:PRK09544   151 VDVNGQVALYDLIDQLRRELDCAVlmVSHDL 181
ABC_6TM_TAP1 cd18589
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ...
813-999 1.54e-10

Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.


Pssm-ID: 350033 [Multi-domain]  Cd Length: 289  Bit Score: 63.64  E-value: 1.54e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  813 DDPETKRQNSNLFSLLflalGIISFITFFLQGFTFGKAGEILTKRLRYMVFRSMLRQDVSWFDdpKNTTGALTTRLANDA 892
Cdd:cd18589     30 DAPEAFTAAITVMSLL----TIASAVSEFVCDLIYNITMSRIHSRLQGLVFAAVLRQEIAFFD--SNQTGDIVSRVTTDT 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  893 AQVKGAIGSRLAVITQNIANLGTGIIISFIYGWQLTLLLLAIVPIIAIAGVVEMKMLSGQALKDKKELEGSGKIATEAIE 972
Cdd:cd18589    104 EDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQQSLAVQVQKSLARANQVAVETFS 183
                          170       180
                   ....*....|....*....|....*..
gi 1149123047  973 NFRTVVSLTQEQKFEHMYAQSLQVPYR 999
Cdd:cd18589    184 AMKTVRSFANEEGEAQRYRQRLQKTYR 210
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
471-657 2.15e-10

The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.


Pssm-ID: 213204 [Multi-domain]  Cd Length: 246  Bit Score: 62.43  E-value: 2.15e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  471 YPSRKEVKILKGLNLKVQSG-----QTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDI----------RTINVR- 534
Cdd:cd03237      1 YTYPTMKKTLGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVsykpqyikadYEGTVRd 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  535 FLREIIGVVSQEPvLFATTIAEnirygrenvtmdeiekavkeanaydfimklPHKFDTLVGERGAQLSGGQKQRIAIARA 614
Cdd:cd03237     81 LLSSITKDFYTHP-YFKTEIAK------------------------------PLQIEQILDREVPELSGGELQRVAIAAC 129
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1149123047  615 LVRNPKILLLDEATSALDTESEAVVQVAL----DKARKgrTTIVIAH 657
Cdd:cd03237    130 LSKDADIYLLDEPSAYLDVEQRLMASKVIrrfaENNEK--TAFVVEH 174
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
465-636 2.18e-10

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 64.75  E-value: 2.18e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  465 RNVHFSYPSrkeVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVR-FLREIIGVV 543
Cdd:PRK10982     2 SNISKSFPG---VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKeALENGISMV 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  544 SQE-PVLFATTIAENI---RYGRENVTMDEiEKAVKEANAYdfimklphkFDTL-----VGERGAQLSGGQKQRIAIARA 614
Cdd:PRK10982    79 HQElNLVLQRSVMDNMwlgRYPTKGMFVDQ-DKMYRDTKAI---------FDELdididPRAKVATLSVSQMQMIEIAKA 148
                          170       180
                   ....*....|....*....|..
gi 1149123047  615 LVRNPKILLLDEATSALdTESE 636
Cdd:PRK10982   149 FSYNAKIVIMDEPTSSL-TEKE 169
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
487-660 2.26e-10

The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.


Pssm-ID: 213203 [Multi-domain]  Cd Length: 255  Bit Score: 62.77  E-value: 2.26e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  487 VQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSvDGQDIRTInvrfLREIIGVVSQEpvLFATTIAENIRYGRENVT 566
Cdd:cd03236     23 PREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFD-DPPDWDEI----LDEFRGSELQN--YFTKLLEGDVKVIVKPQY 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  567 MDEIEKAVKeANAYDFIMKLP--HKFDTLVG--------ERG-AQLSGGQKQRIAIARALVRNPKILLLDEATSALDTES 635
Cdd:cd03236     96 VDLIPKAVK-GKVGELLKKKDerGKLDELVDqlelrhvlDRNiDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQ 174
                          170       180
                   ....*....|....*....|....*.
gi 1149123047  636 E-AVVQVALDKARKGRTTIVIAHRLS 660
Cdd:cd03236    175 RlNAARLIRELAEDDNYVLVVEHDLA 200
ABC_6TM_exporter_like cd18564
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
827-1075 2.56e-10

Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 350008 [Multi-domain]  Cd Length: 307  Bit Score: 63.30  E-value: 2.56e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  827 LLFLALGIIsFITF------FLQGFTFGKAGEILTKRLRYMVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIG 900
Cdd:cd18564     53 LLLAAAALV-GIALlrglasYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHD--RRRTGDLLSRLTGDVGAIQDLLV 129
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  901 SRLAVITQNIANLGTGIIISFIYGWQLTLLLLAIVPIIAIAgVVEMKMLSGQALKDKKELEGS-GKIATEAIENFRTVVS 979
Cdd:cd18564    130 SGVLPLLTNLLTLVGMLGVMFWLDWQLALIALAVAPLLLLA-ARRFSRRIKEASREQRRREGAlASVAQESLSAIRVVQA 208
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  980 LTQEQKFEHMYAQSLQVPYRNSLRKAHI-------FGITFSFTQAMMYFsyagcfrFGAYLVAHKLMSFEDvLLVFSAVV 1052
Cdd:cd18564    209 FGREEHEERRFARENRKSLRAGLRAARLqallspvVDVLVAVGTALVLW-------FGAWLVLAGRLTPGD-LLVFLAYL 280
                          250       260
                   ....*....|....*....|....
gi 1149123047 1053 FGAMA-VGQVSSFAPDYAKAKISA 1075
Cdd:cd18564    281 KNLYKpVRDLAKLTGRIAKASASA 304
ABC_6TM_Rv0194_D2_like cd18546
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ...
189-406 2.89e-10

Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349990 [Multi-domain]  Cd Length: 292  Bit Score: 62.89  E-value: 2.89e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  189 SGIGAGVLVAAYIQVSFWCLAAGRQ----IHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFF 264
Cdd:cd18546     42 AAAYLAVVLAGWVAQRAQTRLTGRTgerlLYDLRLRVFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLV 121
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  265 QSMATFFTGFIVGFTRGWKLTLVILAISPVLGLsAAVWAKILSSFtdkellAYAKA-GAVAE------EVLAAIRTVIAF 337
Cdd:cd18546    122 VSLLTLVGIAVVLLVLDPRLALVALAALPPLAL-ATRWFRRRSSR------AYRRArERIAAvnadlqETLAGIRVVQAF 194
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  338 GGQKKELERYnKNLEEAKRIGIKKAITAN-ISIGAAFLLIYASYALAFWYGTTLVLSGEYSIGqVLTVFF 406
Cdd:cd18546    195 RRERRNAERF-AELSDDYRDARLRAQRLVaIYFPGVELLGNLATAAVLLVGAWRVAAGTLTVG-VLVAFL 262
ABC_6TM_Rv0194_D2_like cd18546
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ...
824-1078 3.26e-10

Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349990 [Multi-domain]  Cd Length: 292  Bit Score: 62.89  E-value: 3.26e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  824 LFSLLFLALGIISFITFFLQGFTFGKAGEILTKRLRYMVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIGSRL 903
Cdd:cd18546     40 LAAAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFAHLQRLSLDFHE--RETSGRIMTRMTSDIDALSELLQTGL 117
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  904 AVITQNIANLGTGIIISFIYGWQLTLLLLAIVPIIAIAGVVEMKmLSGQALKDKKElegsgKIAT------EAIENFRTV 977
Cdd:cd18546    118 VQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALATRWFRR-RSSRAYRRARE-----RIAAvnadlqETLAGIRVV 191
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  978 VSLTQEQKFEHMYAQsLQVPYRNS-LRKAHIFGITFSFTQAMMYFSYAGCFRFGAYLVAHKLMSFeDVLLVF---SAVVF 1053
Cdd:cd18546    192 QAFRRERRNAERFAE-LSDDYRDArLRAQRLVAIYFPGVELLGNLATAAVLLVGAWRVAAGTLTV-GVLVAFllyLRRFF 269
                          250       260
                   ....*....|....*....|....*
gi 1149123047 1054 GAMavGQVSSFAPDYAKAKISAAHI 1078
Cdd:cd18546    270 API--QQLSQVFDSYQQARAALEKI 292
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
1126-1331 6.96e-10

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 61.10  E-value: 6.96e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1126 LSLEVKKGQTLALVGSSGCGKSTvvqLLERFYD--PLAGKVLLDGKEIKRLNVQWL---RAHLgiVSQEPILF------- 1193
Cdd:PRK03695    15 LSAEVRAGEILHLVGPNGAGKST---LLARMAGllPGSGSIQFAGQPLEAWSAAELarhRAYL--SQQQTPPFampvfqy 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1194 -DCSIAENIAYGDNSRVVsqEEIVRAAKeanihafiesLPNKYSTKVGdkgtQLSGGQKQRIAIArALVRQ------PH- 1265
Cdd:PRK03695    90 lTLHQPDKTRTEAVASAL--NEVAEALG----------LDDKLGRSVN----QLSGGEWQRVRLA-AVVLQvwpdinPAg 152
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1149123047 1266 -ILLLDEATSALDtesekVVQE-ALDK-----AREGRTCIVIAHRLS-TIQNADLIVVFQNGRVKEHGTHQQLL 1331
Cdd:PRK03695   153 qLLLLDEPMNSLD-----VAQQaALDRllselCQQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVL 221
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
1109-1311 8.26e-10

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127 [Multi-domain]  Cd Length: 200  Bit Score: 59.96  E-value: 8.26e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1109 EVVFNYPtrpDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGIVSQ 1188
Cdd:PRK13540     6 ELDFDYH---DQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHR 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1189 EPILFDCSIAENIAYG--DNSRVVSQEEIVRAAKEANIHAFIESLpnkystkvgdkgtqLSGGQKQRIAIARALVRQPHI 1266
Cdd:PRK13540    83 SGINPYLTLRENCLYDihFSPGAVGITELCRLFSLEHLIDYPCGL--------------LSSGQKRQVALLRLWMSKAKL 148
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1149123047 1267 LLLDEATSALDTESEKVVQEALDKAR-EGRTCIVIAHRLSTIQNAD 1311
Cdd:PRK13540   149 WLLDEPLVALDELSLLTIITKIQEHRaKGGAVLLTSHQDLPLNKAD 194
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
482-662 1.64e-09

leucine/isoleucine/valine transporter ATP-binding subunit; Provisional


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 60.00  E-value: 1.64e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  482 GLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDI--------------RTI-NVRFLREIIGV---- 542
Cdd:PRK11300    23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIeglpghqiarmgvvRTFqHVRLFREMTVIenll 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  543 VSQE--------PVLFATTiaeniRYGREnvtmdEIEKAVKEANAYDFIMKLPhkfdtLVGERGAQLSGGQKQRIAIARA 614
Cdd:PRK11300   103 VAQHqqlktglfSGLLKTP-----AFRRA-----ESEALDRAATWLERVGLLE-----HANRQAGNLAYGQQRRLEIARC 167
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1149123047  615 LVRNPKILLLDEATSALDTESEAVVQVALDKARK--GRTTIVIAHRLSTV 662
Cdd:PRK11300   168 MVTQPEILMLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLV 217
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
1118-1320 1.86e-09

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 61.67  E-value: 1.86e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1118 PDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIK-RLNVQWLRAHLGIVSQE-PILFDC 1195
Cdd:PRK10982     9 PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQElNLVLQR 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1196 SIAENIAYGDNSR---VVSQEEIVRAAKeanihAFIESLPNKYSTKvgDKGTQLSGGQKQRIAIARALVRQPHILLLDEA 1272
Cdd:PRK10982    89 SVMDNMWLGRYPTkgmFVDQDKMYRDTK-----AIFDELDIDIDPR--AKVATLSVSQMQMIEIAKAFSYNAKIVIMDEP 161
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1149123047 1273 TSALdteSEKVVQ---EALDKAREgRTC--IVIAHRLSTI-QNADLIVVFQNGR 1320
Cdd:PRK10982   162 TSSL---TEKEVNhlfTIIRKLKE-RGCgiVYISHKMEEIfQLCDEITILRDGQ 211
ABC_6TM_exporter_like cd18550
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
798-940 2.22e-09

Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349994 [Multi-domain]  Cd Length: 294  Bit Score: 60.19  E-value: 2.22e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  798 FAIIFSKIIGV----FTR--IDD--PETKRQNSNLFSLLFLALGIISFITFFLQGFTFGKAGEILTKRLRYMVFRSMLRQ 869
Cdd:cd18550      6 LLILLSALLGLlpplLLReiIDDalPQGDLGLLVLLALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRVQLYAHLQRM 85
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1149123047  870 DVSWFDDPKntTGALTTRLANDAAQVKGAIGSRLAVITQNIANLGTGIIISFIYGWQLTLLLLAIVPIIAI 940
Cdd:cd18550     86 SLAFFTRTR--TGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVL 154
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
1127-1331 2.33e-09

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 61.47  E-value: 2.33e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1127 SLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIK-RLNVQWLRAhlGIV------SQEPILFDCSIAE 1199
Cdd:PRK11288   273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDiRSPRDAIRA--GIMlcpedrKAEGIIPVHSVAD 350
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1200 NIAYGDNSRVVSQEEIVRAAKEA-NIHAFIESL----PNKySTKVGdkgtQLSGGQKQRIAIARALVRQPHILLLDEATS 1274
Cdd:PRK11288   351 NINISARRHHLRAGCLINNRWEAeNADRFIRSLniktPSR-EQLIM----NLSGGNQQKAILGRWLSEDMKVILLDEPTR 425
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1149123047 1275 ALDTESEKVVQEAL-DKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRV-----KEHGTHQQLL 1331
Cdd:PRK11288   426 GIDVGAKHEIYNVIyELAAQGVAVLFVSSDLPEVLGvADRIVVMREGRIagelaREQATERQAL 489
ABC_6TM_exporter_like cd18778
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
781-943 3.04e-09

Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 350051 [Multi-domain]  Cd Length: 293  Bit Score: 59.86  E-value: 3.04e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  781 FVVGVFCAIINGGLQpafaIIFSKIIGVFT-RIDDPETKRQNSNLFSLLFLALGIISFITFFLQGFTFGKAGEILTKRLR 859
Cdd:cd18778      1 LILTLLCALLSTLLG----LVPPWLIRELVdLVTIGSKSLGLLLGLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADLR 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  860 YMVFRSMLRQDVSWFDDPKntTGALTTRLANDAAQVKGAIgsrLAVITQNIANLGTGIIIS---FIYGWQLTLLLLAIVP 936
Cdd:cd18778     77 SDLYDKLQRLSLRYFDDRQ--TGDLMSRVINDVANVERLI---ADGIPQGITNVLTLVGVAiilFSINPKLALLTLIPIP 151

                   ....*..
gi 1149123047  937 IIAIAGV 943
Cdd:cd18778    152 FLALGAW 158
PLN03211 PLN03211
ABC transporter G-25; Provisional
475-661 3.42e-09

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 61.43  E-value: 3.42e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  475 KEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQ-LMQRLYDPT-EGMVSVDGqdiRTINVRFLREIiGVVSQEPVLFA- 551
Cdd:PLN03211    79 QERTILNGVTGMASPGEILAVLGPSGSGKSTLLNaLAGRIQGNNfTGTILANN---RKPTKQILKRT-GFVTQDDILYPh 154
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  552 TTIAENIRYGRENVTMDEIEKAVKEANAYDFI--MKLPHKFDTLVGE---RGaqLSGGQKQRIAIARALVRNPKILLLDE 626
Cdd:PLN03211   155 LTVRETLVFCSLLRLPKSLTKQEKILVAESVIseLGLTKCENTIIGNsfiRG--ISGGERKRVSIAHEMLINPSLLILDE 232
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1149123047  627 ATSALD-TESEAVVQVALDKARKGRTTIVIAHRLST 661
Cdd:PLN03211   233 PTSGLDaTAAYRLVLTLGSLAQKGKTIVTSMHQPSS 268
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
1126-1326 3.42e-09

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 60.14  E-value: 3.42e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1126 LSLEVKKGQTLALVGSSGCGKS----TVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLR----AHLGIVSQEPI--LFDC 1195
Cdd:PRK11022    26 ISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISEKERRnlvgAEVAMIFQDPMtsLNPC 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1196 -----SIAENIAY--GDNSRVVSQeeivRAakeanihafIESLpnkysTKVG--DKGT-------QLSGGQKQRIAIARA 1259
Cdd:PRK11022   106 ytvgfQIMEAIKVhqGGNKKTRRQ----RA---------IDLL-----NQVGipDPASrldvyphQLSGGMSQRVMIAMA 167
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1260 LVRQPHILLLDEATSALD-TESEKVVQEALD-KAREGRTCIVIAHRLSTI-QNADLIVVFQNGRVKEHGT 1326
Cdd:PRK11022   168 IACRPKLLIADEPTTALDvTIQAQIIELLLElQQKENMALVLITHDLALVaEAAHKIIVMYAGQVVETGK 237
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
1123-1307 4.07e-09

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 59.13  E-value: 4.07e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1123 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLGiVSQE-----PILFDcSI 1197
Cdd:PRK15056    23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYVP-QSEEvdwsfPVLVE-DV 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1198 AENIAYGDNSRVVSQEEIVRAAKEANIhAFIESLPNKYStKVGdkgtQLSGGQKQRIAIARALVRQPHILLLDEATSALD 1277
Cdd:PRK15056   101 VMMGRYGHMGWLRRAKKRDRQIVTAAL-ARVDMVEFRHR-QIG----ELSGGQKKRVFLARAIAQQGQVILLDEPFTGVD 174
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1149123047 1278 TESEKVVQEALDKAR-EGRTCIVIAHRLSTI 1307
Cdd:PRK15056   175 VKTEARIISLLRELRdEGKTMLVSTHNLGSV 205
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
1108-1323 4.65e-09

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 60.57  E-value: 4.65e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1108 GEVVFNYP--TRPDIPVLQGLSLEVKKGQTLALVGSSGCGKStvvQLLERFY--DPLA-GKVLLDGKEIK-RLNVQWLRA 1181
Cdd:PRK09700   262 HETVFEVRnvTSRDRKKVRDISFSVCRGEILGFAGLVGSGRT---ELMNCLFgvDKRAgGEIRLNGKDISpRSPLDAVKK 338
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1182 HLGIVSQ---EPILF-DCSIAENIA---------YGDNSRVVSQEEIVRAAKEANihafiESLPNKYSTkVGDKGTQLSG 1248
Cdd:PRK09700   339 GMAYITEsrrDNGFFpNFSIAQNMAisrslkdggYKGAMGLFHEVDEQRTAENQR-----ELLALKCHS-VNQNITELSG 412
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1149123047 1249 GQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQNA-DLIVVFQNGRVKE 1323
Cdd:PRK09700   413 GNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQlADDGKVILMVSSELPEIITVcDRIAVFCEGRLTQ 489
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
442-634 4.97e-09

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 60.73  E-value: 4.97e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  442 KPSIDSYSKSGhkpdniKGNLEFRNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMV 521
Cdd:PRK11147   306 KMQVEEASRSG------KIVFEMENVNYQIDGKQ---LVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI 376
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  522 SVDGQdirtINVRFL---REIIgvvsqEPvlfATTIAENIRYGRENVTMDEIEKAVKeanAY--DFIMKlPHKFDTLVge 596
Cdd:PRK11147   377 HCGTK----LEVAYFdqhRAEL-----DP---EKTVMDNLAEGKQEVMVNGRPRHVL---GYlqDFLFH-PKRAMTPV-- 438
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1149123047  597 rgAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTE 634
Cdd:PRK11147   439 --KALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVE 474
ABC_6TM_PrtD_LapB_HlyB_like cd18566
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ...
821-1034 5.22e-09

Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.


Pssm-ID: 350010 [Multi-domain]  Cd Length: 294  Bit Score: 59.13  E-value: 5.22e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  821 NSNLFSLLFLALGIISFITF-----FLQGFTFGKAGEILTKRLRYMVFRSMLRQDVSWFDdpKNTTGALTTRLaNDAAQV 895
Cdd:cd18566     35 NESIPTLQVLVIGVVIAILLesllrLLRSYILAWIGARFDHRLSNAAFEHLLSLPLSFFE--REPSGAHLERL-NSLEQI 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  896 KGAIGSRLAVITQNIANLGTGIIISFIYGWQLTLLLLAIVPIIAIAGVVEMKMLSgQALKDKKELEGS-GKIATEAIENF 974
Cdd:cd18566    112 REFLTGQALLALLDLPFVLIFLGLIWYLGGKLVLVPLVLLGLFVLVAILLGPILR-RALKERSRADERrQNFLIETLTGI 190
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1149123047  975 RTVVSLTQEQ----KFEHMYAQSLQVPYRNSLRKAHIFGITFSFTQAMMyfsyAGCFRFGAYLV 1034
Cdd:cd18566    191 HTIKAMAMEPqmlrRYERLQANAAYAGFKVAKINAVAQTLGQLFSQVSM----VAVVAFGALLV 250
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
1123-1314 5.37e-09

ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.


Pssm-ID: 213238 [Multi-domain]  Cd Length: 261  Bit Score: 58.78  E-value: 5.37e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1123 LQGLSLEVKKGQTLALVGSSGCGKSTVVqlLERFYDPLAGKVLLDGKEIKRLNVQWLRAHLG---IVSQEPI-------- 1191
Cdd:cd03271     11 LKNIDVDIPLGVLTCVTGVSGSGKSSLI--NDTLYPALARRLHLKKEQPGNHDRIEGLEHIDkviVIDQSPIgrtprsnp 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1192 -----LFD------CSIAENIAYgdNSRVVSqeeiVRAaKEANIH-----------AFIESLP---NKYST--------- 1237
Cdd:cd03271     89 atytgVFDeirelfCEVCKGKRY--NRETLE----VRY-KGKSIAdvldmtveealEFFENIPkiaRKLQTlcdvglgyi 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1238 KVGDKGTQLSGGQKQRIAIARALVRQ---PHILLLDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQNADLI 1313
Cdd:cd03271    162 KLGQPATTLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRLVDkGNTVVVIEHNLDVIKCADWI 241

                   .
gi 1149123047 1314 V 1314
Cdd:cd03271    242 I 242
ABC_6TM_PrtD_LapB_HlyB_like cd18782
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ...
191-411 7.80e-09

uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.


Pssm-ID: 350055 [Multi-domain]  Cd Length: 294  Bit Score: 58.76  E-value: 7.80e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  191 IGAGVLVAAYIQVSFWCL-------AAGRQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLtDDVSKINEGI-GDKIGM 262
Cdd:cd18782     44 IGVVMLVAALLEAVLTALrtylftdTANRIDLELGGTIIDHLLRLPLGFFDKRPVGELSTRI-SELDTIRGFLtGTALTT 122
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  263 FFQSMATFFTgFIVGFTRGWKLTLVILAISPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAfggQKK 342
Cdd:cd18782    123 LLDVLFSVIY-IAVLFSYSPLLTLVVLATVPLQLLLTFLFGPILRRQIRRRAEASAKTQSYLVESLTGIQTVKA---QNA 198
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1149123047  343 EL-------ERYNKNLEEAKRIGIKKAITANISigaaFLLIYASYALAFWYGTTLVLSGEYSIGQVLTvfFSVLIG 411
Cdd:cd18782    199 ELkarwrwqNRYARSLGEGFKLTVLGTTSGSLS----QFLNKLSSLLVLWVGAYLVLRGELTLGQLIA--FRILSG 268
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
471-635 8.06e-09

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 59.75  E-value: 8.06e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  471 YPSRKevKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGmvsvdgqdirtiNVRFLREI-IGVVSQEPVL 549
Cdd:PRK11819    16 VPPKK--QILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEG------------EARPAPGIkVGYLPQEPQL 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  550 FAT-TIAENIRYGrenvtMDEIEKAVKEANAYDFIMKLPH-KFDTLVGERG----------------------------- 598
Cdd:PRK11819    82 DPEkTVRENVEEG-----VAEVKAALDRFNEIYAAYAEPDaDFDALAAEQGelqeiidaadawdldsqleiamdalrcpp 156
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1149123047  599 -----AQLSGGQKQRIAIARALVRNPKILLLDEATSALDTES 635
Cdd:PRK11819   157 wdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
PLN03140 PLN03140
ABC transporter G family member; Provisional
477-682 9.94e-09

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 60.24  E-value: 9.94e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  477 VKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLM--QRLYDPTEGMVSVDG-----------------QDIRT--INVR- 534
Cdd:PLN03140   893 LQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLagRKTGGYIEGDIRISGfpkkqetfarisgyceqNDIHSpqVTVRe 972
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  535 ------FLREIIGVVSQEPVLFattiaenirygrenvtMDEIEKAVKEANAYDFIMKLPhkfdtlvGERGaqLSGGQKQR 608
Cdd:PLN03140   973 sliysaFLRLPKEVSKEEKMMF----------------VDEVMELVELDNLKDAIVGLP-------GVTG--LSTEQRKR 1027
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1149123047  609 IAIARALVRNPKILLLDEATSALDTESEAVVQVAL-DKARKGRTTIVIAHRLSTvrnaDVIAGFDDGVIVEKGNH 682
Cdd:PLN03140  1028 LTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVrNTVDTGRTVVCTIHQPSI----DIFEAFDELLLMKRGGQ 1098
3a01203 TIGR00954
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...
464-660 1.06e-08

Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 273360 [Multi-domain]  Cd Length: 659  Bit Score: 59.76  E-value: 1.06e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  464 FRNVHFSYPSRKevKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGqdirtinvrflREIIGVV 543
Cdd:TIGR00954  454 FENIPLVTPNGD--VLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPA-----------KGKLFYV 520
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  544 SQEPVLFATTIAENIRYgrENVTMDEIEKAVKEAN--AYDFIMKLPHKFDTLVGERGAQ-----LSGGQKQRIAIARALV 616
Cdd:TIGR00954  521 PQRPYMTLGTLRDQIIY--PDSSEDMKRRGLSDKDleQILDNVQLTHILEREGGWSAVQdwmdvLSGGEKQRIAMARLFY 598
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1149123047  617 RNPKILLLDEATSALDTESE-AVVQVAldkARKGRTTIVIAHRLS 660
Cdd:TIGR00954  599 HKPQFAILDECTSAVSVDVEgYMYRLC---REFGITLFSVSHRKS 640
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
480-668 1.08e-08

ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.


Pssm-ID: 213238 [Multi-domain]  Cd Length: 261  Bit Score: 57.62  E-value: 1.08e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  480 LKGLNLKVQSGQTVALVGNSGCGKSTTVQ------LMQRL---------YDPTEGMVSVDgqdiRTINV------RFLRE 538
Cdd:cd03271     11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINdtlypaLARRLhlkkeqpgnHDRIEGLEHID----KVIVIdqspigRTPRS 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  539 I----IGVVSQEPVLFATtIAENIRYGRE-------NVTMDEI-EKAVKEAnaYDF---IMKLPHKFDTLV--------- 594
Cdd:cd03271     87 NpatyTGVFDEIRELFCE-VCKGKRYNREtlevrykGKSIADVlDMTVEEA--LEFfenIPKIARKLQTLCdvglgyikl 163
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1149123047  595 GERGAQLSGGQKQRIAIARALVR---NPKILLLDEATSALDTESEAVVQVALDK-ARKGRTTIVIAHRLSTVRNADVI 668
Cdd:cd03271    164 GQPATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRlVDKGNTVVVIEHNLDVIKCADWI 241
ABC_6TM_T1SS_like cd18555
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ...
190-413 1.30e-08

Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.


Pssm-ID: 349999 [Multi-domain]  Cd Length: 294  Bit Score: 57.91  E-value: 1.30e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  190 GIGAGVLVAAYIQVSF---WCLAagrQIHK-----IRKQFFHAIMRQEIGWFDVHDVGELNTRLtDDVSKINEGIGDKIG 261
Cdd:cd18555     45 GIGILILFLLYGLFSFlrgYIII---KLQTkldksLMSDFFEHLLKLPYSFFENRSSGDLLFRA-NSNVYIRQILSNQVI 120
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  262 MFFQSMATFFTGFIVGFTRGWKLTLVILAISPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQK 341
Cdd:cd18555    121 SLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLLLLLTRKKIKKLNQEEIVAQTKVQSYLTETLYGIETIKSLGSEK 200
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1149123047  342 KELERYNKNLEEAKRIGIKKAITANISIGAAFLLIYASYALAFWYGTTLVLSGEYSIGQVLTvfFSVLIGAF 413
Cdd:cd18555    201 NIYKKWENLFKKQLKAFKKKERLSNILNSISSSIQFIAPLLILWIGAYLVINGELTLGELIA--FSSLAGSF 270
ABC_6TM_HetC_like cd18568
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ...
220-411 1.45e-08

Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.


Pssm-ID: 350012 [Multi-domain]  Cd Length: 294  Bit Score: 57.96  E-value: 1.45e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  220 QFFHAIMRQEIGWFDVHDVGELNTRltddvskINEGigDKIGMFF--QSMATF---FTGFIVG---FTRGWKLTLVILAI 291
Cdd:cd18568     80 DFYKHLLSLPLSFFASRKVGDIITR-------FQEN--QKIRRFLtrSALTTIldlLMVFIYLglmFYYNLQLTLIVLAF 150
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  292 SPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQ----KKELERYNKNLEEAKRiGIKKAITANI 367
Cdd:cd18568    151 IPLYVLLTLLSSPKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAErpirWRWENKFAKALNTRFR-GQKLSIVLQL 229
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1149123047  368 SIGAAFLLiyaSYALAFWYGTTLVLSGEYSIGQVltVFFSVLIG 411
Cdd:cd18568    230 ISSLINHL---GTIAVLWYGAYLVISGQLTIGQL--VAFNMLFG 268
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
462-628 1.82e-08

ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 58.49  E-value: 1.82e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVhfsypSRKEVkiLKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRF-LREII 540
Cdd:COG1129    257 LEVEGL-----SVGGV--VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDaIRAGI 329
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  541 GVVS----QEPVLFATTIAENI------RYGReNVTMDEiEKAVKEANAY--DFIMKLPHKfDTLVGergaQLSGGQKQR 608
Cdd:COG1129    330 AYVPedrkGEGLVLDLSIRENItlasldRLSR-GGLLDR-RRERALAEEYikRLRIKTPSP-EQPVG----NLSGGNQQK 402
                          170       180
                   ....*....|....*....|
gi 1149123047  609 IAIARALVRNPKILLLDEAT 628
Cdd:COG1129    403 VVLAKWLATDPKVLILDEPT 422
PRK13543 PRK13543
heme ABC exporter ATP-binding protein CcmA;
1116-1279 2.27e-08

heme ABC exporter ATP-binding protein CcmA;


Pssm-ID: 184129 [Multi-domain]  Cd Length: 214  Bit Score: 56.01  E-value: 2.27e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1116 TRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNvqwlRA-HLGIVSQEPIL-F 1193
Cdd:PRK13543    20 SRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD----RSrFMAYLGHLPGLkA 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1194 DCSIAENIAY--GDNSRVVSQeeivraakeanihafiesLPNKYSTKVGDKG------TQLSGGQKQRIAIARALVRQPH 1265
Cdd:PRK13543    96 DLSTLENLHFlcGLHGRRAKQ------------------MPGSALAIVGLAGyedtlvRQLSAGQKKRLALARLWLSPAP 157
                          170
                   ....*....|....
gi 1149123047 1266 ILLLDEATSALDTE 1279
Cdd:PRK13543   158 LWLLDEPYANLDLE 171
ABC_6TM_exporter_like cd18565
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
829-1053 2.87e-08

Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 350009 [Multi-domain]  Cd Length: 313  Bit Score: 57.19  E-value: 2.87e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  829 FLALGIISFITF-------FLQGFTFGKAGEILTKRLRYMVFRSMLRQDVSWFDDpkNTTGALTTRLANDAAQVKGAIGS 901
Cdd:cd18565     53 LWLLGGLTVAAFlleslfqYLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFED--RQTGDLMSVLNNDVNQLERFLDD 130
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  902 RLAVITQNIANLGTGIIISFIYGWQLTLLLLAIVPIIAIAGVVEMKMLSGQALKDKKELegsGKIAT---EAIENFRTVV 978
Cdd:cd18565    131 GANSIIRVVVTVLGIGAILFYLNWQLALVALLPVPLIIAGTYWFQRRIEPRYRAVREAV---GDLNArleNNLSGIAVIK 207
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1149123047  979 SLTQEQK-FEHMYAQSLQvpYRNSLRKAHIFGITFSFT-QAMMYFSYAGCFRFGAYLVAHKLMSFEDVLLVFSAVVF 1053
Cdd:cd18565    208 AFTAEDFeRERVADASEE--YRDANWRAIRLRAAFFPViRLVAGAGFVATFVVGGYWVLDGPPLFTGTLTVGTLVTF 282
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
599-755 2.97e-08

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 58.04  E-value: 2.97e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  599 AQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALdKARKGrTTIVIAHRLSTVRN-ADVIAGFDDGVIV 677
Cdd:PRK11147   155 SSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFL-KTFQG-SIIFISHDRSFIRNmATRIVDLDRGKLV 232
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  678 E-KGNHDELMKEKGIYFKLVTMQTAGNEVELenaADES---KSEIDAlEMSSNDSR----SSLIRKRSTRRSVRGS---Q 746
Cdd:PRK11147   233 SyPGNYDQYLLEKEEALRVEELQNAEFDRKL---AQEEvwiRQGIKA-RRTRNEGRvralKALRRERSERREVMGTakmQ 308

                   ....*....
gi 1149123047  747 AQDRKLSTK 755
Cdd:PRK11147   309 VEEASRSGK 317
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
475-1338 3.00e-08

Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 58.58  E-value: 3.00e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  475 KEVKILKGLNLKVQSGQTVALVGNSGCGKST-----TVQLMQRLYDpTEGMVSVDGQDIRTInVRFLREIIGVVSQEPVL 549
Cdd:TIGR00956   72 KTFDILKPMDGLIKPGELTVVLGRPGSGCSTllktiASNTDGFHIG-VEGVITYDGITPEEI-KKHYRGDVVYNAETDVH 149
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  550 FAT-TIAE-----------NIRYgrENVtmDEIEKAVKEANAYDFIMKLPHKFDTLVGE---RGaqLSGGQKQRIAIARA 614
Cdd:TIGR00956  150 FPHlTVGEtldfaarcktpQNRP--DGV--SREEYAKHIADVYMATYGLSHTRNTKVGNdfvRG--VSGGERKRVSIAEA 223
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  615 LVRNPKILLLDEATSALDTESeavvqvALDKARKGRTTIVIAHRLSTV------RNA----DVIAGFDDGVIVEKGNHDE 684
Cdd:TIGR00956  224 SLGGAKIQCWDNATRGLDSAT------ALEFIRALKTSANILDTTPLVaiyqcsQDAyelfDKVIVLYEGYQIYFGPADK 297
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  685 LMKekgiYFK--------------LVTMQTAGNEvELENAADESKSEIDALEMSS---NDSRSSLIRKRSTRRSVRGSQA 747
Cdd:TIGR00956  298 AKQ----YFEkmgfkcpdrqttadFLTSLTSPAE-RQIKPGYEKKVPRTPQEFETywrNSPEYAQLMKEIDEYLDRCSES 372
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  748 QDRKL--------STKEALDESIPPVSFWRIMKlnltewpYFVVGVFCAIINGGLQPAF----AIIFSKIIG-VFTRIDD 814
Cdd:TIGR00956  373 DTKEAyreshvakQSKRTRPSSPYTVSFSMQVK-------YCLARNFLRMKGNPSFTLFmvfgNIIMALILSsVFYNLPK 445
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  815 PETK---RQNSNLFSLLFLALgiisfiTFFLQGFTFGKAGEILTKRLRYMVFRSM--------------LRQDVSWF--- 874
Cdd:TIGR00956  446 NTSDfysRGGALFFAILFNAF------SSLLEIASMYEARPIVEKHRKYALYHPSadaiasiiseipfkIIESVVFNiil 519
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  875 ---DDPKNTTGALTTRLAND--AAQVKGAIGSRLAVITQNI--ANLGTGIIIsfiygwqLTLLLLA--IVPIIAIAG--- 942
Cdd:TIGR00956  520 yfmVNFRRTAGRFFFYLLILfiCTLAMSHLFRSIGAVTKTLseAMTPAAILL-------LALSIYTgfAIPRPSMLGwsk 592
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  943 ----------------VVEM---KMLSGQALKdkkelEGSGKIATEAIENFRTVVSLTQEQKF---EHMYAQSLQVPYRN 1000
Cdd:TIGR00956  593 wiyyvnplayafeslmVNEFhgrRFECSQYVP-----SGGGYDNLGVTNKVCTVVGAEPGQDYvdgDDYLKLSFQYYNSH 667
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1001 SLRKahiFGITFSFTqammyfsyagCFRFGAYLVAHKLMSfedvllvfsavvfGAMAVGQVSSF----APDYAKA-KISA 1075
Cdd:TIGR00956  668 KWRN---FGIIIGFT----------VFFFFVYILLTEFNK-------------GAKQKGEILVFrrgsLKRAKKAgETSA 721
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1076 AHII-----MIIEKTPLIDS---YSTEGLMPNTLEGNVTF-GEVVFNYPTRPDIPV-LQGLSLEVKKGQTLALVGSSGCG 1145
Cdd:TIGR00956  722 SNKNdieagEVLGSTDLTDEsddVNDEKDMEKESGEDIFHwRNLTYEVKIKKEKRViLNNVDGWVKPGTLTALMGASGAG 801
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1146 KSTvvqLLerfyDPLAGkvlldgkeikRLNVQWLRAHLGIVSQEPIlfDCSIAENIAYGDNSRVVSQEEIVRaakEANIH 1225
Cdd:TIGR00956  802 KTT---LL----NVLAE----------RVTTGVITGGDRLVNGRPL--DSSFQRSIGYVQQQDLHLPTSTVR---ESLRF 859
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1226 AFIESLPNKYSTK----------------------VGDKGTQLSGGQKQRIAIARALVRQPHILL-LDEATSALDTESEK 1282
Cdd:TIGR00956  860 SAYLRQPKSVSKSekmeyveevikllemesyadavVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAW 939
                          970       980       990      1000      1010      1020
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1283 VVQEALDK-AREGRTCIVIAHRLStiqnADLIVVFQngrvkehgthQQLLAQKG---IYF 1338
Cdd:TIGR00956  940 SICKLMRKlADHGQAILCTIHQPS----AILFEEFD----------RLLLLQKGgqtVYF 985
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
1106-1316 3.18e-08

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 57.90  E-value: 3.18e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1106 TFGEVVFNYPtrpDIPV-LQGLSLEV-----KKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDgkeikrLNV--- 1176
Cdd:PRK13409   335 SERETLVEYP---DLTKkLGDFSLEVeggeiYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE------LKIsyk 405
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1177 -QWLRA-HLGIVSQepilFDCSIAENIaygDNSRVvsQEEIVraaKEANIHAFIESlpnkystKVGDkgtqLSGGQKQRI 1254
Cdd:PRK13409   406 pQYIKPdYDGTVED----LLRSITDDL---GSSYY--KSEII---KPLQLERLLDK-------NVKD----LSGGELQRV 462
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1149123047 1255 AIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGR--TCIVIAHRLSTIQN-ADLIVVF 1316
Cdd:PRK13409   463 AIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEReaTALVVDHDIYMIDYiSDRLMVF 527
ABC_6TM_exporter_like cd18540
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
181-407 3.36e-08

Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349984 [Multi-domain]  Cd Length: 295  Bit Score: 56.72  E-value: 3.36e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  181 MTRYA-------------YYYSGIGAGVLVAAYIQVSFWCLAAGRQ----IHKIRKQFFHAIMRQEIGWFDVHDVGELNT 243
Cdd:cd18540     24 LTKYAidhfitpgtldglTGFILLYLGLILIQALSVFLFIRLAGKIemgvSYDLRKKAFEHLQTLSFSYFDKTPVGWIMA 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  244 RLTDDVSKINE----GIGDkigMFFQSMATFFTgFIVGFTRGWKLTLVILAISPVLglsaaVWAKILssFTDKELLAYAK 319
Cdd:cd18540    104 RVTSDTQRLGEiiswGLVD---LVWGITYMIGI-LIVMLILNWKLALIVLAVVPVL-----AVVSIY--FQKKILKAYRK 172
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  320 AGAVAEEVLAA-------IRTVIAFGGQKKELERYNKNLEEAKRIGIKKAITANISIGAAFLLIYASYALAFWYGTTLVL 392
Cdd:cd18540    173 VRKINSRITGAfnegitgAKTTKTLVREEKNLREFKELTEEMRRASVRAARLSALFLPIVLFLGSIATALVLWYGGILVL 252
                          250
                   ....*....|....*
gi 1149123047  393 SGEYSIGQvLTVFFS 407
Cdd:cd18540    253 AGAITIGT-LVAFIS 266
ABC_6TM_CyaB_HlyB_like cd18588
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ...
274-414 3.84e-08

Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunits of T1SS, such as CyaG and HlyB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. Additionally, CyaB is part of the three T1SS complex proteins for adenylate cyclase toxin CyaA, which is a primary virulence factor in Bordetella pertussis: CyaB (an ABC transporter) CyaD (a membrane fusion protein), and CyaE (an outer membrane protein).


Pssm-ID: 350032 [Multi-domain]  Cd Length: 294  Bit Score: 56.35  E-value: 3.84e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  274 FIVGFTRGWKLTLVILAISPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEE 353
Cdd:cd18588    133 LAVMFYYSPTLTLIVLASLPLYALLSLLVTPILRRRLEEKFQRGAENQSFLVETVTGIETVKSLAVEPQFQRRWEELLAR 212
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1149123047  354 AKRIGIKKAITANISIGAAFLLIYASYALAFWYGTTLVLSGEYSIGQVltVFFSVLIGAFS 414
Cdd:cd18588    213 YVKASFKTANLSNLASQIVQLIQKLTTLAILWFGAYLVMDGELTIGQL--IAFNMLAGQVS 271
ABC_6TM_ABCC_D2 cd18580
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ...
178-419 3.89e-08

Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.


Pssm-ID: 350024 [Multi-domain]  Cd Length: 294  Bit Score: 56.36  E-value: 3.89e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  178 EEDMTRYAYYYSGIGAGVLVAAYIQVSFW----CLAAGRQIHKirkQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKIN 253
Cdd:cd18580     34 NSSSGYYLGVYAALLVLASVLLVLLRWLLfvlaGLRASRRLHD---KLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLID 110
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  254 EGIGDKIGMFFQSMATFFTGFIV-GFTRGWkltlvILAISPVLGLSAAVWAK-------------------ILSSFTdke 313
Cdd:cd18580    111 EELPLALLDFLQSLFSVLGSLIViAIVSPY-----FLIVLPPLLVVYYLLQRyylrtsrqlrrlesesrspLYSHFS--- 182
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  314 llayakagavaeEVLAAIRTVIAFGGQKKELERYNKNLeeakrigikkaitaNISIGAAFLLIYASYALAFWYgttlvls 393
Cdd:cd18580    183 ------------ETLSGLSTIRAFGWQERFIEENLRLL--------------DASQRAFYLLLAVQRWLGLRL------- 229
                          250       260
                   ....*....|....*....|....*.
gi 1149123047  394 geysigQVLTVFFSVLIGAFSVGQAS 419
Cdd:cd18580    230 ------DLLGALLALVVALLAVLLRS 249
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
483-659 4.50e-08

retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]


Pssm-ID: 130324 [Multi-domain]  Cd Length: 2272  Bit Score: 58.10  E-value: 4.50e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  483 LNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTiNVRFLREIIGVVSQEPVLfattiaENIRYGR 562
Cdd:TIGR01257 1958 LCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDVHQNMGYCPQFDAI------DDLLTGR 2030
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  563 EN---------VTMDEIEKAvkeANAYDFIMKLPHKFDTLVGergaQLSGGQKQRIAIARALVRNPKILLLDEATSALDT 633
Cdd:TIGR01257 2031 EHlylyarlrgVPAEEIEKV---ANWSIQSLGLSLYADRLAG----TYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDP 2103
                          170       180
                   ....*....|....*....|....*..
gi 1149123047  634 ESEAVV-QVALDKARKGRTTIVIAHRL 659
Cdd:TIGR01257 2104 QARRMLwNTIVSIIREGRAVVLTSHSM 2130
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
1121-1335 4.74e-08

retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]


Pssm-ID: 130324 [Multi-domain]  Cd Length: 2272  Bit Score: 58.10  E-value: 4.74e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1121 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIkRLNVQWLRAHLGIVSQEPILFDCSIA-E 1199
Cdd:TIGR01257 1953 PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI-LTNISDVHQNMGYCPQFDAIDDLLTGrE 2031
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1200 NIAYGDNSRVVSQEEIVRAAKEAnihafIESLP-NKYSTKVGdkGTqLSGGQKQRIAIARALVRQPHILLLDEATSALDT 1278
Cdd:TIGR01257 2032 HLYLYARLRGVPAEEIEKVANWS-----IQSLGlSLYADRLA--GT-YSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDP 2103
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1149123047 1279 ESEKVVQEAL-DKAREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLLAQKG 1335
Cdd:TIGR01257 2104 QARRMLWNTIvSIIREGRAVVLTSHSMEECEAlCTRLAIMVKGAFQCLGTIQHLKSKFG 2162
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
1122-1305 5.06e-08

The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.


Pssm-ID: 213203 [Multi-domain]  Cd Length: 255  Bit Score: 55.45  E-value: 5.06e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1122 VLQGLSLeVKKGQTLALVGSSGCGKSTVVQLLE--------RFYDPLAGKVLLD---GKEIKRLNVQWLRAHLGI----- 1185
Cdd:cd03236     16 KLHRLPV-PREGQVLGLVGPNGIGKSTALKILAgklkpnlgKFDDPPDWDEILDefrGSELQNYFTKLLEGDVKVivkpq 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1186 -VSQEPILFDCSIAENIAYGDNSRVvsQEEIVRAAKEANIhafiesLPNKYStkvgdkgtQLSGGQKQRIAIARALVRQP 1264
Cdd:cd03236     95 yVDLIPKAVKGKVGELLKKKDERGK--LDELVDQLELRHV------LDRNID--------QLSGGELQRVAIAAALARDA 158
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1149123047 1265 HILLLDEATSALDT----ESEKVVQEAldkAREGRTCIVIAHRLS 1305
Cdd:cd03236    159 DFYFFDEPSSYLDIkqrlNAARLIREL---AEDDNYVLVVEHDLA 200
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
1119-1333 5.63e-08

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 56.95  E-value: 5.63e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1119 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAhlgIVSQE------PIL 1192
Cdd:PRK10938    15 DTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQK---LVSDEwqrnntDML 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1193 fdcSIAENiAYGDNSRVVSQEEIVRAAKEANIHAF--IESL---PNKYstkvgdkgtqLSGGQKQRIAIARALVRQPHIL 1267
Cdd:PRK10938    92 ---SPGED-DTGRTTAEIIQDEVKDPARCEQLAQQfgITALldrRFKY----------LSTGETRKTLLCQALMSEPDLL 157
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1149123047 1268 LLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLLAQ 1333
Cdd:PRK10938   158 ILDEPFDGLDVASRQQLAELLASlHQSGITLVLVLNRFDEIPDfVQFAGVLADCTLAETGEREEILQQ 225
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
472-684 6.01e-08

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 56.84  E-value: 6.01e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  472 PSRKEVKILKG------LNLKVQSGQTVALVGNSGCGKSttvQLMQRLY---DPTEGMVSVDGQdirTINVRFLREII-- 540
Cdd:PRK11288   255 EVRLRLDGLKGpglrepISFSVRAGEIVGLFGLVGAGRS---ELMKLLYgatRRTAGQVYLDGK---PIDIRSPRDAIra 328
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  541 GVV------SQEPVLFATTIAENIRYG--RENVTMDEIEKAVKEA-NAYDFIMKL----PHKfDTLVGergaQLSGGQKQ 607
Cdd:PRK11288   329 GIMlcpedrKAEGIIPVHSVADNINISarRHHLRAGCLINNRWEAeNADRFIRSLniktPSR-EQLIM----NLSGGNQQ 403
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  608 RIAIARALVRNPKILLLDEATSALD--TESEaVVQVALDKARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKGNHDE 684
Cdd:PRK11288   404 KAILGRWLSEDMKVILLDEPTRGIDvgAKHE-IYNVIYELAAQGVAVLFVSSDLPEVLGvADRIVVMREGRIAGELAREQ 482
PRK13543 PRK13543
heme ABC exporter ATP-binding protein CcmA;
473-634 8.11e-08

heme ABC exporter ATP-binding protein CcmA;


Pssm-ID: 184129 [Multi-domain]  Cd Length: 214  Bit Score: 54.47  E-value: 8.11e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  473 SRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTIN-VRFlreiIGVVSQEPVLFA 551
Cdd:PRK13543    20 SRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDrSRF----MAYLGHLPGLKA 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  552 TTIA-ENIRY-----GRENVTMdeiekavkEANAYDfIMKLPHKFDTLVgergAQLSGGQKQRIAIARALVRNPKILLLD 625
Cdd:PRK13543    96 DLSTlENLHFlcglhGRRAKQM--------PGSALA-IVGLAGYEDTLV----RQLSAGQKKRLALARLWLSPAPLWLLD 162

                   ....*....
gi 1149123047  626 EATSALDTE 634
Cdd:PRK13543   163 EPYANLDLE 171
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
1119-1311 8.44e-08

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 56.56  E-value: 8.44e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1119 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLE----RFYdplAGKVLLDGK---------EIKRlnvqwlraHLGI 1185
Cdd:PRK10938   272 DRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITgdhpQGY---SNDLTLFGRrrgsgetiwDIKK--------HIGY 340
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1186 VS-------------QEPIL---FDcSIAENIAYGDNSRVVSQEEIVRAAkeanihafieslpnkYSTKVGDKGTQ-LSG 1248
Cdd:PRK10938   341 VSsslhldyrvstsvRNVILsgfFD-SIGIYQAVSDRQQKLAQQWLDILG---------------IDKRTADAPFHsLSW 404
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1149123047 1249 GQkQRIA-IARALVRQPHILLLDEATSALDTESEKVVQEALDK-AREGRT--------------CivIAHRLSTIQNAD 1311
Cdd:PRK10938   405 GQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVlISEGETqllfvshhaedapaC--ITHRLEFVPDGD 480
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
462-691 8.84e-08

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 56.44  E-value: 8.84e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSvdgqdiRTINVRflreiIG 541
Cdd:PRK15064   320 LEVENLTKGFDNGP---LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVK------WSENAN-----IG 385
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  542 VVSQEPVL-FATTIA---------------ENIR--YGRENVTMDEIEKAVKeanaydfimklphkfdtlvgergaQLSG 603
Cdd:PRK15064   386 YYAQDHAYdFENDLTlfdwmsqwrqegddeQAVRgtLGRLLFSQDDIKKSVK------------------------VLSG 441
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  604 GQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKArKGrTTIVIAH------RLSTvrnaDVIAGFDDGVIV 677
Cdd:PRK15064   442 GEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKY-EG-TLIFVSHdrefvsSLAT----RIIEITPDGVVD 515
                          250
                   ....*....|....
gi 1149123047  678 EKGNHDELMKEKGI 691
Cdd:PRK15064   516 FSGTYEEYLRSQGI 529
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
1116-1277 1.05e-07

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 56.21  E-value: 1.05e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1116 TRPDIPVLQ----------GLSLEVKKGQTLALVGSSGCGKStvvQLLERFY---DPLAGKVLLDGKEIKRLNVQwLRAH 1182
Cdd:PRK15439   262 QAAGAPVLTvedltgegfrNISLEVRAGEILGLAGVVGAGRT---ELAETLYglrPARGGRIMLNGKEINALSTA-QRLA 337
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1183 LGIV-----SQEPILF-DCSIAENI---AYGDNSRvvsqeeIVRAAKEANI-HAFIESLPNKYSTKVGDKGTqLSGGQKQ 1252
Cdd:PRK15439   338 RGLVylpedRQSSGLYlDAPLAWNVcalTHNRRGF------WIKPARENAVlERYRRALNIKFNHAEQAART-LSGGNQQ 410
                          170       180
                   ....*....|....*....|....*
gi 1149123047 1253 RIAIARALVRQPHILLLDEATSALD 1277
Cdd:PRK15439   411 KVLIAKCLEASPQLLIVDEPTRGVD 435
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
453-677 1.17e-07

D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 131681 [Multi-domain]  Cd Length: 500  Bit Score: 55.99  E-value: 1.17e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  453 HKPDNIKGN-LEFRNVHFSYPSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPT-EGMVSVDGQ--DI 528
Cdd:TIGR02633  248 HEPHEIGDViLEARNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKpvDI 327
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  529 RT---------INVRFLREIIGVVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPHKFDTLvgergA 599
Cdd:TIGR02633  328 RNpaqairagiAMVPEDRKRHGIVPILGVGKNITLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLPI-----G 402
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1149123047  600 QLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEA-VVQVALDKARKGRTTIVIAHRLSTVrnadviAGFDDGVIV 677
Cdd:TIGR02633  403 RLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYeIYKLINQLAQEGVAIIVVSSELAEV------LGLSDRVLV 475
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
1108-1289 1.19e-07

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 56.11  E-value: 1.19e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1108 GEVVF-----NYpTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKeikrLNVQWL--- 1179
Cdd:PRK11147   316 GKIVFemenvNY-QIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTK----LEVAYFdqh 390
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1180 RAHLgivsqEPilfDCSIAENIAYGdnsrvvSQEEIVRAAKEaniHA------FIESlPNKYSTKVgdkgTQLSGGQKQR 1253
Cdd:PRK11147   391 RAEL-----DP---EKTVMDNLAEG------KQEVMVNGRPR---HVlgylqdFLFH-PKRAMTPV----KALSGGERNR 448
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1149123047 1254 IAIARALVRQPHILLLDEATSALDTESEKVVQEALD 1289
Cdd:PRK11147   449 LLLARLFLKPSNLLILDEPTNDLDVETLELLEELLD 484
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
1123-1326 1.38e-07

The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.


Pssm-ID: 213204 [Multi-domain]  Cd Length: 246  Bit Score: 54.34  E-value: 1.38e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1123 LQGLSLEVKKG-----QTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKrLNVQWLRAHL-GIVSQepILFDCS 1196
Cdd:cd03237     10 LGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS-YKPQYIKADYeGTVRD--LLSSIT 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1197 iaeNIAYGDNSrvvSQEEIVRAAKeanihafIESLpnkYSTKVgdkgTQLSGGQKQRIAIARALVRQPHILLLDEATSAL 1276
Cdd:cd03237     87 ---KDFYTHPY---FKTEIAKPLQ-------IEQI---LDREV----PELSGGELQRVAIAACLSKDADIYLLDEPSAYL 146
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1149123047 1277 DTESE----KVVQEALDKARegRTCIVIAHRLSTIQN-ADLIVVFQnGRVKEHGT 1326
Cdd:cd03237    147 DVEQRlmasKVIRRFAENNE--KTAFVVEHDIIMIDYlADRLIVFE-GEPSVNGV 198
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
1105-1326 1.41e-07

Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 55.95  E-value: 1.41e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1105 VTFGEVVFNYPtrpDIPV-LQGLSLEV-----KKGQTLALVGSSGCGKSTVVQLLerfydplAGKVLLDGKEI-KRLNV- 1176
Cdd:COG1245    335 EKEEETLVEYP---DLTKsYGGFSLEVeggeiREGEVLGIVGPNGIGKTTFAKIL-------AGVLKPDEGEVdEDLKIs 404
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1177 ---QWLRAHLGIVSQEpILFDcSIAENIaygDNSRVvsQEEIVRAAKeanihafIESLPNKYstkVGDkgtqLSGGQKQR 1253
Cdd:COG1245    405 ykpQYISPDYDGTVEE-FLRS-ANTDDF---GSSYY--KTEIIKPLG-------LEKLLDKN---VKD----LSGGELQR 463
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1149123047 1254 IAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGR--TCIVIAHRLSTIQN-ADLIVVFqNGRVKEHGT 1326
Cdd:COG1245    464 VAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRgkTAMVVDHDIYLIDYiSDRLMVF-EGEPGVHGH 538
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
558-685 1.67e-07

excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273184 [Multi-domain]  Cd Length: 925  Bit Score: 56.17  E-value: 1.67e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  558 IRYGRENVTmDEIEKAVKEAnaYDFIMKLP---HKFDTLV---------GERGAQLSGGQKQRIAIARALVR---NPKIL 622
Cdd:TIGR00630  778 VKYKGKNIA-DVLDMTVEEA--YEFFEAVPsisRKLQTLCdvglgyirlGQPATTLSGGEAQRIKLAKELSKrstGRTLY 854
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1149123047  623 LLDEATSALDTESEA----VVQVALDKarkGRTTIVIAHRLSTVRNADVI------AGFDDGVIVEKGNHDEL 685
Cdd:TIGR00630  855 ILDEPTTGLHFDDIKklleVLQRLVDK---GNTVVVIEHNLDVIKTADYIidlgpeGGDGGGTVVASGTPEEV 924
PLN03073 PLN03073
ABC transporter F family; Provisional
1105-1328 2.35e-07

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 55.25  E-value: 2.35e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1105 VTFGEVVFNYPTRPDIpvLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKeiKRLNVqWLRAHL- 1183
Cdd:PLN03073   509 ISFSDASFGYPGGPLL--FKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAK--VRMAV-FSQHHVd 583
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1184 GI-VSQEPILFdcsiaeniaygdnsrvvsQEEIVRAAKEANIHAFIESLPNKYSTKVGDKGTqLSGGQKQRIAIARALVR 1262
Cdd:PLN03073   584 GLdLSSNPLLY------------------MMRCFPGVPEQKLRAHLGSFGVTGNLALQPMYT-LSGGQKSRVAFAKITFK 644
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1149123047 1263 QPHILLLDEATSALDTESEKVVQEALDKAREGrtCIVIAHRLSTIQNA-DLIVVFQNGRVKE-HGTHQ 1328
Cdd:PLN03073   645 KPHILLLDEPSNHLDLDAVEALIQGLVLFQGG--VLMVSHDEHLISGSvDELWVVSEGKVTPfHGTFH 710
ABC_6TM_exporter_like cd18540
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
778-940 2.40e-07

Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349984 [Multi-domain]  Cd Length: 295  Bit Score: 54.02  E-value: 2.40e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  778 WPYFVVGVFCAIINGGLQPAFAIIFSKIIGVFTRIDDPETKrqnsNLFSLLFLALGIISFITFFLQGFTFGKAGEILTKR 857
Cdd:cd18540      1 KKLLILLIILMLLVALLDAVFPLLTKYAIDHFITPGTLDGL----TGFILLYLGLILIQALSVFLFIRLAGKIEMGVSYD 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  858 LRYMVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIGSRLAVITQNIANLGTGIIISFIYGWQLTLLLLAIVPI 937
Cdd:cd18540     77 LRKKAFEHLQTLSFSYFD--KTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVPV 154

                   ...
gi 1149123047  938 IAI 940
Cdd:cd18540    155 LAV 157
ABC_6TM_YknV_like cd18545
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ...
823-940 2.51e-07

Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349989 [Multi-domain]  Cd Length: 293  Bit Score: 54.01  E-value: 2.51e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  823 NLFSLLFLALGIISFITFFLQGFTFGKAGEILTKRLRYMVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVKGAIGSR 902
Cdd:cd18545     40 LIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFD--SRPVGKILSRVINDVNSLSDLLSNG 117
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1149123047  903 LAVITQNIANLGTGIIISFIYGWQLTLLLLAIVPIIAI 940
Cdd:cd18545    118 LINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVL 155
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
1121-1336 2.61e-07

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 54.90  E-value: 2.61e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1121 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLerfydplAGKVLLDGKEIKrlnvqWL-RAHLGIVSQEP--------I 1191
Cdd:PRK15064   333 PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTL-------VGELEPDSGTVK-----WSeNANIGYYAQDHaydfendlT 400
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1192 LFDCsIAENIAYGDNSRVV---------SQEEIvraakeanihafieslpnKYSTKVgdkgtqLSGGQKQRIAIARALVR 1262
Cdd:PRK15064   401 LFDW-MSQWRQEGDDEQAVrgtlgrllfSQDDI------------------KKSVKV------LSGGEKGRMLFGKLMMQ 455
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1263 QPHILLLDEATSALDTESEKVVQEALDKArEGrTCIVIAH------RLSTiqnaDLIVVFQNGRVKEHGTHQQLLAQKGI 1336
Cdd:PRK15064   456 KPNVLVMDEPTNHMDMESIESLNMALEKY-EG-TLIFVSHdrefvsSLAT----RIIEITPDGVVDFSGTYEEYLRSQGI 529
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
1244-1280 3.39e-07

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 54.74  E-value: 3.39e-07
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1149123047 1244 TQLSGGQKQRIAIARALVRQPHILLLDEATSALDTES 1280
Cdd:PRK11819   162 TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
1121-1332 3.41e-07

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 54.62  E-value: 3.41e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1121 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAHlGIV------SQEPILFD 1194
Cdd:PRK10762   266 PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLAN-GIVyisedrKRDGLVLG 344
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1195 CSIAENI---AYGDNSRVVSQeeIVRAAKEANIHAFIESLPNKYSTKVGDKGtQLSGGQKQRIAIARALVRQPHILLLDE 1271
Cdd:PRK10762   345 MSVKENMsltALRYFSRAGGS--LKHADEQQAVSDFIRLFNIKTPSMEQAIG-LLSGGNQQKVAIARGLMTRPKVLILDE 421
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1149123047 1272 ATSALDTESEKVVQEALDKAR-EGRTCIVIAHRLSTIQN-ADLIVVFQNGRV-----KEHGTHQQLLA 1332
Cdd:PRK10762   422 PTRGVDVGAKKEIYQLINQFKaEGLSIILVSSEMPEVLGmSDRILVMHEGRIsgeftREQATQEKLMA 489
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
1122-1288 4.46e-07

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 54.41  E-value: 4.46e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1122 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLdGKEIKrlnvqwlrahLGIVSQEPILF---DCSIA 1198
Cdd:PRK10636   327 ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL-AKGIK----------LGYFAQHQLEFlraDESPL 395
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1199 ENIAygdnsRVVSQEeivraaKEANIHAFIESLPNKySTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDT 1278
Cdd:PRK10636   396 QHLA-----RLAPQE------LEQKLRDYLGGFGFQ-GDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDL 463
                          170
                   ....*....|
gi 1149123047 1279 ESEKVVQEAL 1288
Cdd:PRK10636   464 DMRQALTEAL 473
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
1115-1333 5.19e-07

ABC-type uncharacterized transport system, ATPase component [General function prediction only];


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 53.17  E-value: 5.19e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1115 PTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRaHLGIV----SQep 1190
Cdd:COG4586     30 REYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFAR-RIGVVfgqrSQ-- 106
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1191 ILFDCSIAENIA-----YGdnsrvVSQEEIvraakEANIHAFIESLpnkystKVGDKGT----QLSGGQKQRIAIARALV 1261
Cdd:COG4586    107 LWWDLPAIDSFRllkaiYR-----IPDAEY-----KKRLDELVELL------DLGELLDtpvrQLSLGQRMRCELAAALL 170
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1149123047 1262 RQPHILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLLAQ 1333
Cdd:COG4586    171 HRPKILFLDEPTIGLDVVSKEAIREFLKEynRERGTTILLTSHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKER 245
PLN03073 PLN03073
ABC transporter F family; Provisional
455-640 5.59e-07

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 54.10  E-value: 5.59e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  455 PDNIKGN--LEFRNVHFSYPSRKevKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVsvdgqdIRTIN 532
Cdd:PLN03073   500 PDDRPGPpiISFSDASFGYPGGP--LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV------FRSAK 571
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  533 VRflreiIGVVSQEPVLFATTIAENIRYgrenvtMDEIEKAVKEanaydfiMKLPHKFDT--LVGERGAQ----LSGGQK 606
Cdd:PLN03073   572 VR-----MAVFSQHHVDGLDLSSNPLLY------MMRCFPGVPE-------QKLRAHLGSfgVTGNLALQpmytLSGGQK 633
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1149123047  607 QRIAIARALVRNPKILLLDEATSALDTES-EAVVQ 640
Cdd:PLN03073   634 SRVAFAKITFKKPHILLLDEPSNHLDLDAvEALIQ 668
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
497-632 6.21e-07

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 53.98  E-value: 6.21e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  497 GNSGCGKSTTVQLMQRLYDPTEGMV-----SVDGQDIRTinvrflREIIGVVSQEPVLfattiaenirYG----REN--- 564
Cdd:NF033858   299 GSNGCGKSTTMKMLTGLLPASEGEAwlfgqPVDAGDIAT------RRRVGYMSQAFSL----------YGeltvRQNlel 362
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1149123047  565 ------VTMDEIEKAVKEanaydfimkLPHKFD--TLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALD 632
Cdd:NF033858   363 harlfhLPAAEIAARVAE---------MLERFDlaDVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
1238-1314 6.96e-07

excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273184 [Multi-domain]  Cd Length: 925  Bit Score: 53.86  E-value: 6.96e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1238 KVGDKGTQLSGGQKQRIAIARALVRQ---PHILLLDEATSALDTESEK----VVQEALDKareGRTCIVIAHRLSTIQNA 1310
Cdd:TIGR00630  822 RLGQPATTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKklleVLQRLVDK---GNTVVVIEHNLDVIKTA 898

                   ....
gi 1149123047 1311 DLIV 1314
Cdd:TIGR00630  899 DYII 902
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
1244-1280 7.80e-07

ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.


Pssm-ID: 274744 [Multi-domain]  Cd Length: 552  Bit Score: 53.40  E-value: 7.80e-07
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1149123047 1244 TQLSGGQKQRIAIARALVRQPHILLLDEATSALDTES 1280
Cdd:TIGR03719  160 TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES 196
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
1245-1316 1.47e-06

Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 52.48  E-value: 1.47e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1149123047 1245 QLSGGQKQRIAIARALVRQPHILLLDEATSALD----TESEKVVQEAldkAREGRTCIVIAHRLSTIQN-ADLIVVF 1316
Cdd:COG1245    212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLDiyqrLNVARLIREL---AEEGKYVLVVEHDLAILDYlADYVHIL 285
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
600-661 1.95e-06

Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 52.09  E-value: 1.95e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1149123047  600 QLSGGQKQRIAIARALVRNPKILLLDEATSALD-TESEAVVQVALDKARKGRTTIVIAHRLST 661
Cdd:COG1245    212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLDiYQRLNVARLIRELAEEGKYVLVVEHDLAI 274
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
1130-1302 2.16e-06

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 52.09  E-value: 2.16e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1130 VKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGkeikrlnvQWlraHLGIVSQEPILFDCSIAENIAYGDnsRV 1209
Cdd:PRK10636    24 INPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPG--------NW---QLAWVNQETPALPQPALEYVIDGD--RE 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1210 VSQ-EEIVRAAKEAN--------------IHAF-IESLPNKYSTKVGDKGTQL-------SGGQKQRIAIARALVRQPHI 1266
Cdd:PRK10636    91 YRQlEAQLHDANERNdghaiatihgkldaIDAWtIRSRAASLLHGLGFSNEQLerpvsdfSGGWRMRLNLAQALICRSDL 170
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1149123047 1267 LLLDEATSALDTESEKVVQEALdKAREGrTCIVIAH 1302
Cdd:PRK10636   171 LLLDEPTNHLDLDAVIWLEKWL-KSYQG-TLILISH 204
ABC_6TM_T1SS_like cd18779
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ...
287-413 2.32e-06

uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.


Pssm-ID: 350052 [Multi-domain]  Cd Length: 294  Bit Score: 51.01  E-value: 2.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  287 VILAISP-----VLGLSAAVWAKILSSF------TDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAK 355
Cdd:cd18779    135 LLFAQSPllglvVLGLAALQVALLLATRrrvrelMARELAAQAEAQSYLVEALSGIETLKASGAEDRALDRWSNLFVDQL 214
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1149123047  356 RIGIKKAITANISIGAAFLLIYASYALAFWYGTTLVLSGEYSIGQVLTvfFSVLIGAF 413
Cdd:cd18779    215 NASLRRGRLDALVDALLATLRLAAPLVLLWVGAWQVLDGQLSLGTMLA--LNALAGAF 270
ABC_6TM_VMR1_D2_like cd18604
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ...
178-301 3.12e-06

Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.


Pssm-ID: 350048 [Multi-domain]  Cd Length: 297  Bit Score: 50.54  E-value: 3.12e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  178 EEDMTRYAYYYSGIGAGVLVAAYIQVSFWC---LAAGRQIHKirkQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINE 254
Cdd:cd18604     39 EVSVLYYLGIYALISLLSVLLGTLRYLLFFfgsLRASRKLHE---RLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDS 115
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1149123047  255 GIGDKIGMFFQSMATFFTGFIvgftrgwkltlVILAISPVLGLSAAV 301
Cdd:cd18604    116 ELADSLSSLLESTLSLLVILI-----------AIVVVSPAFLLPAVV 151
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
1115-1277 4.01e-06

First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213200 [Multi-domain]  Cd Length: 202  Bit Score: 49.18  E-value: 4.01e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1115 PTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKST----VVQLLERFYDPlAGKVLLDGKEIKRLNVQWlRAHLGIVSQEp 1190
Cdd:cd03233     15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTllkaLANRTEGNVSV-EGDIHYNGIPYKEFAEKY-PGEIIYVSEE- 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1191 ilfDCSIAEniaygdnsrvVSQEEIVRAAKEANIHAFIeslpnkystkvgdKGtqLSGGQKQRIAIARALVRQPHILLLD 1270
Cdd:cd03233     92 ---DVHFPT----------LTVRETLDFALRCKGNEFV-------------RG--ISGGERKRVSIAEALVSRASVLCWD 143

                   ....*..
gi 1149123047 1271 EATSALD 1277
Cdd:cd03233    144 NSTRGLD 150
PLN03073 PLN03073
ABC transporter F family; Provisional
490-736 4.06e-06

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 51.40  E-value: 4.06e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  490 GQTVALVGNSGCGKSTTVQLM------------QRLY-------DPTEGMVSVDGQDIRtiNVRFLREIIGVVSQEPVLF 550
Cdd:PLN03073   203 GRHYGLVGRNGTGKTTFLRYMamhaidgipkncQILHveqevvgDDTTALQCVLNTDIE--RTQLLEEEAQLVAQQRELE 280
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  551 ATTIAENIRyGRENVTMD---------EIEKAVKEANAY-------------DFIMKLPHKfdtlvgeRGAQLSGGQKQR 608
Cdd:PLN03073   281 FETETGKGK-GANKDGVDkdavsqrleEIYKRLELIDAYtaearaasilaglSFTPEMQVK-------ATKTFSGGWRMR 352
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  609 IAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARKgrTTIVIAHR---LSTVRnADVIAGFDDGVIVEKGNHDEl 685
Cdd:PLN03073   353 IALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPK--TFIVVSHArefLNTVV-TDILHLHGQKLVTYKGDYDT- 428
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1149123047  686 mkekgiyFKLVTMQTAGNEVELENAADESKSEIDAL--EMSSNDSRSSLIRKR 736
Cdd:PLN03073   429 -------FERTREEQLKNQQKAFESNERSRSHMQAFidKFRYNAKRASLVQSR 474
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
558-668 4.27e-06

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 51.75  E-value: 4.27e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  558 IRYGRENVTmDEIEKAVKEANayDFIMKLPH---KFDTL---------VGERGAQLSGGQKQRIAIARAL---VRNPKIL 622
Cdd:PRK00635   758 VRYKGKNIA-DILEMTAYEAE--KFFLDEPSiheKIHALcslgldylpLGRPLSSLSGGEIQRLKLAYELlapSKKPTLY 834
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1149123047  623 LLDEATSALDTES-EAVVQVALDKARKGRTTIVIAHRLSTVRNADVI 668
Cdd:PRK00635   835 VLDEPTTGLHTHDiKALIYVLQSLTHQGHTVVIIEHNMHVVKVADYV 881
PRK13546 PRK13546
teichoic acids export ABC transporter ATP-binding subunit TagH;
480-715 4.92e-06

teichoic acids export ABC transporter ATP-binding subunit TagH;


Pssm-ID: 184131 [Multi-domain]  Cd Length: 264  Bit Score: 49.81  E-value: 4.92e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  480 LKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQ-DIRTINVRFLREIIGVvsqepvlfattiaENI 558
Cdd:PRK13546    40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEvSVIAISAGLSGQLTGI-------------ENI 106
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  559 RYGR--ENVTMDEIEKAVKEANAY----DFIMKLPHKFdtlvgergaqlSGGQKQRIAIARALVRNPKILLLDEATSALD 632
Cdd:PRK13546   107 EFKMlcMGFKRKEIKAMTPKIIEFselgEFIYQPVKKY-----------SSGMRAKLGFSINITVNPDILVIDEALSVGD 175
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  633 tesEAVVQVALDK----ARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKGNHDELMKEKGIYFKLVTMQTAGNEVEL 707
Cdd:PRK13546   176 ---QTFAQKCLDKiyefKEQNKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYGELDDVLPKYEAFLNDFKKKSKAEQKEF 252

                   ....*...
gi 1149123047  708 ENAADESK 715
Cdd:PRK13546   253 RNKLDESR 260
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
1246-1316 5.55e-06

ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.


Pssm-ID: 213205 [Multi-domain]  Cd Length: 176  Bit Score: 48.09  E-value: 5.55e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1149123047 1246 LSGGQKQRIAIARALVRQPH--ILLLDEATSALDTESEKVVQEALDKAR-EGRTCIVIAHRLSTIQNADLIVVF 1316
Cdd:cd03238     88 LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIdLGNTVILIEHNLDVLSSADWIIDF 161
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
477-657 6.28e-06

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 50.58  E-value: 6.28e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  477 VKILKGLNLKVQSGQ-----TVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDgqdirtINVRFLREIIGVVSQEPV-LF 550
Cdd:PRK13409   347 TKKLGDFSLEVEGGEiyegeVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE------LKISYKPQYIKPDYDGTVeDL 420
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  551 ATTIAENIRygrENVTMDEIEKAvkeanaydfiMKLPHKFDTLVGErgaqLSGGQKQRIAIARALVRNPKILLLDEATSA 630
Cdd:PRK13409   421 LRSITDDLG---SSYYKSEIIKP----------LQLERLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAH 483
                          170       180
                   ....*....|....*....|....*....
gi 1149123047  631 LDTESEAVVQVALDK--ARKGRTTIVIAH 657
Cdd:PRK13409   484 LDVEQRLAVAKAIRRiaEEREATALVVDH 512
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
462-632 6.37e-06

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 50.31  E-value: 6.37e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYPSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYD-PTEGMVSVDGQDIRTINVR-FLREI 539
Cdd:PRK13549   260 LEVRNLTAWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIRNPQqAIAQG 339
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  540 IGVVSQE-------PVLfatTIAENI------RYGRENVtmdeIEKAVKEANAYDFIMKLPHKFDTLVgERGAQLSGGQK 606
Cdd:PRK13549   340 IAMVPEDrkrdgivPVM---GVGKNItlaaldRFTGGSR----IDDAAELKTILESIQRLKVKTASPE-LAIARLSGGNQ 411
                          170       180
                   ....*....|....*....|....*.
gi 1149123047  607 QRIAIARALVRNPKILLLDEATSALD 632
Cdd:PRK13549   412 QKAVLAKCLLLNPKILILDEPTRGID 437
ABC_6TM_YwjA_like cd18549
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ...
781-1048 6.44e-06

Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar proteins; This group represents the six-transmembrane helical domain of an uncharacterized ABC transporter YwjA from Bacillus subtilis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349993 [Multi-domain]  Cd Length: 295  Bit Score: 49.76  E-value: 6.44e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  781 FVVGVFCAIINGGLQPAFAIIFSKIIGVFTriddPEtkrQNSNLFSLLFLALGIISFITFFLQgFTFGKAGEILTKR--- 857
Cdd:cd18549      4 FFLDLFCAVLIAALDLVFPLIVRYIIDDLL----PS---KNLRLILIIGAILLALYILRTLLN-YFVTYWGHVMGARiet 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  858 -LRYMVFRSMLRQDVSWFDdpKNTTGALTTRLANDAAQVkgaigSRLA-------VITqnIANLGTGIIISFIYGWQLTL 929
Cdd:cd18549     76 dMRRDLFEHLQKLSFSFFD--NNKTGQLMSRITNDLFDI-----SELAhhgpedlFIS--IITIIGSFIILLTINVPLTL 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  930 LLLAIVPIIAIAGVVEMKMLSGQALKDKKELegsGKIATEAIENF---RTVVSLTQE----QKFE---HMYAQSLQVPYR 999
Cdd:cd18549    147 IVFALLPLMIIFTIYFNKKMKKAFRRVREKI---GEINAQLEDSLsgiRVVKAFANEeyeiEKFDegnDRFLESKKKAYK 223
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1149123047 1000 NSlrkAHIFGITFSFTQaMMYFSYAGcfrFGAYLVAHKLMSFEDvLLVF 1048
Cdd:cd18549    224 AM---AYFFSGMNFFTN-LLNLVVLV---AGGYFIIKGEITLGD-LVAF 264
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
487-657 6.44e-06

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 50.55  E-value: 6.44e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  487 VQSGQTVALVGNSGCGKSTTVQLMQrlydpteGMVSVDGQDIRTINVRFLreiiGVVSQE-PVLFATTIAENIRYGREnv 565
Cdd:PRK10636    24 INPGQKVGLVGKNGCGKSTLLALLK-------NEISADGGSYTFPGNWQL----AWVNQEtPALPQPALEYVIDGDRE-- 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  566 tMDEIEKAVKEANAYD---FIMKLPHKFDTL----VGERGAQL------------------SGGQKQRIAIARALVRNPK 620
Cdd:PRK10636    91 -YRQLEAQLHDANERNdghAIATIHGKLDAIdawtIRSRAASLlhglgfsneqlerpvsdfSGGWRMRLNLAQALICRSD 169
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1149123047  621 ILLLDEATSALDTesEAVVQvaLDKARKGR--TTIVIAH 657
Cdd:PRK10636   170 LLLLDEPTNHLDL--DAVIW--LEKWLKSYqgTLILISH 204
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
1130-1315 6.49e-06

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 50.58  E-value: 6.49e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1130 VKKGQTLALVGSSGCGKSTVVQLL---------------------ERFydplAGKVLLDgkEIKRLNVQWLRAHLGI--V 1186
Cdd:PRK13409    96 PKEGKVTGILGPNGIGKTTAVKILsgelipnlgdyeeepswdevlKRF----RGTELQN--YFKKLYNGEIKVVHKPqyV 169
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1187 SQEPILFDCSIAENIAYGDNSRVVsqEEIVraaKEANIhafieslpnkysTKVGDKG-TQLSGGQKQRIAIARALVRQPH 1265
Cdd:PRK13409   170 DLIPKVFKGKVRELLKKVDERGKL--DEVV---ERLGL------------ENILDRDiSELSGGELQRVAIAAALLRDAD 232
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1149123047 1266 ILLLDEATSALDtesekvVQEALDKAR------EGRTCIVIAHRLSTIQN-ADLIVV 1315
Cdd:PRK13409   233 FYFFDEPTSYLD------IRQRLNVARlirelaEGKYVLVVEHDLAVLDYlADNVHI 283
ABC_6TM_PrtD_LapB_HlyB_like cd18566
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ...
215-400 8.34e-06

Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.


Pssm-ID: 350010 [Multi-domain]  Cd Length: 294  Bit Score: 49.12  E-value: 8.34e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  215 HKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDdVSKINEgigdkigmFF--QSMATF------FTGFIVGFTRGWKLTL 286
Cdd:cd18566     75 HRLSNAAFEHLLSLPLSFFEREPSGAHLERLNS-LEQIRE--------FLtgQALLALldlpfvLIFLGLIWYLGGKLVL 145
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  287 VILAISPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKRIGIKKAITAN 366
Cdd:cd18566    146 VPLVLLGLFVLVAILLGPILRRALKERSRADERRQNFLIETLTGIHTIKAMAMEPQMLRRYERLQANAAYAGFKVAKINA 225
                          170       180       190
                   ....*....|....*....|....*....|....
gi 1149123047  367 ISIGAAFLLIYASYALAFWYGTTLVLSGEYSIGQ 400
Cdd:cd18566    226 VAQTLGQLFSQVSMVAVVAFGALLVINGDLTVGA 259
PRK13541 PRK13541
cytochrome c biogenesis protein CcmA; Provisional
1140-1313 8.89e-06

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184128 [Multi-domain]  Cd Length: 195  Bit Score: 47.94  E-value: 8.89e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1140 GSSGCGKSTVVQLLERFYDPLAGKVLLDGKEIKRLNVQWLRAhlgIVSQEPILFDCSIAENIAYGdnSRVVSQEEIVRAA 1219
Cdd:PRK13541    33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTY---IGHNLGLKLEMTVFENLKFW--SEIYNSAETLYAA 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1220 keanIHAFieslpnKYSTKVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALD-KAREGRTCI 1298
Cdd:PRK13541   108 ----IHYF------KLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVmKANSGGIVL 177
                          170
                   ....*....|....*
gi 1149123047 1299 VIAHRLSTIQNADLI 1313
Cdd:PRK13541   178 LSSHLESSIKSAQIL 192
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
474-632 1.02e-05

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 49.62  E-value: 1.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  474 RKEVKILKG-----LNLKVQSGQTVALVGNSGCGKSttvQLMQRLYDP---TEGMVSVDGQDIRTINVR-FLREIIGVVS 544
Cdd:PRK10762   257 RLKVDNLSGpgvndVSFTLRKGEILGVSGLMGAGRT---ELMKVLYGAlprTSGYVTLDGHEVVTRSPQdGLANGIVYIS 333
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  545 QEP----VLFATTIAEN---------------IRYGRENVTMDeiekavkeanayDFIM----KLPHKfDTLVGErgaqL 601
Cdd:PRK10762   334 EDRkrdgLVLGMSVKENmsltalryfsraggsLKHADEQQAVS------------DFIRlfniKTPSM-EQAIGL----L 396
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1149123047  602 SGGQKQRIAIARALVRNPKILLLDEATSALD 632
Cdd:PRK10762   397 SGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
476-690 1.07e-05

oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 49.35  E-value: 1.07e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  476 EVKILKGLNLKVQSGQTVALVGNSGCGKSTTVqLMQRLYDPTEGMvsvdgQDIR----TINVRFLREIIGVvsQEPVLFA 551
Cdd:NF000106    25 EVKAVDGVDLDVREGTVLGVLGP*GAA**RGA-LPAHV*GPDAGR-----RPWRf*twCANRRALRRTIG*--HRPVR*G 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  552 TTIAENiryGRENVTM--DEIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATS 629
Cdd:NF000106    97 RRESFS---GRENLYMigR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTT 173
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1149123047  630 ALD--TESEAVVQVAlDKARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKGNHDELMKEKG 690
Cdd:NF000106   174 GLDprTRNEVWDEVR-SMVRDGATVLLTTQYMEEAEQlAHELTVIDRGRVIADGKVDELKTKVG 236
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
1119-1306 1.29e-05

ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.


Pssm-ID: 274744 [Multi-domain]  Cd Length: 552  Bit Score: 49.55  E-value: 1.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1119 DIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLdGKEIKRLNVQWLRAHLgivsqEPilfDCSIA 1198
Cdd:TIGR03719  334 DKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVKLAYVDQSRDAL-----DP---NKTVW 404
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1199 ENIAYGdnsrvvsQEEIVRAAKEANIHAFIESLPNKYS---TKVGdkgtQLSGGQKQRIAIARALVRQPHILLLDEATSA 1275
Cdd:TIGR03719  405 EEISGG-------LDIIKLGKREIPSRAYVGRFNFKGSdqqKKVG----QLSGGERNRVHLAKTLKSGGNVLLLDEPTND 473
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1149123047 1276 LDTESEKVVQEALDKAreGRTCIVIAH------RLST 1306
Cdd:TIGR03719  474 LDVETLRALEEALLNF--AGCAVVISHdrwfldRIAT 508
PRK13541 PRK13541
cytochrome c biogenesis protein CcmA; Provisional
462-668 1.63e-05

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184128 [Multi-domain]  Cd Length: 195  Bit Score: 47.17  E-value: 1.63e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  462 LEFRNVHFSYpsrkEVKILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTInvrflreiig 541
Cdd:PRK13541     2 LSLHQLQFNI----EQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNI---------- 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  542 vvsQEPvlFATTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPH--KFDTLVGERGAQLSGGQKQRIAIARALVRNP 619
Cdd:PRK13541    68 ---AKP--YCTYIGHNLGLKLEMTVFENLKFWSEIYNSAETLYAAIHyfKLHDLLDEKCYSLSSGMQKIVAIARLIACQS 142
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1149123047  620 KILLLDEATSALDTESEAVV-QVALDKARKGRTTIVIAHRLSTVRNADVI 668
Cdd:PRK13541   143 DLWLLDEVETNLSKENRDLLnNLIVMKANSGGIVLLSSHLESSIKSAQIL 192
GguA NF040905
sugar ABC transporter ATP-binding protein;
1104-1300 1.76e-05

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 49.02  E-value: 1.76e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1104 NVTFGEVVF-------NYPTRPDIPVLQGLSLEVKKGQTLALVGSSGCGKS-TVVQLLERFYDP-LAGKVLLDGKEIKRL 1174
Cdd:NF040905   250 TPKIGEVVFevknwtvYHPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTeLAMSVFGRSYGRnISGTVFKDGKEVDVS 329
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1175 NVQWL-----------RAHLGIVSQEPILFDCSIA--ENIAygdNSRVVSQEEIVRAAKEanihaFIESLPNKYSTkVGD 1241
Cdd:NF040905   330 TVSDAidaglayvtedRKGYGLNLIDDIKRNITLAnlGKVS---RRGVIDENEEIKVAEE-----YRKKMNIKTPS-VFQ 400
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1149123047 1242 KGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDT----ESEKVVQEAldkAREGRTCIVI 1300
Cdd:NF040905   401 KVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVgakyEIYTIINEL---AAEGKGVIVI 460
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
465-657 1.97e-05

Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 49.01  E-value: 1.97e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  465 RNVHFSYPSRkeVKILKGLNLKVQSGQ-----TVALVGNSGCGKSTTVQLMQRLYDPTEGmvSVDG--------QDIRT- 530
Cdd:COG1245    338 EETLVEYPDL--TKSYGGFSLEVEGGEiregeVLGIVGPNGIGKTTFAKILAGVLKPDEG--EVDEdlkisykpQYISPd 413
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  531 --INVR-FLREIIGVVsqepvlFATTIAENirygrenvtmdEIEKAvkeanaydfiMKLPHKFDTLVGErgaqLSGGQKQ 607
Cdd:COG1245    414 ydGTVEeFLRSANTDD------FGSSYYKT-----------EIIKP----------LGLEKLLDKNVKD----LSGGELQ 462
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1149123047  608 RIAIARALVRNPKILLLDEATSALDTESEAVVQVALDK-AR-KGRTTIVIAH 657
Cdd:COG1245    463 RVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRfAEnRGKTAMVVDH 514
ABC_6TM_YOR1_D2_like cd18606
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ...
828-940 2.09e-05

Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.


Pssm-ID: 350050 [Multi-domain]  Cd Length: 290  Bit Score: 47.85  E-value: 2.09e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  828 LFLALGIISFITFFLQGFTFGKAGEILTKRLRYMVFRSMLRQDVSWFDdpknTT--GALTTRLANDAAQVKGAIGSRLAV 905
Cdd:cd18606     40 IYAGLGVLQAIFLFLFGLLLAYLGIRASKRLHNKALKRVLRAPMSFFD----TTplGRILNRFSKDTDVLDNELPDSLRM 115
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1149123047  906 ITQNIANLGTGIIISFIYgwqLTLLLLAIVPIIAI 940
Cdd:cd18606    116 FLYTLSSIIGTFILIIIY---LPWFAIALPPLLVL 147
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
1246-1317 2.16e-05

ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.


Pssm-ID: 213189 [Multi-domain]  Cd Length: 177  Bit Score: 46.41  E-value: 2.16e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1149123047 1246 LSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVFQ 1317
Cdd:cd03222     72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEegKKTALVVEHDLAVLDYlSDRIHVFE 146
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
487-659 3.46e-05

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 48.27  E-value: 3.46e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  487 VQSGQTVALVGNSGCGKSTTV-----QLMQRLYDPTEGmVSVDgqdirtinvRFLREIIGVVSQEpvLFATTIAENIRYG 561
Cdd:PRK13409    96 PKEGKVTGILGPNGIGKTTAVkilsgELIPNLGDYEEE-PSWD---------EVLKRFRGTELQN--YFKKLYNGEIKVV 163
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  562 RENVTMDEIEKAVKeANAYDFIMKLPH--KFDTLVGERG---------AQLSGGQKQRIAIARALVRNPKILLLDEATSA 630
Cdd:PRK13409   164 HKPQYVDLIPKVFK-GKVRELLKKVDErgKLDEVVERLGlenildrdiSELSGGELQRVAIAAALLRDADFYFFDEPTSY 242
                          170       180
                   ....*....|....*....|....*....
gi 1149123047  631 LDTESEAVVQVALDKARKGRTTIVIAHRL 659
Cdd:PRK13409   243 LDIRQRLNVARLIRELAEGKYVLVVEHDL 271
ABC_6TM_AarD_CydDC_like cd18561
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ...
239-406 4.09e-05

Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and similar proteins; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).


Pssm-ID: 350005 [Multi-domain]  Cd Length: 289  Bit Score: 46.89  E-value: 4.09e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  239 GELNTRLTDDVSKINEGIGDKIGMFFQSMATFFTGFIVGFTRGWKLTLVILAISPVLGLSAAVWAKILSSFTDKELLAYA 318
Cdd:cd18561     93 GELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVALILLVFALLIPLSPALWDRLAKDTGRRHWAAYG 172
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  319 KAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKRIGIKKAITANISIGAAFLLIYASYALAFWYGTTLVLSGEYSI 398
Cdd:cd18561    173 RLSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLRQATMKVLAVSLLSSGIMGLATALGTALALGVGALRVLGGQLTL 252

                   ....*...
gi 1149123047  399 GQVLTVFF 406
Cdd:cd18561    253 SSLLLILF 260
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
600-671 4.59e-05

ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.


Pssm-ID: 213194 [Multi-domain]  Cd Length: 162  Bit Score: 45.04  E-value: 4.59e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1149123047  600 QLSGGQKQRIAIARAL----VRNPKILLLDEATSALDTES-EAVVQVALDKARKGRTTIVIAHRLSTVRNADVIAGF 671
Cdd:cd03227     77 QLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDgQALAEAILEHLVKGAQVIVITHLPELAELADKLIHI 153
ABC_6TM_T1SS_like cd18555
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ...
801-1041 5.16e-05

Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.


Pssm-ID: 349999 [Multi-domain]  Cd Length: 294  Bit Score: 46.73  E-value: 5.16e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  801 IFSKIIGVFTR--IDD--PETKRQNSNLFSLLFLALGIISFITFFLQGFTFGKAGEILTKRLRYMVFRSMLRQDVSWFDd 876
Cdd:cd18555     16 LLTLLIPILTQyvIDNviVPGNLNLLNVLGIGILILFLLYGLFSFLRGYIIIKLQTKLDKSLMSDFFEHLLKLPYSFFE- 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  877 pKNTTGALTTRlANDAAQVKGAIGSRLAVITQNIANLGTGIIISFIYGWQLTLLLLAIVPIIAIAGVVEMKMLSGqalKD 956
Cdd:cd18555     95 -NRSSGDLLFR-ANSNVYIRQILSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLLLLLTRKKIKK---LN 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  957 KKELEGSGK---IATEAIENFRTVVSLTQEQKF----EHMYAQSLQVpyrnSLRKAHIFGITFSFTQAMMYFSYAGCFRF 1029
Cdd:cd18555    170 QEEIVAQTKvqsYLTETLYGIETIKSLGSEKNIykkwENLFKKQLKA----FKKKERLSNILNSISSSIQFIAPLLILWI 245
                          250
                   ....*....|..
gi 1149123047 1030 GAYLVAHKLMSF 1041
Cdd:cd18555    246 GAYLVINGELTL 257
ABC_6TM_PrtD_LapB_HlyB_like cd18782
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ...
785-1041 6.77e-05

uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.


Pssm-ID: 350055 [Multi-domain]  Cd Length: 294  Bit Score: 46.43  E-value: 6.77e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  785 VFCAIINGGLQPAFAIIFSKIIGVFTRIDDPETkrqnsnLFSLLFLALGIISFITFF--LQGFTFGKAGEILTKRLRYMV 862
Cdd:cd18782      8 LALSFVVQLLGLANPLLFQVIIDKVLVQQDLAT------LYVIGVVMLVAALLEAVLtaLRTYLFTDTANRIDLELGGTI 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  863 FRSMLRQDVSWFDdpKNTTGALTTRLaNDAAQVKG-AIGSRLAVITQNIANLGTgIIISFIYGWQLTLLLLAIVPIIAIA 941
Cdd:cd18782     82 IDHLLRLPLGFFD--KRPVGELSTRI-SELDTIRGfLTGTALTTLLDVLFSVIY-IAVLFSYSPLLTLVVLATVPLQLLL 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  942 GVVEMKMLSGQaLKDKKELEGSGKIA-TEAIENFRTVVSLTQE----QKFEHMYAQSLQVPYRNSLRKAHIFGITFSFTQ 1016
Cdd:cd18782    158 TFLFGPILRRQ-IRRRAEASAKTQSYlVESLTGIQTVKAQNAElkarWRWQNRYARSLGEGFKLTVLGTTSGSLSQFLNK 236
                          250       260
                   ....*....|....*....|....*
gi 1149123047 1017 ammyFSYAGCFRFGAYLVAHKLMSF 1041
Cdd:cd18782    237 ----LSSLLVLWVGAYLVLRGELTL 257
ABC_6TM_HetC_like cd18568
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ...
820-1040 6.98e-05

Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.


Pssm-ID: 350012 [Multi-domain]  Cd Length: 294  Bit Score: 46.40  E-value: 6.98e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  820 QNSNLFSLLFLALGIISF-------ITFFLQGFTFGKAGEILTKRLrymvFRSMLRQDVSWFDdpKNTTGALTTRLA-ND 891
Cdd:cd18568     36 KNISLLNLILIGLLIVGIfqillsaVRQYLLDYFANRIDLSLLSDF----YKHLLSLPLSFFA--SRKVGDIITRFQeNQ 109
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  892 AAQ---VKGAIGSRLAVITQNIAnlgtgIIISFIYGWQLTLLLLAIVPIIAIAGVV---EMKMLSGQALKDKKELEGSgk 965
Cdd:cd18568    110 KIRrflTRSALTTILDLLMVFIY-----LGLMFYYNLQLTLIVLAFIPLYVLLTLLsspKLKRNSREIFQANAEQQSF-- 182
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  966 iATEAIENFRTVVSLTQEQKF----EHMYAQSLQVPYRNSlrkahIFGITFSFT-QAMMYFSYAGCFRFGAYLVAHKLMS 1040
Cdd:cd18568    183 -LVEALTGIATIKALAAERPIrwrwENKFAKALNTRFRGQ-----KLSIVLQLIsSLINHLGTIAVLWYGAYLVISGQLT 256
uvrA PRK00349
excinuclease ABC subunit UvrA;
1238-1314 7.96e-05

excinuclease ABC subunit UvrA;


Pssm-ID: 234734 [Multi-domain]  Cd Length: 943  Bit Score: 47.37  E-value: 7.96e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1238 KVGDKGTQLSGGQKQRIAIARALVRQPH---ILLLDEATSALDTES----EKVVQEALDKareGRTCIVIAHRLSTIQNA 1310
Cdd:PRK00349   823 KLGQPATTLSGGEAQRVKLAKELSKRSTgktLYILDEPTTGLHFEDirklLEVLHRLVDK---GNTVVVIEHNLDVIKTA 899

                   ....
gi 1149123047 1311 DLIV 1314
Cdd:PRK00349   900 DWII 903
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
446-689 9.43e-05

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 46.70  E-value: 9.43e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  446 DSYSKSGHKPDNIKGN--LEFRNVhfsypSRKEVKILKGLNLKVQSGQTVALVGNSGCGKSttvQLMQRLY--DP-TEGM 520
Cdd:PRK09700   248 NRFNAMKENVSNLAHEtvFEVRNV-----TSRDRKKVRDISFSVCRGEILGFAGLVGSGRT---ELMNCLFgvDKrAGGE 319
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  521 VSVDGQDIRTIN-VRFLREIIGVVSQ---EPVLFAT-TIAENI------RYGRENVTM----DEIEKAVKEANAYDFIMK 585
Cdd:PRK09700   320 IRLNGKDISPRSpLDAVKKGMAYITEsrrDNGFFPNfSIAQNMaisrslKDGGYKGAMglfhEVDEQRTAENQRELLALK 399
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  586 LpHKFDTLVGErgaqLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDK-ARKGRTTIVIAHRLSTVRN 664
Cdd:PRK09700   400 C-HSVNQNITE----LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQlADDGKVILMVSSELPEIIT 474
                          250       260
                   ....*....|....*....|....*..
gi 1149123047  665 A-DVIAGFDDGVIVEK-GNHDELMKEK 689
Cdd:PRK09700   475 VcDRIAVFCEGRLTQIlTNRDDMSEEE 501
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
601-656 1.10e-04

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 46.26  E-value: 1.10e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1149123047  601 LSGGQKQRIAIARALVRNPKILLLDEATSALDTESE-AVVQVALDKARKGRTTIVIA 656
Cdd:PRK10982   392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKfEIYQLIAELAKKDKGIIIIS 448
PLN03073 PLN03073
ABC transporter F family; Provisional
1245-1302 1.13e-04

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 46.78  E-value: 1.13e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1149123047 1245 QLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKARegRTCIVIAH 1302
Cdd:PLN03073   344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWP--KTFIVVSH 399
ABC_6TM_CvaB_RaxB_like cd18567
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ...
221-407 1.17e-04

Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium.


Pssm-ID: 350011 [Multi-domain]  Cd Length: 294  Bit Score: 45.53  E-value: 1.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  221 FFHAIMRQEIGWFDVHDVGELNTRLtDDVSKINEGIGDK-IGMFFQSMATFFTgFIVGFTRGWKLTLVILAISPVLGLSA 299
Cdd:cd18567     81 LFRHLLRLPLSYFEKRHLGDIVSRF-GSLDEIQQTLTTGfVEALLDGLMAILT-LVMMFLYSPKLALIVLAAVALYALLR 158
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  300 AVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKRIGIKKAItANISIGAAF-LLIYA 378
Cdd:cd18567    159 LALYPPLRRATEEQIVASAKEQSHFLETIRGIQTIKLFGREAEREARWLNLLVDAINADIRLQR-LQILFSAANgLLFGL 237
                          170       180
                   ....*....|....*....|....*....
gi 1149123047  379 SYALAFWYGTTLVLSGEYSIGqVLTVFFS 407
Cdd:cd18567    238 ENILVIYLGALLVLDGEFTVG-MLFAFLA 265
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
487-659 1.78e-04

ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.


Pssm-ID: 213189 [Multi-domain]  Cd Length: 177  Bit Score: 43.71  E-value: 1.78e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  487 VQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEgmvsvdgqdirtinvrflreiigvvsqepvlfattiaenirygrENVT 566
Cdd:cd03222     22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNG--------------------------------------------DNDE 57
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  567 MDEIEKAVKeanaydfimklPHKFDtlvgergaqLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDK- 645
Cdd:cd03222     58 WDGITPVYK-----------PQYID---------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRl 117
                          170
                   ....*....|....*
gi 1149123047  646 -ARKGRTTIVIAHRL 659
Cdd:cd03222    118 sEEGKKTALVVEHDL 132
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
480-680 1.79e-04

ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.


Pssm-ID: 213205 [Multi-domain]  Cd Length: 176  Bit Score: 43.85  E-value: 1.79e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  480 LKGLNLKVQSGQTVALVGNSGCGKSTTVQlmQRLYDPTEGMVSVDGQdirtinvRFLREIIGVVSQepvlFATTIAENIR 559
Cdd:cd03238     11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVN--EGLYASGKARLISFLP-------KFSRNKLIFIDQ----LQFLIDVGLG 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  560 YgrenvtmdeiekavkeanaydfiMKLPHKFDTLvgergaqlSGGQKQRIAIARALVRNPK--ILLLDEATSALDTESEA 637
Cdd:cd03238     78 Y-----------------------LTLGQKLSTL--------SGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDIN 126
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1149123047  638 VVQVALDKAR-KGRTTIVIAHRLSTVRNADVI------AGFDDGVIVEKG 680
Cdd:cd03238    127 QLLEVIKGLIdLGNTVILIEHNLDVLSSADWIidfgpgSGKSGGKVVFSG 176
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
1240-1335 3.10e-04

oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 44.73  E-value: 3.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1240 GDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESE-KVVQEALDKAREGRTCIVIAHRLSTI-QNADLIVVFQ 1317
Cdd:NF000106   139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRnEVWDEVRSMVRDGATVLLTTQYMEEAeQLAHELTVID 218
                           90
                   ....*....|....*...
gi 1149123047 1318 NGRVKEHGTHQQLLAQKG 1335
Cdd:NF000106   219 RGRVIADGKVDELKTKVG 236
PRK15093 PRK15093
peptide ABC transporter ATP-binding protein SapD;
1245-1332 4.49e-04

peptide ABC transporter ATP-binding protein SapD;


Pssm-ID: 185049 [Multi-domain]  Cd Length: 330  Bit Score: 44.02  E-value: 4.49e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1245 QLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTI-QNADLIVVFQNGRV 1321
Cdd:PRK15093   158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnnNTTILLISHDLQMLsQWADKINVLYCGQT 237
                           90
                   ....*....|.
gi 1149123047 1322 KEHGTHQQLLA 1332
Cdd:PRK15093   238 VETAPSKELVT 248
PLN03140 PLN03140
ABC transporter G family member; Provisional
1210-1305 6.81e-04

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 44.45  E-value: 6.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1210 VSQEEIVRAAKEANIHAFIESLPNKYstkVGDKG-TQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEAL 1288
Cdd:PLN03140   986 VSKEEKMMFVDEVMELVELDNLKDAI---VGLPGvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTV 1062
                           90
                   ....*....|....*...
gi 1149123047 1289 -DKAREGRTCIVIAHRLS 1305
Cdd:PLN03140  1063 rNTVDTGRTVVCTIHQPS 1080
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
484-688 9.22e-04

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 43.46  E-value: 9.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  484 NLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRFLREIigvVSQEpvlfattiaenirYGRE 563
Cdd:PRK10938    23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKL---VSDE-------------WQRN 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  564 NVTM---DE----------IEKAVKEANAYDFIMKLPHkFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSA 630
Cdd:PRK10938    87 NTDMlspGEddtgrttaeiIQDEVKDPARCEQLAQQFG-ITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDG 165
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  631 LDTESEAVVQVALDK-ARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVIVEKGNHDELMKE 688
Cdd:PRK10938   166 LDVASRQQLAELLASlHQSGITLVLVLNRFDEIPDfVQFAGVLADCTLAETGEREEILQQ 225
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
443-666 9.63e-04

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 43.46  E-value: 9.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  443 PSIDSYSKSGHKPDNIKgNLEFRNVHFSYPSRKevkILKGLNLKVQSGQTVALVGNSGCGKSTTVQLMQRlyDPTEGMvS 522
Cdd:PRK10938   243 PEPDEPSARHALPANEP-RIVLNNGVVSYNDRP---ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG--DHPQGY-S 315
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  523 VD----------GQDIRTInvrflREIIGVVSQEPVL---FATTIAENIRYGrenvTMDEI--EKAVKEANaydfiMKLP 587
Cdd:PRK10938   316 NDltlfgrrrgsGETIWDI-----KKHIGYVSSSLHLdyrVSTSVRNVILSG----FFDSIgiYQAVSDRQ-----QKLA 381
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  588 HKFDTLVGERGAQ-------LSGGQkQRIA-IARALVRNPKILLLDEATSALDTESEAVVQVALDK-ARKGRTTIV---- 654
Cdd:PRK10938   382 QQWLDILGIDKRTadapfhsLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVlISEGETQLLfvsh 460
                          250       260
                   ....*....|....*....|
gi 1149123047  655 --------IAHRLSTVRNAD 666
Cdd:PRK10938   461 haedapacITHRLEFVPDGD 480
UvrA COG0178
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
1244-1314 1.15e-03

Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];


Pssm-ID: 439948 [Multi-domain]  Cd Length: 941  Bit Score: 43.48  E-value: 1.15e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1149123047 1244 TQLSGGQKQRIAIARALVR---QPHILLLDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIV 1314
Cdd:COG0178    825 TTLSGGEAQRVKLASELSKrstGKTLYILDEPTTGLHFHDIRKLLEVLHRLVDkGNTVVVIEHNLDVIKTADWII 899
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
483-676 1.20e-03

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 43.12  E-value: 1.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  483 LNLKVQSGQTVALVGNSGCGKSTTVQLMQRLYDPTEGMVSVDGQDIRTINVRfLREIIGVV-----SQEPVLF------- 550
Cdd:PRK15439   282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTA-QRLARGLVylpedRQSSGLYldaplaw 360
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  551 -ATTIAEN-----IRYGRENVTMDEIEKAVKeanaydfiMKLPHKfDTLVGergaQLSGGQKQRIAIARALVRNPKILLL 624
Cdd:PRK15439   361 nVCALTHNrrgfwIKPARENAVLERYRRALN--------IKFNHA-EQAAR----TLSGGNQQKVLIAKCLEASPQLLIV 427
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1149123047  625 DEATSALDTESEA-VVQVALDKARKGRTTIVIAHRLSTVRN-ADVIAGFDDGVI 676
Cdd:PRK15439   428 DEPTRGVDVSARNdIYQLIRSIAAQNVAVLFISSDLEEIEQmADRVLVMHQGEI 481
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
1245-1314 1.37e-03

ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.


Pssm-ID: 213194 [Multi-domain]  Cd Length: 162  Bit Score: 40.81  E-value: 1.37e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1149123047 1245 QLSGGQKQRIAIARALVRQPH----ILLLDEATSALDTESEKVVQEALDKAR-EGRTCIVIAHRLSTIQNADLIV 1314
Cdd:cd03227     77 QLSGGEKELSALALILALASLkprpLYILDEIDRGLDPRDGQALAEAILEHLvKGAQVIVITHLPELAELADKLI 151
ABC_6TM_MRP7_D2_like cd18605
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ...
169-415 1.37e-03

Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).


Pssm-ID: 350049 [Multi-domain]  Cd Length: 300  Bit Score: 42.52  E-value: 1.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  169 NDTGFFMNLEEDMTRYAYYYSGIGAGVLVAAYIQ-VSFW--CLAAGRQIHKirkQFFHAIMRQEIGWFDVHDVGELNTRL 245
Cdd:cd18605     29 SNNSFFNFINDSFNFFLTVYGFLAGLNSLFTLLRaFLFAygGLRAARRLHN---KLLSSILFAKMSFFDKTPVGRILNRF 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  246 TDDVSKINEGIGDKIGMFFQSMATFFtGFIVGFTRGWKLTLVILAISPVLG----------------LSAAVWAKILSSF 309
Cdd:cd18605    106 SSDVYTIDDSLPFILNILLAQLFGLL-GYLVVICYQLPWLLLLLLPLAFIYyriqryyratsrelkrLNSVNLSPLYTHF 184
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  310 TdkellayakagavaeEVLAAIRTVIAFGGQKKELERYNKNLEEAKRIGikkaitanisigaaflliYASYALAFWYGTT 389
Cdd:cd18605    185 S---------------ETLKGLVTIRAFRKQERFLKEYLEKLENNQRAQ------------------LASQAASQWLSIR 231
                          250       260
                   ....*....|....*....|....*.
gi 1149123047  390 LVLSGeysigqVLTVFFSVLIGAFSV 415
Cdd:cd18605    232 LQLLG------VLIVTFVALTAVVQH 251
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
1159-1343 1.68e-03

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 42.89  E-value: 1.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1159 PLAGKVLLDGKeikrlnvqwlraHLGIVSQEPIlfdcsiaENIAygdnsRVVSQEEIVRAAKEANIHAFIESLPnkystk 1238
Cdd:PRK00635  1643 PLAQEVVYEGK------------HFGQLLQTPI-------EEVA-----ETFPFLKKIQKPLQALIDNGLGYLP------ 1692
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1239 VGDKGTQLSGGQKQRIAIARALV---RQPHILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQNADLIV 1314
Cdd:PRK00635  1693 LGQNLSSLSLSEKIAIKIAKFLYlppKHPTLFLLDEIATSLDNQQKSALLVQLRTlVSLGHSVIYIDHDPALLKQADYLI 1772
                          170       180       190
                   ....*....|....*....|....*....|..
gi 1149123047 1315 VFQNGRVKEHGthqQLL---AQKGIYFSMVSV 1343
Cdd:PRK00635  1773 EMGPGSGKTGG---KILfsgPPKDISASKDSL 1801
ABC_6TM_CyaB_HlyB_like cd18588
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ...
917-1034 1.69e-03

Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunits of T1SS, such as CyaG and HlyB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. Additionally, CyaB is part of the three T1SS complex proteins for adenylate cyclase toxin CyaA, which is a primary virulence factor in Bordetella pertussis: CyaB (an ABC transporter) CyaD (a membrane fusion protein), and CyaE (an outer membrane protein).


Pssm-ID: 350032 [Multi-domain]  Cd Length: 294  Bit Score: 42.10  E-value: 1.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  917 IIISFIYGWQLTLLLLAIVPIIAIAGVVEMKMLsgQALKDKKELEGSGKIA--TEAIENFRTVVSLTQEQKFEHMYAQSL 994
Cdd:cd18588    133 LAVMFYYSPTLTLIVLASLPLYALLSLLVTPIL--RRRLEEKFQRGAENQSflVETVTGIETVKSLAVEPQFQRRWEELL 210
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1149123047  995 QVPYRNSLRKAHIFGITFSFTQAMMYFSYAGCFRFGAYLV 1034
Cdd:cd18588    211 ARYVKASFKTANLSNLASQIVQLIQKLTTLAILWFGAYLV 250
ABC_6TM_VMR1_D2_like cd18604
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ...
824-944 2.14e-03

Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.


Pssm-ID: 350048 [Multi-domain]  Cd Length: 297  Bit Score: 41.68  E-value: 2.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  824 LFSLLFLALGIISFITFFLQGFtfgKAGEILTKRLRYMVFRSMLRqdvsWFDdpKNTTGALTTRLANDAaqvkGAIGSRL 903
Cdd:cd18604     51 LISLLSVLLGTLRYLLFFFGSL---RASRKLHERLLHSVLRAPLR----WLD--TTPVGRILNRFSKDI----ETIDSEL 117
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1149123047  904 AVITQNIANLGTGIIISFIygwqltlLLLAIVPIIAIAGVV 944
Cdd:cd18604    118 ADSLSSLLESTLSLLVILI-------AIVVVSPAFLLPAVV 151
ABC_6TM_Sav1866_like cd18554
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ...
200-406 2.97e-03

Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.


Pssm-ID: 349998 [Multi-domain]  Cd Length: 299  Bit Score: 41.25  E-value: 2.97e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  200 YIQVSFWCLAAGRQIHKIRKQFFHAIMRQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQSMATFFTGFIVGFT 279
Cdd:cd18554     64 YYRQYFAQWIANKILYDIRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLV 143
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  280 RGWKLTLVILAISPVLGLSAAVWAKILSSFTDKELLAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNKNLEEAKRIGI 359
Cdd:cd18554    144 LNPKLTFVSLVIFPFYILAVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRAL 223
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1149123047  360 KKAITANISIGAAFLLIYASYALAFWYGTTLVLSGEYSIGQvLTVFF 406
Cdd:cd18554    224 KHTRWNAKTFSAVNTITDLAPLLVIGFAAYLVIEGNLTVGT-LVAFV 269
uvrA PRK00349
excinuclease ABC subunit UvrA;
579-668 3.20e-03

excinuclease ABC subunit UvrA;


Pssm-ID: 234734 [Multi-domain]  Cd Length: 943  Bit Score: 41.98  E-value: 3.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  579 AYDF---IMKLPHKFDTLV---------GERGAQLSGGQKQRIAIARALVRNP--KIL-LLDEATSALDTESEA----VV 639
Cdd:PRK00349   797 ALEFfeaIPKIARKLQTLVdvglgyiklGQPATTLSGGEAQRVKLAKELSKRStgKTLyILDEPTTGLHFEDIRklleVL 876
                           90       100
                   ....*....|....*....|....*....
gi 1149123047  640 QVALDKarkGRTTIVIAHRLSTVRNADVI 668
Cdd:PRK00349   877 HRLVDK---GNTVVVIEHNLDVIKTADWI 902
PRK01889 PRK01889
GTPase RsgA; Reviewed
1118-1153 3.22e-03

GTPase RsgA; Reviewed


Pssm-ID: 234988 [Multi-domain]  Cd Length: 356  Bit Score: 41.46  E-value: 3.22e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1149123047 1118 PDIPV-----LQGLSLEV-----KKGQTLALVGSSGCGKSTVV-QLL 1153
Cdd:PRK01889   170 PGVPVlavsaLDGEGLDVlaawlSGGKTVALLGSSGVGKSTLVnALL 216
PRK15093 PRK15093
peptide ABC transporter ATP-binding protein SapD;
600-686 3.26e-03

peptide ABC transporter ATP-binding protein SapD;


Pssm-ID: 185049 [Multi-domain]  Cd Length: 330  Bit Score: 41.33  E-value: 3.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  600 QLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARK--GRTTIVIAHRLSTVRN-ADVIAGFDDGVI 676
Cdd:PRK15093   158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnnNTTILLISHDLQMLSQwADKINVLYCGQT 237
                           90
                   ....*....|
gi 1149123047  677 VEKGNHDELM 686
Cdd:PRK15093   238 VETAPSKELV 247
ABC_6TM_LapB_like cd18587
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; ...
917-1040 3.37e-03

Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), such as LapB. LapB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion, LapA is a RTX (repeats in toxin) protein found in Pseudomonas fluorescens and is required for biofilm formation in this organism. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. In this T1SS system, LapB is a cytoplasmic membrane-localized ATPase, LapC is a membrane fusion protein, and LapE is an outer membrane protein.


Pssm-ID: 350031  Cd Length: 293  Bit Score: 41.27  E-value: 3.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  917 IIISFIyGWQLTLLLLAIVPIIAIAGVV---EMKMLSGQALKdkkelEGSGKIAT--EAIENFRTVVSLTQEQKFEHMYA 991
Cdd:cd18587    133 AVIALI-GGPLALVPLVAIPLVLLYGLLlqkPLRRLVEESMR-----ESAQKNALlvESLSGLETIKALGAEGRMQRRWE 206
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1149123047  992 QSLQVPYRNSLRKAHIFGITFSFTQAMMYFSYAGCFRFGAYLVAHKLMS 1040
Cdd:cd18587    207 EAVAALARSSLKSRLLSSSATNFAQFVQQLVTVAIVIVGVYLISDGELT 255
PRK13546 PRK13546
teichoic acids export ABC transporter ATP-binding subunit TagH;
1123-1333 3.65e-03

teichoic acids export ABC transporter ATP-binding subunit TagH;


Pssm-ID: 184131 [Multi-domain]  Cd Length: 264  Bit Score: 40.95  E-value: 3.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1123 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPLAGKVLLDGkeikrlNVQWLRAHLGIVSQepilfdCSIAENIA 1202
Cdd:PRK13546    40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG------EVSVIAISAGLSGQ------LTGIENIE 107
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1203 YGDNSRVVSQEEIVRAAKE----ANIHAFIESLPNKYSTkvgdkgtqlsgGQKQRIAIARALVRQPHILLLDEATSALDt 1278
Cdd:PRK13546   108 FKMLCMGFKRKEIKAMTPKiiefSELGEFIYQPVKKYSS-----------GMRAKLGFSINITVNPDILVIDEALSVGD- 175
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047 1279 esEKVVQEALDKARE----GRTCIVIAHRLSTIQN-ADLIVVFQNGRVKEHGTHQQLLAQ 1333
Cdd:PRK13546   176 --QTFAQKCLDKIYEfkeqNKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYGELDDVLPK 233
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
604-686 4.21e-03

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 41.42  E-value: 4.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  604 GQKQRIAIARALVRNPKILLLDEATSALDTES----EAVVqvaldKARKGrTTIVIAH-R--LSTV--RNADViagfDDG 674
Cdd:PRK15064   159 GWKLRVLLAQALFSNPDILLLDEPTNNLDINTirwlEDVL-----NERNS-TMIIISHdRhfLNSVctHMADL----DYG 228
                           90
                   ....*....|...
gi 1149123047  675 VI-VEKGNHDELM 686
Cdd:PRK15064   229 ELrVYPGNYDEYM 241
ABC_6TM_Sav1866_like cd18554
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ...
821-959 4.40e-03

Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.


Pssm-ID: 349998 [Multi-domain]  Cd Length: 299  Bit Score: 40.87  E-value: 4.40e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  821 NSNLFSLLFLALGIISFITFFL--------QGFTFGKAGEILtKRLRYMVFRSMLRQDVSWFDDpkNTTGALTTRLANDA 892
Cdd:cd18554     37 LDEKVYKLFTIIGIMFFIFLILrppveyyrQYFAQWIANKIL-YDIRKDLFDHLQKLSLRYYAN--NRSGEIISRVINDV 113
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1149123047  893 AQVKGAIGSRLAVITQNIANLGTGIIISFIYGWQLTLLLLAIVPIIAIAgvveMKMLSGQALKDKKE 959
Cdd:cd18554    114 EQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLVIFPFYILA----VKYFFGRLRKLTKE 176
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
593-668 4.51e-03

ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.


Pssm-ID: 213207 [Multi-domain]  Cd Length: 204  Bit Score: 39.90  E-value: 4.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  593 LVGERGaQLSGGQKQ------RIAIARALVRNPKILLLDEATSALDTESEAVVQVALDKARKG---RTTIVIAHRLSTVR 663
Cdd:cd03240    109 LLDMRG-RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEESLAEIIEERKSqknFQLIVITHDEELVD 187

                   ....*
gi 1149123047  664 NADVI 668
Cdd:cd03240    188 AADHI 192
COG4639 COG4639
Predicted kinase [General function prediction only];
493-581 7.66e-03

Predicted kinase [General function prediction only];


Pssm-ID: 443677 [Multi-domain]  Cd Length: 145  Bit Score: 38.27  E-value: 7.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1149123047  493 VALVGNSGCGKSTTVqlmQRLYDPTEgMVSVDgqDIRTInvRFLREIIGVVSQEPV-LFATTIAENIRYGRE------NV 565
Cdd:COG4639      5 VVLIGLPGSGKSTFA---RRLFAPTE-VVSSD--DIRAL--LGGDENDQSAWGDVFqLAHEIARARLRAGRLtvvdatNL 76
                           90
                   ....*....|....*.
gi 1149123047  566 TMDEIEKAVKEANAYD 581
Cdd:COG4639     77 QREARRRLLALARAYG 92
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
1246-1314 8.89e-03

ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.


Pssm-ID: 213237 [Multi-domain]  Cd Length: 226  Bit Score: 39.16  E-value: 8.89e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1149123047 1246 LSGGQKQRIAIARAL------VrqphILLLDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIV 1314
Cdd:cd03270    138 LSGGEAQRIRLATQIgsgltgV----LYVLDEPSIGLHPRDNDRLIETLKRLRDlGNTVLVVEHDEDTIRAADHVI 209
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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