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Conserved domains on  [gi|6755046|ref|NP_035205|]
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ATP-dependent translocase ABCB1 [Mus musculus]

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
55-1270 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: 593.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     55 LAAIIHGTLLPLLMLVFGnmtdsftkaeasilpsitnqsgpnstLIISNSSLEEEMAIYAYYYTGIGAGVLIVAYIqvSL 134
Cdd:PTZ00265   67 VCATISGGTLPFFVSVFG--------------------------VIMKNMNLGENVNDIIFSLVLIGIFQFILSFI--SS 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    135 WCL--AAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDKIGMFFQSITTFLAGFIIGFISGWK 212
Cdd:PTZ00265  119 FCMdvVTTKILKTLKLEFLKSVFYQDGQFHDNNPGSKLTSDLDFYLEQVNAGIGTKFITIFTYASAFLGLYIWSLFKNAR 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    213 LTLVILAVSPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQKELERYNKNLEEAKNVGIKKAI 292
Cdd:PTZ00265  199 LTLCITCVFPLIYICGVICNKKVKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGEKTILKKFNLSEKLYSKYILKANF 278
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    293 TASISIGIAYLLVYASYALAFWYGTSLVLS--------NEYSIGEVLTVFFSILLGTFSIGHLAPNIEAFANARGAAFEI 364
Cdd:PTZ00265  279 MESLHIGMINGFILASYAFGFWYGTRIIISdlsnqqpnNDFHGGSVISILLGVLISMFMLTIILPNITEYMKSLEATNSL 358
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    365 FKIIDNEPSIDSFSTKGYKPDsiMGNLEFKNVHFNYPSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYD 444
Cdd:PTZ00265  359 YEIINRKPLVENNDDGKKLKD--IKKIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYD 436
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    445 PLEGVVSI-DGQDIRTINVRYLREIIGVVSQEPVLFATTIAENIRYG--------------RED---------------- 493
Cdd:PTZ00265  437 PTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSlyslkdlealsnyyNEDgndsqenknkrnscra 516
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    494 ------------VTMDEIEKAVKEANA---------------YDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVR 546
Cdd:PTZ00265  517 kcagdlndmsntTDSNELIEMRKNYQTikdsevvdvskkvliHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIR 596
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    547 NPKILLLDEATSALDTESEAVVQAALD--KAREGRTTIVIAHRLSTVRNADVI--------------------------- 597
Cdd:PTZ00265  597 NPKILILDEATSSLDNKSEYLVQKTINnlKGNENRITIIIAHRLSTIRYANTIfvlsnrergstvdvdiigedptkdnke 676
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    598 --------------------AGFDGGVIVEQGNHDELMREK-GIYFKLVMTQT--------------------------R 630
Cdd:PTZ00265  677 nnnknnkddnnnnnnnnnnkINNAGSYIIEQGTHDALMKNKnGIYYTMINNQKvsskkssnndndkdsdmkssaykdseR 756
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    631 GNEIEP--GNNAYGSQS----------DTDASElTSEESKSPLIRRSIYRSvhRKQDQERRLSMKE--AVDEDVPLVSFw 696
Cdd:PTZ00265  757 GYDPDEmnGNSKHENESasnkksckmsDENASE-NNAGGKLPFLRNLFKRK--PKAPNNLRIVYREifSYKKDVTIIAL- 832
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    697 rilnlnlsewpyllvgvlCAVINGCIQPVFAIVFSRIVGVFSrddDHETKRQNCNLFSLFFLVMGLISFVTYFFQGFTFG 776
Cdd:PTZ00265  833 ------------------SILVAGGLYPVFALLYAKYVSTLF---DFANLEANSNKYSLYILVIAIAMFISETLKNYYNN 891
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    777 KAGEILTKRVRYMVFKSMLRQDISWFDDHKNSTGSLTTRLASDASSVKGAMGARLAVVTQNVANLGTGVILSLVYgwqlt 856
Cdd:PTZ00265  892 VIGEKVEKTMKRRLFENILYQEISFFDQDKHAPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSMVMSFYF----- 966
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    857 lllvviIPLI--VLGGI--IEMKLLSGQAL----KD--KKQLEISGKI----------------ATEAIENFRTIVSLTR 910
Cdd:PTZ00265  967 ------CPIVaaVLTGTyfIFMRVFAIRARltanKDveKKEINQPGTVfaynsddeifkdpsflIQEAFYNMNTVIIYGL 1040
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    911 EQKFETMYAQSLQVPYRNAMKKAHVFGITFSFTQAMMYFSYAACFRFGAYLVAQQLMTFENVMLVFSAVVFGAMAAGNTS 990
Cdd:PTZ00265 1041 EDYFCNLIEKAIDYSNKGQKRKTLVNSMLWGFSQSAQLFINSFAYWFGSFLIRRGTILVDDFMKSLFTFLFTGSYAGKLM 1120
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    991 SFAPDYAKAKVSASHIIRIIEKTPEIDSYSTEGLK---PTLLEGNVKFNGVQFNYPTRPNIPVLQGLSLEVKKGQTLALV 1067
Cdd:PTZ00265 1121 SLKGDSENAKLSFEKYYPLIIRKSNIDVRDNGGIRiknKNDIKGKIEIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIV 1200
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1068 GSSGCGKSTVVQLLERFYD------------------------------------------------------PMAGSVF 1093
Cdd:PTZ00265 1201 GETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfKNSGKIL 1280
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1094 LDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAENIAYGDNSraVSHEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQ 1173
Cdd:PTZ00265 1281 LDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKED--ATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKS 1358
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1174 LSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEAL----DKAreGRTCIVIAHRLSTIQNADLIVVIENGK- 1248
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIvdikDKA--DKTIITIAHRIASIKRSDKIVVFNNPDr 1436
                        1450      1460
                  ....*....|....*....|....*..
gi 6755046   1249 ----VKEHGTHQQLL-AQKGIYFSMVQ 1270
Cdd:PTZ00265 1437 tgsfVQAHGTHEELLsVQDGVYKKYVK 1463
 
Name Accession Description Interval E-value
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
55-1270 0e+00

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 593.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     55 LAAIIHGTLLPLLMLVFGnmtdsftkaeasilpsitnqsgpnstLIISNSSLEEEMAIYAYYYTGIGAGVLIVAYIqvSL 134
Cdd:PTZ00265   67 VCATISGGTLPFFVSVFG--------------------------VIMKNMNLGENVNDIIFSLVLIGIFQFILSFI--SS 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    135 WCL--AAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDKIGMFFQSITTFLAGFIIGFISGWK 212
Cdd:PTZ00265  119 FCMdvVTTKILKTLKLEFLKSVFYQDGQFHDNNPGSKLTSDLDFYLEQVNAGIGTKFITIFTYASAFLGLYIWSLFKNAR 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    213 LTLVILAVSPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQKELERYNKNLEEAKNVGIKKAI 292
Cdd:PTZ00265  199 LTLCITCVFPLIYICGVICNKKVKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGEKTILKKFNLSEKLYSKYILKANF 278
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    293 TASISIGIAYLLVYASYALAFWYGTSLVLS--------NEYSIGEVLTVFFSILLGTFSIGHLAPNIEAFANARGAAFEI 364
Cdd:PTZ00265  279 MESLHIGMINGFILASYAFGFWYGTRIIISdlsnqqpnNDFHGGSVISILLGVLISMFMLTIILPNITEYMKSLEATNSL 358
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    365 FKIIDNEPSIDSFSTKGYKPDsiMGNLEFKNVHFNYPSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYD 444
Cdd:PTZ00265  359 YEIINRKPLVENNDDGKKLKD--IKKIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYD 436
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    445 PLEGVVSI-DGQDIRTINVRYLREIIGVVSQEPVLFATTIAENIRYG--------------RED---------------- 493
Cdd:PTZ00265  437 PTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSlyslkdlealsnyyNEDgndsqenknkrnscra 516
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    494 ------------VTMDEIEKAVKEANA---------------YDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVR 546
Cdd:PTZ00265  517 kcagdlndmsntTDSNELIEMRKNYQTikdsevvdvskkvliHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIR 596
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    547 NPKILLLDEATSALDTESEAVVQAALD--KAREGRTTIVIAHRLSTVRNADVI--------------------------- 597
Cdd:PTZ00265  597 NPKILILDEATSSLDNKSEYLVQKTINnlKGNENRITIIIAHRLSTIRYANTIfvlsnrergstvdvdiigedptkdnke 676
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    598 --------------------AGFDGGVIVEQGNHDELMREK-GIYFKLVMTQT--------------------------R 630
Cdd:PTZ00265  677 nnnknnkddnnnnnnnnnnkINNAGSYIIEQGTHDALMKNKnGIYYTMINNQKvsskkssnndndkdsdmkssaykdseR 756
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    631 GNEIEP--GNNAYGSQS----------DTDASElTSEESKSPLIRRSIYRSvhRKQDQERRLSMKE--AVDEDVPLVSFw 696
Cdd:PTZ00265  757 GYDPDEmnGNSKHENESasnkksckmsDENASE-NNAGGKLPFLRNLFKRK--PKAPNNLRIVYREifSYKKDVTIIAL- 832
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    697 rilnlnlsewpyllvgvlCAVINGCIQPVFAIVFSRIVGVFSrddDHETKRQNCNLFSLFFLVMGLISFVTYFFQGFTFG 776
Cdd:PTZ00265  833 ------------------SILVAGGLYPVFALLYAKYVSTLF---DFANLEANSNKYSLYILVIAIAMFISETLKNYYNN 891
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    777 KAGEILTKRVRYMVFKSMLRQDISWFDDHKNSTGSLTTRLASDASSVKGAMGARLAVVTQNVANLGTGVILSLVYgwqlt 856
Cdd:PTZ00265  892 VIGEKVEKTMKRRLFENILYQEISFFDQDKHAPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSMVMSFYF----- 966
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    857 lllvviIPLI--VLGGI--IEMKLLSGQAL----KD--KKQLEISGKI----------------ATEAIENFRTIVSLTR 910
Cdd:PTZ00265  967 ------CPIVaaVLTGTyfIFMRVFAIRARltanKDveKKEINQPGTVfaynsddeifkdpsflIQEAFYNMNTVIIYGL 1040
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    911 EQKFETMYAQSLQVPYRNAMKKAHVFGITFSFTQAMMYFSYAACFRFGAYLVAQQLMTFENVMLVFSAVVFGAMAAGNTS 990
Cdd:PTZ00265 1041 EDYFCNLIEKAIDYSNKGQKRKTLVNSMLWGFSQSAQLFINSFAYWFGSFLIRRGTILVDDFMKSLFTFLFTGSYAGKLM 1120
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    991 SFAPDYAKAKVSASHIIRIIEKTPEIDSYSTEGLK---PTLLEGNVKFNGVQFNYPTRPNIPVLQGLSLEVKKGQTLALV 1067
Cdd:PTZ00265 1121 SLKGDSENAKLSFEKYYPLIIRKSNIDVRDNGGIRiknKNDIKGKIEIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIV 1200
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1068 GSSGCGKSTVVQLLERFYD------------------------------------------------------PMAGSVF 1093
Cdd:PTZ00265 1201 GETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfKNSGKIL 1280
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1094 LDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAENIAYGDNSraVSHEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQ 1173
Cdd:PTZ00265 1281 LDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKED--ATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKS 1358
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1174 LSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEAL----DKAreGRTCIVIAHRLSTIQNADLIVVIENGK- 1248
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIvdikDKA--DKTIITIAHRIASIKRSDKIVVFNNPDr 1436
                        1450      1460
                  ....*....|....*....|....*..
gi 6755046   1249 ----VKEHGTHQQLL-AQKGIYFSMVQ 1270
Cdd:PTZ00265 1437 tgsfVQAHGTHEELLsVQDGVYKKYVK 1463
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
38-631 7.14e-180

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 542.83  E-value: 7.14e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    38 MFRYAdWLDKLCMILGTLAAIIHGTLLPLLMLVFGNMTDSFTkaeasilpsitnqSGPNSTLIISnssleeemaiYAYYY 117
Cdd:COG1132   12 LLRYL-RPYRGLLILALLLLLLSALLELLLPLLLGRIIDALL-------------AGGDLSALLL----------LLLLL 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   118 TGIGAGVLIVAYIQVSLWCLAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDKIGMFFQSIT 197
Cdd:COG1132   68 LGLALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVV 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   198 TFLAGFIIGFISGWKLTLVILAVSPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQKELERYN 277
Cdd:COG1132  148 TLIGALVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFR 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   278 KNLEEAKNVGIKKAITASISIGIAYLLVYASYALAFWYGTSLVLSNEYSIGEVLTVFFSILLGTFSIGHLAPNIEAFANA 357
Cdd:COG1132  228 EANEELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRA 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   358 RGAAFEIFKIIDNEPSIDSfSTKGYKPDSIMGNLEFKNVHFNYPSRSEVqiLKGLNLKVKSGQTVALVGNSGCGKSTTVQ 437
Cdd:COG1132  308 LASAERIFELLDEPPEIPD-PPGAVPLPPVRGEIEFENVSFSYPGDRPV--LKDISLTIPPGETVALVGPSGSGKSTLVN 384
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   438 LMQRLYDPLEGVVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENIRYGREDVTMDEIEKAVKEANAYDFIMKLPH 517
Cdd:COG1132  385 LLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPD 464
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   518 QFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVI 597
Cdd:COG1132  465 GYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRI 544
                        570       580       590
                 ....*....|....*....|....*....|....
gi 6755046   598 AGFDGGVIVEQGNHDELMREKGIYFKLVMTQTRG 631
Cdd:COG1132  545 LVLDDGRIVEQGTHEELLARGGLYARLYRLQFGE 578
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
1033-1272 1.43e-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: 458.16  E-value: 1.43e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1033 VKFNGVQFNYPTRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLG 1112
Cdd:cd03249    1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1113 IVSQEPILFDCSIAENIAYGDNSRAVshEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQP 1192
Cdd:cd03249   81 LVSQEPVLFDGTIAENIRYGKPDATD--EEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNP 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1193 HILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQKGIYFSMVQAG 1272
Cdd:cd03249  159 KILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
138-625 5.60e-141

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 445.71  E-value: 5.60e-141
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     138 AAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDKIGMFFQSITTFLAGFIIGFISGWKLTLVI 217
Cdd:TIGR00958  228 TMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTMVT 307
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     218 LAVSPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQKELERYNKNLEEAKNVGIKKAITASIS 297
Cdd:TIGR00958  308 LINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRKALAYAGY 387
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     298 IGIAYLLVYASYALAFWYGTSLVLSNEYSIGEVLtvffSILLGTFSIGHLAPNIEAFAN----ARGAAFEIFKIIDNEPS 373
Cdd:TIGR00958  388 LWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLV----SFLLYQEQLGEAVRVLSYVYSgmmqAVGASEKVFEYLDRKPN 463
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     374 IDSfsTKGYKPDSIMGNLEFKNVHFNYPSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSID 453
Cdd:TIGR00958  464 IPL--TGTLAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLD 541
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     454 GQDIRTINVRYLREIIGVVSQEPVLFATTIAENIRYGREDVTMDEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGG 533
Cdd:TIGR00958  542 GVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGG 621
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     534 QKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAalDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDE 613
Cdd:TIGR00958  622 QKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQ 699
                          490
                   ....*....|..
gi 6755046     614 LMREKGIYFKLV 625
Cdd:TIGR00958  700 LMEDQGCYKHLV 711
ABC_membrane pfam00664
ABC transporter transmembrane region; This family represents a unit of six transmembrane ...
50-342 1.28e-82

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: 271.44  E-value: 1.28e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046      50 MILGTLAAIIHGTLLPLLMLVFGNMTDSFTKaeasilpsitnqsgpnstliiSNSSLEEEMAIYAYYYTGIGAGVLIVAY 129
Cdd:pfam00664    1 LILAILLAILSGAISPAFPLVLGRILDVLLP---------------------DGDPETQALNVYSLALLLLGLAQFILSF 59
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     130 IQVSLWCLAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDKIGMFFQSITTFLAGFIIGFIS 209
Cdd:pfam00664   60 LQSYLLNHTGERLSRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYY 139
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     210 GWKLTLVILAVSPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQKELERYNKNLEEAKNVGIK 289
Cdd:pfam00664  140 GWKLTLVLLAVLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIK 219
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 6755046     290 KAITASISIGIAYLLVYASYALAFWYGTSLVLSNEYSIGE--VLTVFFSILLGTF 342
Cdd:pfam00664  220 KAVANGLSFGITQFIGYLSYALALWFGAYLVISGELSVGDlvAFLSLFAQLFGPL 274
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
400-595 5.23e-22

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 94.99  E-value: 5.23e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    400 YPSRsevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGqdirTINVRYLREIIGVVSQEPVlf 479
Cdd:NF040873    2 YGGR---PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG----GARVAYVPQRSEVPDSLPL-- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    480 atTIAENI------------RYGREDvtmdeiEKAVKEAnaydfIMKLphQFDTLVGERGAQLSGGQKQRIAIARALVRN 547
Cdd:NF040873   73 --TVRDLVamgrwarrglwrRLTRDD------RAAVDDA-----LERV--GLADLAGRQLGELSGGQRQRALLAQGLAQE 137
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 6755046    548 PKILLLDEATSALDTESEAVVQAAL-DKAREGRTTIVIAHRLSTVRNAD 595
Cdd:NF040873  138 ADLLLLDEPTTGLDAESRERIIALLaEEHARGATVVVVTHDLELVRRAD 186
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
1042-1244 1.18e-21

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 93.84  E-value: 1.18e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1042 YPTRPnipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQwlrahlgiVSQEPILF 1121
Cdd:NF040873    2 YGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQ--------RSEVPDSL 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1122 DCSIAENIAYGDNSRAVSHEEIVRAAKEAnihqFIDSLpdkynTRVGDKG------TQLSGGQKQRIAIARALVRQPHIL 1195
Cdd:NF040873   71 PLTVRDLVAMGRWARRGLWRRLTRDDRAA----VDDAL-----ERVGLADlagrqlGELSGGQRQRALLAQGLAQEADLL 141
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 6755046   1196 LLDEATSALDTESEKVVQEAL-DKAREGRTCIVIAHRLSTIQNADLIVVI 1244
Cdd:NF040873  142 LLDEPTTGLDAESRERIIALLaEEHARGATVVVVTHDLELVRRADPCVLL 191
GguA NF040905
sugar ABC transporter ATP-binding protein;
1044-1251 4.45e-17

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 86.00  E-value: 4.45e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1044 TRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYdP---MAGSVFLDGKE-----IKQlnvqwlRAHLGIV- 1114
Cdd:NF040905   10 TFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PhgsYEGEILFDGEVcrfkdIRD------SEALGIVi 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1115 -SQE----PILfdcSIAENIAYGdNSRA----VSHEEIVRAAKE--ANIhqfidSLPDKYNTRVGDKGTqlsgGQKQRIA 1183
Cdd:NF040905   83 iHQElaliPYL---SIAENIFLG-NERAkrgvIDWNETNRRAREllAKV-----GLDESPDTLVTDIGV----GKQQLVE 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1184 IARALVRQPHILLLDEATSAL-DTESEKVVQEALDKAREGRTCIVIAHRLSTI-QNADLIVVIENGKVKE 1251
Cdd:NF040905  150 IAKALSKDVKLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIrRVADSITVLRDGRTIE 219
GguA NF040905
sugar ABC transporter ATP-binding protein;
406-597 1.11e-14

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 78.29  E-value: 1.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    406 VQILKGLNLKVKSGQTVALVGNSGCGKSTtvqLMQRL-----YDPLEGVVSIDGQ-----DIRTinvrylREIIGVV--S 473
Cdd:NF040905   14 VKALDDVNLSVREGEIHALCGENGAGKST---LMKVLsgvypHGSYEGEILFDGEvcrfkDIRD------SEALGIViiH 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    474 QE----PVLfatTIAENIRYGREDVTMDEI--EKAVKEANAYDFIMKLPHQFDTLVGERGAqlsgGQKQRIAIARALVRN 547
Cdd:NF040905   85 QElaliPYL---SIAENIFLGNERAKRGVIdwNETNRRARELLAKVGLDESPDTLVTDIGV----GKQQLVEIAKALSKD 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 6755046    548 PKILLLDEATSAL-DTESEAVVQAALDKAREGRTTIVIAHRLSTVRN-ADVI 597
Cdd:NF040905  158 VKLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIRRvADSI 209
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
418-610 5.14e-14

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: 70.87  E-value: 5.14e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046      418 SGQTVALVGNSGCGKSTTVQ-LMQRLYDPLEGVVSIDGQDIRTINVRYLREIIgvvsqepvlfattiaenirygredvtm 496
Cdd:smart00382    1 PGEVILIVGPPGSGKTTLARaLARELGPPGGGVIYIDGEDILEEVLDQLLLII--------------------------- 53
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046      497 deiekavkeanaydfimklphqfdtlVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALD--- 573
Cdd:smart00382   54 --------------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrl 107
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|.
gi 6755046      574 ----KAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGN 610
Cdd:smart00382  108 llllKSEKNLTVILTTNDEKDLGPALLRRRFDRRIVLLLIL 148
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
405-619 9.70e-05

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 46.27  E-value: 9.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    405 EVQILKGLNLKVKSGQTVALVGNSGCGKSTTVqLMQRLYDPLEGVVSIDGQdIRTINVRYLREIIGVvsQEPVLFATTIA 484
Cdd:NF000106   25 EVKAVDGVDLDVREGTVLGVLGP*GAA**RGA-LPAHV*GPDAGRRPWRF*-TWCANRRALRRTIG*--HRPVR*GRRES 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    485 ENiryGREDVTM--DEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDT 562
Cdd:NF000106  101 FS---GRENLYMigR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDP 177
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 6755046    563 ESE-AVVQAALDKAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDELMREKG 619
Cdd:NF000106  178 RTRnEVWDEVRSMVRDGATVLLTTQYMEEAEQlAHELTVIDRGRVIADGKVDELKTKVG 236
GguA NF040905
sugar ABC transporter ATP-binding protein;
1043-1228 1.17e-04

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 46.32  E-value: 1.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1043 PTRPNIPVLQGLSLEVKKGQTLALVGSSGCGKS-TVVQLLERFYDP-MAGSVFLDGKEIKQLNVQWL-----------RA 1109
Cdd:NF040905  268 PLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTeLAMSVFGRSYGRnISGTVFKDGKEVDVSTVSDAidaglayvtedRK 347
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1110 HLGIVSQEPILFDCSIAeniaygdNSRAVSHEEIVRAAKEANIHQfidSLPDKYNTR---VGDKGTQLSGGQKQRIAIAR 1186
Cdd:NF040905  348 GYGLNLIDDIKRNITLA-------NLGKVSRRGVIDENEEIKVAE---EYRKKMNIKtpsVFQKVGNLSGGNQQKVVLSK 417
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 6755046   1187 ALVRQPHILLLDEATSALDT----ESEKVVQEAldkAREGRTCIVI 1228
Cdd:NF040905  418 WLFTDPDVLILDEPTRGIDVgakyEIYTIINEL---AAEGKGVIVI 460
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
1168-1263 1.29e-04

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 45.88  E-value: 1.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1168 GDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESE-KVVQEALDKAREGRTCIVIAHRLSTI-QNADLIVVIE 1245
Cdd:NF000106  139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRnEVWDEVRSMVRDGATVLLTTQYMEEAeQLAHELTVID 218
                          90
                  ....*....|....*...
gi 6755046   1246 NGKVKEHGTHQQLLAQKG 1263
Cdd:NF000106  219 RGRVIADGKVDELKTKVG 236
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
1051-1263 2.22e-04

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 45.50  E-value: 2.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1051 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLerfydpmAGSvfldgKEIKQLNVQWL------RAHLGIVSQE------- 1117
Cdd:NF033858   17 LDDVSLDIPAGCMVGLIGPDGVGKSSLLSLI-------AGA-----RKIQQGRVEVLggdmadARHRRAVCPRiaympqg 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1118 ------PILfdcSIAENIA-----YGdNSRAVSHEEIVRAAKEANIHQFIDSLPDKyntrvgdkgtqLSGGQKQRIAIAR 1186
Cdd:NF033858   85 lgknlyPTL---SVFENLDffgrlFG-QDAAERRRRIDELLRATGLAPFADRPAGK-----------LSGGMKQKLGLCC 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1187 ALVRQPHILLLDEATSALDTESEKvvQ-----EALDKAREGRTCIViahrlST--IQNA---DLIVVIENGKVKEHGTHQ 1256
Cdd:NF033858  150 ALIHDPDLLILDEPTTGVDPLSRR--QfweliDRIRAERPGMSVLV-----ATayMEEAerfDWLVAMDAGRVLATGTPA 222

                  ....*..
gi 6755046   1257 QLLAQKG 1263
Cdd:NF033858  223 ELLARTG 229
GguA NF040905
sugar ABC transporter ATP-binding protein;
391-584 5.06e-04

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 44.40  E-value: 5.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    391 LEFKNVHFNYPSRSEVQILKGLNLKVKSGQTVALVGNSGCGKS-TTVQLMQRLYDP-LEGVVSIDGQDIRTINVR----- 463
Cdd:NF040905  258 FEVKNWTVYHPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTeLAMSVFGRSYGRnISGTVFKDGKEVDVSTVSdaida 337
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    464 ---YL---REIIGVVSQEPVLFATTIAENIRYGREDVtMDEIEKaVKEANAY--DFIMKLPHqfdtlVGERGAQLSGGQK 535
Cdd:NF040905  338 glaYVtedRKGYGLNLIDDIKRNITLANLGKVSRRGV-IDENEE-IKVAEEYrkKMNIKTPS-----VFQKVGNLSGGNQ 410
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 6755046    536 QRIAIARALVRNPKILLLDEATSALDT----ESEAVVQaalDKAREGRTTIVI 584
Cdd:NF040905  411 QKVVLSKWLFTDPDVLILDEPTRGIDVgakyEIYTIIN---ELAAEGKGVIVI 460
 
Name Accession Description Interval E-value
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
55-1270 0e+00

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 593.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     55 LAAIIHGTLLPLLMLVFGnmtdsftkaeasilpsitnqsgpnstLIISNSSLEEEMAIYAYYYTGIGAGVLIVAYIqvSL 134
Cdd:PTZ00265   67 VCATISGGTLPFFVSVFG--------------------------VIMKNMNLGENVNDIIFSLVLIGIFQFILSFI--SS 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    135 WCL--AAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDKIGMFFQSITTFLAGFIIGFISGWK 212
Cdd:PTZ00265  119 FCMdvVTTKILKTLKLEFLKSVFYQDGQFHDNNPGSKLTSDLDFYLEQVNAGIGTKFITIFTYASAFLGLYIWSLFKNAR 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    213 LTLVILAVSPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQKELERYNKNLEEAKNVGIKKAI 292
Cdd:PTZ00265  199 LTLCITCVFPLIYICGVICNKKVKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGEKTILKKFNLSEKLYSKYILKANF 278
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    293 TASISIGIAYLLVYASYALAFWYGTSLVLS--------NEYSIGEVLTVFFSILLGTFSIGHLAPNIEAFANARGAAFEI 364
Cdd:PTZ00265  279 MESLHIGMINGFILASYAFGFWYGTRIIISdlsnqqpnNDFHGGSVISILLGVLISMFMLTIILPNITEYMKSLEATNSL 358
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    365 FKIIDNEPSIDSFSTKGYKPDsiMGNLEFKNVHFNYPSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYD 444
Cdd:PTZ00265  359 YEIINRKPLVENNDDGKKLKD--IKKIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYD 436
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    445 PLEGVVSI-DGQDIRTINVRYLREIIGVVSQEPVLFATTIAENIRYG--------------RED---------------- 493
Cdd:PTZ00265  437 PTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSlyslkdlealsnyyNEDgndsqenknkrnscra 516
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    494 ------------VTMDEIEKAVKEANA---------------YDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVR 546
Cdd:PTZ00265  517 kcagdlndmsntTDSNELIEMRKNYQTikdsevvdvskkvliHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIR 596
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    547 NPKILLLDEATSALDTESEAVVQAALD--KAREGRTTIVIAHRLSTVRNADVI--------------------------- 597
Cdd:PTZ00265  597 NPKILILDEATSSLDNKSEYLVQKTINnlKGNENRITIIIAHRLSTIRYANTIfvlsnrergstvdvdiigedptkdnke 676
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    598 --------------------AGFDGGVIVEQGNHDELMREK-GIYFKLVMTQT--------------------------R 630
Cdd:PTZ00265  677 nnnknnkddnnnnnnnnnnkINNAGSYIIEQGTHDALMKNKnGIYYTMINNQKvsskkssnndndkdsdmkssaykdseR 756
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    631 GNEIEP--GNNAYGSQS----------DTDASElTSEESKSPLIRRSIYRSvhRKQDQERRLSMKE--AVDEDVPLVSFw 696
Cdd:PTZ00265  757 GYDPDEmnGNSKHENESasnkksckmsDENASE-NNAGGKLPFLRNLFKRK--PKAPNNLRIVYREifSYKKDVTIIAL- 832
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    697 rilnlnlsewpyllvgvlCAVINGCIQPVFAIVFSRIVGVFSrddDHETKRQNCNLFSLFFLVMGLISFVTYFFQGFTFG 776
Cdd:PTZ00265  833 ------------------SILVAGGLYPVFALLYAKYVSTLF---DFANLEANSNKYSLYILVIAIAMFISETLKNYYNN 891
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    777 KAGEILTKRVRYMVFKSMLRQDISWFDDHKNSTGSLTTRLASDASSVKGAMGARLAVVTQNVANLGTGVILSLVYgwqlt 856
Cdd:PTZ00265  892 VIGEKVEKTMKRRLFENILYQEISFFDQDKHAPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSMVMSFYF----- 966
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    857 lllvviIPLI--VLGGI--IEMKLLSGQAL----KD--KKQLEISGKI----------------ATEAIENFRTIVSLTR 910
Cdd:PTZ00265  967 ------CPIVaaVLTGTyfIFMRVFAIRARltanKDveKKEINQPGTVfaynsddeifkdpsflIQEAFYNMNTVIIYGL 1040
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    911 EQKFETMYAQSLQVPYRNAMKKAHVFGITFSFTQAMMYFSYAACFRFGAYLVAQQLMTFENVMLVFSAVVFGAMAAGNTS 990
Cdd:PTZ00265 1041 EDYFCNLIEKAIDYSNKGQKRKTLVNSMLWGFSQSAQLFINSFAYWFGSFLIRRGTILVDDFMKSLFTFLFTGSYAGKLM 1120
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    991 SFAPDYAKAKVSASHIIRIIEKTPEIDSYSTEGLK---PTLLEGNVKFNGVQFNYPTRPNIPVLQGLSLEVKKGQTLALV 1067
Cdd:PTZ00265 1121 SLKGDSENAKLSFEKYYPLIIRKSNIDVRDNGGIRiknKNDIKGKIEIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIV 1200
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1068 GSSGCGKSTVVQLLERFYD------------------------------------------------------PMAGSVF 1093
Cdd:PTZ00265 1201 GETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfKNSGKIL 1280
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1094 LDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAENIAYGDNSraVSHEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQ 1173
Cdd:PTZ00265 1281 LDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKED--ATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKS 1358
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1174 LSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEAL----DKAreGRTCIVIAHRLSTIQNADLIVVIENGK- 1248
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIvdikDKA--DKTIITIAHRIASIKRSDKIVVFNNPDr 1436
                        1450      1460
                  ....*....|....*....|....*..
gi 6755046   1249 ----VKEHGTHQQLL-AQKGIYFSMVQ 1270
Cdd:PTZ00265 1437 tgsfVQAHGTHEELLsVQDGVYKKYVK 1463
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
38-631 7.14e-180

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 542.83  E-value: 7.14e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    38 MFRYAdWLDKLCMILGTLAAIIHGTLLPLLMLVFGNMTDSFTkaeasilpsitnqSGPNSTLIISnssleeemaiYAYYY 117
Cdd:COG1132   12 LLRYL-RPYRGLLILALLLLLLSALLELLLPLLLGRIIDALL-------------AGGDLSALLL----------LLLLL 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   118 TGIGAGVLIVAYIQVSLWCLAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDKIGMFFQSIT 197
Cdd:COG1132   68 LGLALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVV 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   198 TFLAGFIIGFISGWKLTLVILAVSPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQKELERYN 277
Cdd:COG1132  148 TLIGALVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFR 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   278 KNLEEAKNVGIKKAITASISIGIAYLLVYASYALAFWYGTSLVLSNEYSIGEVLTVFFSILLGTFSIGHLAPNIEAFANA 357
Cdd:COG1132  228 EANEELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRA 307
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   358 RGAAFEIFKIIDNEPSIDSfSTKGYKPDSIMGNLEFKNVHFNYPSRSEVqiLKGLNLKVKSGQTVALVGNSGCGKSTTVQ 437
Cdd:COG1132  308 LASAERIFELLDEPPEIPD-PPGAVPLPPVRGEIEFENVSFSYPGDRPV--LKDISLTIPPGETVALVGPSGSGKSTLVN 384
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   438 LMQRLYDPLEGVVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENIRYGREDVTMDEIEKAVKEANAYDFIMKLPH 517
Cdd:COG1132  385 LLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPD 464
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   518 QFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVI 597
Cdd:COG1132  465 GYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRI 544
                        570       580       590
                 ....*....|....*....|....*....|....
gi 6755046   598 AGFDGGVIVEQGNHDELMREKGIYFKLVMTQTRG 631
Cdd:COG1132  545 LVLDDGRIVEQGTHEELLARGGLYARLYRLQFGE 578
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
694-1271 4.72e-167

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 509.32  E-value: 4.72e-167
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   694 SFWRILNLNLSEWPYLLVGVLCAVINGCIQPVFAIVFSRIVGVFSRDDDHETkrqnCNLFSLFFLVMGLISFVTYFFQGF 773
Cdd:COG1132    8 LLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSA----LLLLLLLLLGLALLRALLSYLQRY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   774 TFGKAGEILTKRVRYMVFKSMLRQDISWFDDHknSTGSLTTRLASDASSVKGAMGARLAVVTQNVANLGTGVILSLVYGW 853
Cdd:COG1132   84 LLARLAQRVVADLRRDLFEHLLRLPLSFFDRR--RTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDW 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   854 QLTLLLVVIIPLIVLGGIIEMKLLSGQALK-DKKQLEISGKIaTEAIENFRTIVSLTREQKFETMYAQSLQVPYRNAMKK 932
Cdd:COG1132  162 RLALIVLLVLPLLLLVLRLFGRRLRKLFRRvQEALAELNGRL-QESLSGIRVVKAFGREERELERFREANEELRRANLRA 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   933 AHVFGITFSFTQAMMYFSYAACFRFGAYLVAQQLMTFENVMLVFSAVVFGAMAAGNTSSFAPDYAKAKVSASHIIRIIEK 1012
Cdd:COG1132  241 ARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDE 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1013 TPEIDSySTEGLKPTLLEGNVKFNGVQFNYPtrPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSV 1092
Cdd:COG1132  321 PPEIPD-PPGAVPLPPVRGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRI 397
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1093 FLDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAENIAYGDNSraVSHEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGT 1172
Cdd:COG1132  398 LIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPD--ATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGV 475
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1173 QLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEH 1252
Cdd:COG1132  476 NLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQ 555
                        570
                 ....*....|....*....
gi 6755046  1253 GTHQQLLAQKGIYFSMVQA 1271
Cdd:COG1132  556 GTHEELLARGGLYARLYRL 574
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
1033-1272 1.43e-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: 458.16  E-value: 1.43e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1033 VKFNGVQFNYPTRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLG 1112
Cdd:cd03249    1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1113 IVSQEPILFDCSIAENIAYGDNSRAVshEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQP 1192
Cdd:cd03249   81 LVSQEPVLFDGTIAENIRYGKPDATD--EEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNP 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1193 HILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQKGIYFSMVQAG 1272
Cdd:cd03249  159 KILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
392-628 2.97e-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: 457.00  E-value: 2.97e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   392 EFKNVHFNYPSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIGV 471
Cdd:cd03249    2 EFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   472 VSQEPVLFATTIAENIRYGREDVTMDEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKIL 551
Cdd:cd03249   82 VSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKIL 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6755046   552 LLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREKGIYFKLVMTQ 628
Cdd:cd03249  162 LLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
ABC_6TM_Pgp_ABCB1 cd18558
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ...
50-364 1.77e-149

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: 452.89  E-value: 1.77e-149
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    50 MILGTLAAIIHGTLLPLLMLVFGNMTDSFTKAEASILPSitNQSGPNSTLIISNSsLEEEMAIYAYYYTGIGAGVLIVAY 129
Cdd:cd18558    1 MVVGILCAIIHGGLLPAFMVIFGDMTDSFTNGGMTNITG--NSSGLNSSAGPFEK-LEEEMTLYAYYYLIIGAIVLITAY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   130 IQVSLWCLAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDKIGMFFQSITTFLAGFIIGFIS 209
Cdd:cd18558   78 IQGSFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIR 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   210 GWKLTLVILAVSPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQKELERYNKNLEEAKNVGIK 289
Cdd:cd18558  158 GWKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIK 237
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6755046   290 KAITASISIGIAYLLVYASYALAFWYGTSLVLSNEYSIGEVLTVFFSILLGTFSIGHLAPNIEAFANARGAAFEI 364
Cdd:cd18558  238 KAITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGEVLTVFFSVLIGAFSAGQQVPSIEAFANARGAAYHI 312
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
120-629 3.32e-147

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: 462.00  E-value: 3.32e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   120 IGAGVLIVAYIQVSL-----WCLA-AGRQI-HKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDdVSKINDGI-GDKIGM 191
Cdd:COG2274  198 LAIGLLLALLFEGLLrllrsYLLLrLGQRIdLRLSSRFFRHLLRLPLSFFESRSVGDLASRFRD-VESIREFLtGSLLTA 276
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   192 FFQSITTFLAGFIIGFISgWKLTLVILAVSPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQK 271
Cdd:COG2274  277 LLDLLFVLIFLIVLFFYS-PPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESR 355
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   272 ELERYNKNLEEAKNVGIKKAITASISIGIAYLLVYASYALAFWYGTSLVLSNEYSIGEVLTvfFSILLGTF--SIGHLAP 349
Cdd:COG2274  356 FRRRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTLGQLIA--FNILSGRFlaPVAQLIG 433
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   350 NIEAFANARGAAFEIFKIIDNEPSIDSFSTKGyKPDSIMGNLEFKNVHFNYPSRSEvQILKGLNLKVKSGQTVALVGNSG 429
Cdd:COG2274  434 LLQRFQDAKIALERLDDILDLPPEREEGRSKL-SLPRLKGDIELENVSFRYPGDSP-PVLDNISLTIKPGERVAIVGRSG 511
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   430 CGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENIRYGREDVTMDEIEKAVKEANAY 509
Cdd:COG2274  512 SGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLH 591
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   510 DFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLS 589
Cdd:COG2274  592 DFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLS 671
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|
gi 6755046   590 TVRNADVIAGFDGGVIVEQGNHDELMREKGIYFKLVMTQT 629
Cdd:COG2274  672 TIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQQL 711
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
138-625 5.60e-141

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 445.71  E-value: 5.60e-141
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     138 AAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDKIGMFFQSITTFLAGFIIGFISGWKLTLVI 217
Cdd:TIGR00958  228 TMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTMVT 307
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     218 LAVSPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQKELERYNKNLEEAKNVGIKKAITASIS 297
Cdd:TIGR00958  308 LINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRKALAYAGY 387
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     298 IGIAYLLVYASYALAFWYGTSLVLSNEYSIGEVLtvffSILLGTFSIGHLAPNIEAFAN----ARGAAFEIFKIIDNEPS 373
Cdd:TIGR00958  388 LWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLV----SFLLYQEQLGEAVRVLSYVYSgmmqAVGASEKVFEYLDRKPN 463
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     374 IDSfsTKGYKPDSIMGNLEFKNVHFNYPSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSID 453
Cdd:TIGR00958  464 IPL--TGTLAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLD 541
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     454 GQDIRTINVRYLREIIGVVSQEPVLFATTIAENIRYGREDVTMDEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGG 533
Cdd:TIGR00958  542 GVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGG 621
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     534 QKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAalDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDE 613
Cdd:TIGR00958  622 QKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQ 699
                          490
                   ....*....|..
gi 6755046     614 LMREKGIYFKLV 625
Cdd:TIGR00958  700 LMEDQGCYKHLV 711
ABC_6TM_Pgp_ABCB1_D2_like cd18578
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ...
699-1016 6.17e-139

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: 425.33  E-value: 6.17e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   699 LNLNLSEWPYLLVGVLCAVINGCIQPVFAIVFSRIVGVFSRDDDHETKRQNcNLFSLFFLVMGLISFVTYFFQGFTFGKA 778
Cdd:cd18578    1 LKLNKPEWPLLLLGLIGAIIAGAVFPVFAILFSKLISVFSLPDDDELRSEA-NFWALMFLVLAIVAGIAYFLQGYLFGIA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   779 GEILTKRVRYMVFKSMLRQDISWFDDHKNSTGSLTTRLASDASSVKGAMGARLAVVTQNVANLGTGVILSLVYGWQLTLL 858
Cdd:cd18578   80 GERLTRRLRKLAFRAILRQDIAWFDDPENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLALV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   859 LVVIIPLIVLGGIIEMKLLSGQALKDKKQLEISGKIATEAIENFRTIVSLTREQKFETMYAQSLQVPYRNAMKKAHVFGI 938
Cdd:cd18578  160 GLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGL 239
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6755046   939 TFSFTQAMMYFSYAACFRFGAYLVAQQLMTFENVMLVFSAVVFGAMAAGNTSSFAPDYAKAKVSASHIIRIIEKTPEI 1016
Cdd:cd18578  240 GFGLSQSLTFFAYALAFWYGGRLVANGEYTFEQFFIVFMALIFGAQSAGQAFSFAPDIAKAKAAAARIFRLLDRKPEI 317
MsbA_rel TIGR02204
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ...
141-628 1.05e-134

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: 424.11  E-value: 1.05e-134
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     141 RQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDKIGMFFQSITTFLAGFIIGFISGWKLTLVILAV 220
Cdd:TIGR02204   88 RVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTSLVLLA 167
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     221 SPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQKELERYNKNLEEAKNVGIKKAITASISIGI 300
Cdd:TIGR02204  168 VPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVEKAYEAARQRIRTRALLTAI 247
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     301 AYLLVYASYALAFWYGTSLVLSNEYSIGEVLT-VFFSILLGTfSIGHLAPNIEAFANARGAAFEIFKIIDNEPSIDSFST 379
Cdd:TIGR02204  248 VIVLVFGAIVGVLWVGAHDVIAGKMSAGTLGQfVFYAVMVAG-SIGTLSEVWGELQRAAGAAERLIELLQAEPDIKAPAH 326
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     380 KGYKPDSIMGNLEFKNVHFNYPSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRT 459
Cdd:TIGR02204  327 PKTLPVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQ 406
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     460 INVRYLREIIGVVSQEPVLFATTIAENIRYGREDVTMDEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIA 539
Cdd:TIGR02204  407 LDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIA 486
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     540 IARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREKG 619
Cdd:TIGR02204  487 IARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGG 566

                   ....*....
gi 6755046     620 IYFKLVMTQ 628
Cdd:TIGR02204  567 LYARLARLQ 575
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
677-1270 7.11e-133

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: 423.86  E-value: 7.11e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   677 ERRLSMKEAVDEDVPLVSFWRILnlnLSEWPYLLVGVLCAVINGCIQ---PVFA-IVFSRIVGvfsrDDDHETKrqncNL 752
Cdd:COG2274  129 EPTPEFDKRGEKPFGLRWFLRLL---RRYRRLLLQVLLASLLINLLAlatPLFTqVVIDRVLP----NQDLSTL----WV 197
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   753 FSLFFLVMGLISFVTYFFQGFTFGKAGEILTKRVRYMVFKSMLRQDISWFDdhKNSTGSLTTRLaSDASSVKGAMGARLA 832
Cdd:COG2274  198 LAIGLLLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFE--SRSVGDLASRF-RDVESIREFLTGSLL 274
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   833 VVTQNVANLGTGVILSLVYGWQLTLLLVVIIPLIVLGGIIEMKLLsgqALKDKKQLEISGKIAT---EAIENFRTIVSLT 909
Cdd:COG2274  275 TALLDLLFVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRL---RRLSREESEASAKRQSllvETLRGIETIKALG 351
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   910 REQKFETMYAQsLQVPYRNAMKKAHVFGITFS-FTQAMMYFSYAACFRFGAYLVAQQLMTFenVMLV-FSAVVFGAMAA- 986
Cdd:COG2274  352 AESRFRRRWEN-LLAKYLNARFKLRRLSNLLStLSGLLQQLATVALLWLGAYLVIDGQLTL--GQLIaFNILSGRFLAPv 428
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   987 GNTSSFAPDYAKAKVSASHIIRIIEKTPEIDSYSTEGLKPTLlEGNVKFNGVQFNYPTRpNIPVLQGLSLEVKKGQTLAL 1066
Cdd:COG2274  429 AQLIGLLQRFQDAKIALERLDDILDLPPEREEGRSKLSLPRL-KGDIELENVSFRYPGD-SPPVLDNISLTIKPGERVAI 506
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1067 VGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAENIAYGDnsRAVSHEEIVRA 1146
Cdd:COG2274  507 VGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGD--PDATDEEIIEA 584
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1147 AKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCI 1226
Cdd:COG2274  585 ARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVI 664
                        570       580       590       600
                 ....*....|....*....|....*....|....*....|....
gi 6755046  1227 VIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQKGIYFSMVQ 1270
Cdd:COG2274  665 IIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQ 708
ABC_6TM_Pgp_ABCB1_D1_like cd18577
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ...
50-364 1.15e-128

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: 397.62  E-value: 1.15e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    50 MILGTLAAIIHGTLLPLLMLVFGNMTDSFTKaeasilpsitnqsgpNSTLIISNSSLEEEMAIYAYYYTGIGAGVLIVAY 129
Cdd:cd18577    1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFTD---------------FGSGESSPDEFLDDVNKYALYFVYLGIGSFVLSY 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   130 IQVSLWCLAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDKIGMFFQSITTFLAGFIIGFIS 209
Cdd:cd18577   66 IQTACWTITGERQARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIY 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   210 GWKLTLVILAVSPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQKELERYNKNLEEAKNVGIK 289
Cdd:cd18577  146 SWKLTLVLLATLPLIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIK 225
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6755046   290 KAITASISIGIAYLLVYASYALAFWYGTSLVLSNEYSIGEVLTVFFSILLGTFSIGHLAPNIEAFANARGAAFEI 364
Cdd:cd18577  226 KGLVSGLGLGLLFFIIFAMYALAFWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
681-1269 5.16e-127

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 408.34  E-value: 5.16e-127
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     681 SMKEAVDEDV---PLVsfWRILNLNLSEWPYLLVGVL---CAVINGCIQPVF-AIVFSRIVGVFSRDDdhetkrqncnlF 753
Cdd:TIGR00958  134 SEKEAEQGQSetaDLL--FRLLGLSGRDWPWLISAFVfltLSSLGEMFIPFYtGRVIDTLGGDKGPPA-----------L 200
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     754 SLFFLVMGLISFVTYFFQGF---TFGKAGEILTKRVRYMVFKSMLRQDISWFDDHKnsTGSLTTRLASDASSVKGAMGAR 830
Cdd:TIGR00958  201 ASAIFFMCLLSIASSVSAGLrggSFNYTMARINLRIREDLFRSLLRQDLGFFDENK--TGELTSRLSSDTQTMSRSLSLN 278
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     831 LAVVTQNVANLGTGVILSLVYGWQLTLLLVVIIPLIVLGGIIEMKLLsgQALKDKKQLEI--SGKIATEAIENFRTIVSL 908
Cdd:TIGR00958  279 VNVLLRNLVMLLGLLGFMLWLSPRLTMVTLINLPLVFLAEKVFGKRY--QLLSEELQEAVakANQVAEEALSGMRTVRSF 356
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     909 TRE----QKFETMYAQSLQVPYRNAMKKAhVFGITFSFTQAMMYFSYAACfrfGAYLVAQQLMTFEN-VMLVFSAVVFGA 983
Cdd:TIGR00958  357 AAEegeaSRFKEALEETLQLNKRKALAYA-GYLWTTSVLGMLIQVLVLYY---GGQLVLTGKVSSGNlVSFLLYQEQLGE 432
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     984 mAAGNTSSFAPDYAKAKVSASHIIRIIEKTPEIDSysTEGLKPTLLEGNVKFNGVQFNYPTRPNIPVLQGLSLEVKKGQT 1063
Cdd:TIGR00958  433 -AVRVLSYVYSGMMQAVGASEKVFEYLDRKPNIPL--TGTLAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEV 509
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    1064 LALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAENIAYGDNSraVSHEEI 1143
Cdd:TIGR00958  510 VALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTD--TPDEEI 587
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    1144 VRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEalDKAREGR 1223
Cdd:TIGR00958  588 MAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASR 665
                          570       580       590       600
                   ....*....|....*....|....*....|....*....|....*.
gi 6755046    1224 TCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQKGIYFSMV 1269
Cdd:TIGR00958  666 TVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
ABC_6TM_Pgp_ABCB1 cd18558
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ...
709-1006 8.64e-122

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: 379.70  E-value: 8.64e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   709 LLVGVLCAVINGCIQPVFAIVFSRIVGVF----------------SRDDDHETKRQNCNLFSLFFLVMGLISFVTYFFQG 772
Cdd:cd18558    1 MVVGILCAIIHGGLLPAFMVIFGDMTDSFtnggmtnitgnssglnSSAGPFEKLEEEMTLYAYYYLIIGAIVLITAYIQG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   773 FTFGKAGEILTKRVRYMVFKSMLRQDISWFDdhKNSTGSLTTRLASDASSVKGAMGARLAVVTQNVANLGTGVILSLVYG 852
Cdd:cd18558   81 SFWGLAAGRQTKKIRYKFFHAIMRQEIGWFD--VNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   853 WQLTLLLVVIIPLIVLGGIIEMKLLSGQALKDKKQLEISGKIATEAIENFRTIVSLTREQKFETMYAQSLQVPYRNAMKK 932
Cdd:cd18558  159 WKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKK 238
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6755046   933 AHVFGITFSFTQAMMYFSYAACFRFGAYLVAQQLM-TFENVMLVFSAVVFGAMAAGNTSSFAPdYAKAKVSASHI 1006
Cdd:cd18558  239 AITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYsIGEVLTVFFSVLIGAFSAGQQVPSIEA-FANARGAAYHI 312
MsbA_rel TIGR02204
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ...
737-1265 8.04e-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: 373.65  E-value: 8.04e-116
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     737 FSRDDDHETKRqncnLFSLFFLVMGLISFVTyFFQGFTFGKAGEILTKRVRYMVFKSMLRQDISWFDdhKNSTGSLTTRL 816
Cdd:TIGR02204   49 FSKDSSGLLNR----YFAFLLVVALVLALGT-AARFYLVTWLGERVVADIRRAVFAHLISLSPSFFD--KNRSGEVVSRL 121
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     817 ASDASSVKGAMGARLAVVTQNVANLGTGVILSLVYGWQLTLLLVVIIPLIVLGGIIEMKLLSGQALKDKKQLEISGKIAT 896
Cdd:TIGR02204  122 TTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAG 201
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     897 EAIENFRTIVSLTREQKFETMYAQSLQVPYRNAMKKAHVFGITFSFTQAMMYFSYAACFRFGAYLVAQQLMTF-ENVMLV 975
Cdd:TIGR02204  202 ETLGAIRTVQAFGHEDAERSRFGGAVEKAYEAARQRIRTRALLTAIVIVLVFGAIVGVLWVGAHDVIAGKMSAgTLGQFV 281
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     976 FSAVvFGAMAAGNTSSFAPDYAKAKVSASHIIRIIEKTPEIDSYSTEGLKPTLLEGNVKFNGVQFNYPTRPNIPVLQGLS 1055
Cdd:TIGR02204  282 FYAV-MVAGSIGTLSEVWGELQRAAGAAERLIELLQAEPDIKAPAHPKTLPVPLRGEIEFEQVNFAYPARPDQPALDGLN 360
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    1056 LEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAENIAYGdNS 1135
Cdd:TIGR02204  361 LTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYG-RP 439
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    1136 RAvSHEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEA 1215
Cdd:TIGR02204  440 DA-TDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQA 518
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|
gi 6755046    1216 LDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQKGIY 1265
Cdd:TIGR02204  519 LETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGGLY 568
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
126-630 4.59e-115

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: 371.36  E-value: 4.59e-115
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     126 IVAYIQVSLWCLAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDKIGMFFQSITTFLAGFII 205
Cdd:TIGR02203   69 ICSFVSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIV 148
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     206 GFISGWKLTLVILAVSPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQKELERYNKNLEEAKN 285
Cdd:TIGR02203  149 LLYYSWQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRR 228
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     286 VGIKKAITASISIGIAYLLVYASYALAFWYGTSLVLSNEYSIGEVLTVFFSILLGTFSIGHLApNIEA-FANARGAAFEI 364
Cdd:TIGR02203  229 LAMKMTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLT-NVNApMQRGLAAAESL 307
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     365 FKIIDNEPSIDsfsTKGYKPDSIMGNLEFKNVHFNYPSRsEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYD 444
Cdd:TIGR02203  308 FTLLDSPPEKD---TGTRAIERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYE 383
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     445 PLEGVVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENIRYGR-EDVTMDEIEKAVKEANAYDFIMKLPHQFDTLV 523
Cdd:TIGR02203  384 PDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRtEQADRAEIERALAAAYAQDFVDKLPLGLDTPI 463
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     524 GERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGG 603
Cdd:TIGR02203  464 GENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDG 543
                          490       500
                   ....*....|....*....|....*..
gi 6755046     604 VIVEQGNHDELMREKGIYFKLVMTQTR 630
Cdd:TIGR02203  544 RIVERGTHNELLARNGLYAQLHNMQFR 570
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
262-636 1.65e-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: 365.68  E-value: 1.65e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   262 TVIAFGGQQKELERYNKNLEEAKNVGIKKAITAS---------ISIGIAYLLVYASYAlafwygtslVLSNEYSIGEVlt 332
Cdd:COG5265  230 TVKYFGNEAREARRYDEALARYERAAVKSQTSLAllnfgqaliIALGLTAMMLMAAQG---------VVAGTMTVGDF-- 298
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   333 vffsILLGTFSIGHLAP-NIEAFANA--RGAAFEI---FKIIDNEPSIDSfstkgyKPDSIM-----GNLEFKNVHFNY- 400
Cdd:COG5265  299 ----VLVNAYLIQLYIPlNFLGFVYReiRQALADMermFDLLDQPPEVAD------APDAPPlvvggGEVRFENVSFGYd 368
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   401 PSRsevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIGVVSQEPVLFA 480
Cdd:COG5265  369 PER---PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFN 445
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   481 TTIAENIRYGREDVTMDEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSAL 560
Cdd:COG5265  446 DTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSAL 525
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6755046   561 DTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREKGIYFKLVMTQTRGNEIEP 636
Cdd:COG5265  526 DSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMWARQQEEEEAEE 601
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
132-628 3.93e-109

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 355.87  E-value: 3.93e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    132 VSLWCLA--AGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDD------------VSKINDG---IGDKIGMFFQ 194
Cdd:PRK11176   84 ISSYCISwvSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDseqvassssgalITVVREGasiIGLFIMMFYY 163
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    195 SittflagfiigfisgWKLTLVILAVSPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQKELE 274
Cdd:PRK11176  164 S---------------WQLSLILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETK 228
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    275 RYNKNLEEAKNVGIKKAITASISIGIAYLLvyASYALAFwygtSLVLSNEYSIGEVL-----TVFFSILlgtfsIGHLAP 349
Cdd:PRK11176  229 RFDKVSNRMRQQGMKMVSASSISDPIIQLI--ASLALAF----VLYAASFPSVMDTLtagtiTVVFSSM-----IALMRP 297
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    350 -----NIEA-FANARGAAFEIFKIIDNEPSIDsfsTKGYKPDSIMGNLEFKNVHFNYPSRsEVQILKGLNLKVKSGQTVA 423
Cdd:PRK11176  298 lksltNVNAqFQRGMAACQTLFAILDLEQEKD---EGKRVIERAKGDIEFRNVTFTYPGK-EVPALRNINFKIPAGKTVA 373
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    424 LVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENIRYGREDV-TMDEIEKA 502
Cdd:PRK11176  374 LVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIEEA 453
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    503 VKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTI 582
Cdd:PRK11176  454 ARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSL 533
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*.
gi 6755046    583 VIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREKGIYFKLVMTQ 628
Cdd:PRK11176  534 VIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQLHKMQ 579
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
694-1265 8.04e-109

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: 354.41  E-value: 8.04e-109
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     694 SFWRILNLNLSEWPYLLVGVLCAVINGCIQPVFAIVFSRIV-GVFSRDDDHETKRQNCNLFSLFfLVMGLISFVTYFFQG 772
Cdd:TIGR02203    1 TFRRLWSYVRPYKAGLVLAGVAMILVAATESTLAALLKPLLdDGFGGRDRSVLWWVPLVVIGLA-VLRGICSFVSTYLLS 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     773 FTFGKAgeILTKRVRymVFKSMLRQDISWFDdhKNSTGSLTTRLASDASSVKGAMGARLAVVTQNVANLGTGVILSLVYG 852
Cdd:TIGR02203   80 WVSNKV--VRDIRVR--MFEKLLGLPVSFFD--RQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYS 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     853 WQLTLLLVVIIPLIVLGGIIEMKLLSGQALKDKKQLEISGKIATEAIENFRTIVSLTREQKFETMYAQSLQVPYRNAMKK 932
Cdd:TIGR02203  154 WQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKM 233
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     933 AHVFGITFSFTQ-----AMMYFSYAACFRFGA-YLVAQQLMTFENVML-VFSAVvfgamaaGNTSSFAPDYAKAKVSASH 1005
Cdd:TIGR02203  234 TSAGSISSPITQliaslALAVVLFIALFQAQAgSLTAGDFTAFITAMIaLIRPL-------KSLTNVNAPMQRGLAAAES 306
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    1006 IIRIIEKTPEIDsysTEGLKPTLLEGNVKFNGVQFNYPTRpNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFY 1085
Cdd:TIGR02203  307 LFTLLDSPPEKD---TGTRAIERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFY 382
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    1086 DPMAGSVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAENIAYGDnSRAVSHEEIVRAAKEANIHQFIDSLPDKYNT 1165
Cdd:TIGR02203  383 EPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGR-TEQADRAEIERALAAAYAQDFVDKLPLGLDT 461
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    1166 RVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIE 1245
Cdd:TIGR02203  462 PIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMD 541
                          570       580
                   ....*....|....*....|
gi 6755046    1246 NGKVKEHGTHQQLLAQKGIY 1265
Cdd:TIGR02203  542 DGRIVERGTHNELLARNGLY 561
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
391-624 1.09e-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: 341.52  E-value: 1.09e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   391 LEFKNVHFNYPSRsEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIG 470
Cdd:cd03251    1 VEFKNVTFRYPGD-GPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   471 VVSQEPVLFATTIAENIRYGREDVTMDEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKI 550
Cdd:cd03251   80 LVSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6755046   551 LLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREKGIYFKL 624
Cdd:cd03251  160 LILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
1033-1265 2.01e-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: 340.75  E-value: 2.01e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1033 VKFNGVQFNYPTRPNiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLG 1112
Cdd:cd03251    1 VEFKNVTFRYPGDGP-PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1113 IVSQEPILFDCSIAENIAYGDnsRAVSHEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQP 1192
Cdd:cd03251   80 LVSQDVFLFNDTVAENIAYGR--PGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDP 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6755046  1193 HILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQKGIY 1265
Cdd:cd03251  158 PILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVY 230
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
391-624 6.02e-104

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: 328.42  E-value: 6.02e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   391 LEFKNVHFNY-PSRsevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREII 469
Cdd:cd03253    1 IEFENVTFAYdPGR---PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   470 GVVSQEPVLFATTIAENIRYGREDVTMDEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPK 549
Cdd:cd03253   78 GVVPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPP 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6755046   550 ILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREKGIYFKL 624
Cdd:cd03253  158 ILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEM 232
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
1008-1268 9.66e-104

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: 341.80  E-value: 9.66e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1008 RIIEKTPEI-DSYSTEGLKPTllEGNVKFNGVQFNYptRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD 1086
Cdd:COG5265  334 DLLDQPPEVaDAPDAPPLVVG--GGEVRFENVSFGY--DPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYD 409
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1087 PMAGSVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAENIAYGdnsRA-VSHEEIVRAAKEANIHQFIDSLPDKYNT 1165
Cdd:COG5265  410 VTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYG---RPdASEEEVEAAARAAQIHDFIESLPDGYDT 486
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1166 RVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIE 1245
Cdd:COG5265  487 RVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLE 566
                        250       260
                 ....*....|....*....|...
gi 6755046  1246 NGKVKEHGTHQQLLAQKGIYFSM 1268
Cdd:COG5265  567 AGRIVERGTHAELLAQGGLYAQM 589
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
138-619 5.33e-102

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: 335.57  E-value: 5.33e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   138 AAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDKIGMFFQSITTFLAGFIIGFISGWKLTLVI 217
Cdd:COG4988   85 AAARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPQLFLAALVPLLILVAVFPLDWLSGLIL 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   218 LAVSPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQKELERYNKNLEEAKnvgikkAIT---- 293
Cdd:COG4988  165 LVTAPLIPLFMILVGKGAAKASRRQWRALARLSGHFLDRLRGLTTLKLFGRAKAEAERIAEASEDFR------KRTmkvl 238
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   294 --ASISIGIAYLLVYASYALAFWY-GTSLvlsneysIGEVLTVF--FSILLgtfsighLAPniEAF-------------A 355
Cdd:COG4988  239 rvAFLSSAVLEFFASLSIALVAVYiGFRL-------LGGSLTLFaaLFVLL-------LAP--EFFlplrdlgsfyharA 302
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   356 NARGAAFEIFKIIDNEPSIDSFSTKGYKPDSImGNLEFKNVHFNYPSRSEVqiLKGLNLKVKSGQTVALVGNSGCGKSTT 435
Cdd:COG4988  303 NGIAAAEKIFALLDAPEPAAPAGTAPLPAAGP-PSIELEDVSFSYPGGRPA--LDGLSLTIPPGERVALVGPSGAGKSTL 379
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   436 VQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENIRYGREDVTMDEIEKAVKEANAYDFIMKL 515
Cdd:COG4988  380 LNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAAL 459
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   516 PHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNAD 595
Cdd:COG4988  460 PDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQAD 539
                        490       500
                 ....*....|....*....|....
gi 6755046   596 VIAGFDGGVIVEQGNHDELMREKG 619
Cdd:COG4988  540 RILVLDDGRIVEQGTHEELLAKNG 563
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
1033-1271 3.63e-100

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: 318.41  E-value: 3.63e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1033 VKFNGVQFNYPtrPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLG 1112
Cdd:cd03253    1 IEFENVTFAYD--PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1113 IVSQEPILFDCSIAENIAYGDNSraVSHEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQP 1192
Cdd:cd03253   79 VVPQDTVLFNDTIGYNIRYGRPD--ATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNP 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6755046  1193 HILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQKGIYFSMVQA 1271
Cdd:cd03253  157 PILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKA 235
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
389-619 8.40e-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: 316.86  E-value: 8.40e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   389 GNLEFKNVHFNYpsRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREI 468
Cdd:cd03254    1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   469 IGVVSQEPVLFATTIAENIRYGREDVTMDEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNP 548
Cdd:cd03254   79 IGVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDP 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6755046   549 KILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREKG 619
Cdd:cd03254  159 KILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
316-628 1.09e-98

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 327.30  E-value: 1.09e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    316 GTSLVLSNEYSIGEVLT-VFFSILLgtfsIGHLaPNIEAFAN----ARGAAFEIFKIIDNEPSIDSfstkgyKPDSI--- 387
Cdd:PRK13657  261 GAALVQKGQLRVGEVVAfVGFATLL----IGRL-DQVVAFINqvfmAAPKLEEFFEVEDAVPDVRD------PPGAIdlg 329
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    388 --MGNLEFKNVHFNYPSRSevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYL 465
Cdd:PRK13657  330 rvKGAVEFDDVSFSYDNSR--QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASL 407
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    466 REIIGVVSQEPVLFATTIAENIRYGREDVTMDEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALV 545
Cdd:PRK13657  408 RRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALL 487
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    546 RNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREKGIYFKLV 625
Cdd:PRK13657  488 KDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAALL 567

                  ...
gi 6755046    626 MTQ 628
Cdd:PRK13657  568 RAQ 570
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
1031-1263 1.44e-98

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: 313.78  E-value: 1.44e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1031 GNVKFNGVQFNYptRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAH 1110
Cdd:cd03254    1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1111 LGIVSQEPILFDCSIAENIAYGDNSraVSHEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVR 1190
Cdd:cd03254   79 IGVVLQDTFLFSGTIMENIRLGRPN--ATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLR 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6755046  1191 QPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQKG 1263
Cdd:cd03254  157 DPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
757-1265 5.74e-96

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 319.66  E-value: 5.74e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    757 FLVMGLI------SFVTYFFQGFTFGKageiLTKRVRYMVFKSMLRQDISWFDdhKNSTGSLTTRLASDASSVKGAMGAR 830
Cdd:PRK11176   69 LVVIGLMilrgitSFISSYCISWVSGK----VVMTMRRRLFGHMMGMPVSFFD--KQSTGTLLSRITYDSEQVASSSSGA 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    831 LAVVTQNVANLGTGVILSLVYGWQLTLLLVVIIPLIVlggiIEMKLLSG---------------------QALKDKKQLE 889
Cdd:PRK11176  143 LITVVREGASIIGLFIMMFYYSWQLSLILIVIAPIVS----IAIRVVSKrfrnisknmqntmgqvttsaeQMLKGHKEVL 218
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    890 ISGKIATEaIENFRTIVSLTREQKFETMYAQSLQVPyrnamkkahVFGITFSFtqAMMYFSYAAcfrfgaylvaqqlmTF 969
Cdd:PRK11176  219 IFGGQEVE-TKRFDKVSNRMRQQGMKMVSASSISDP---------IIQLIASL--ALAFVLYAA--------------SF 272
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    970 ENVMLVFSA----VVFGAMAA--------GNTSSfapDYAKAKVSASHIIRIIEKTPEIDsystEG-LKPTLLEGNVKFN 1036
Cdd:PRK11176  273 PSVMDTLTAgtitVVFSSMIAlmrplkslTNVNA---QFQRGMAACQTLFAILDLEQEKD----EGkRVIERAKGDIEFR 345
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1037 GVQFNYPTRpNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGIVSQ 1116
Cdd:PRK11176  346 NVTFTYPGK-EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQ 424
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1117 EPILFDCSIAENIAYGDNSRaVSHEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILL 1196
Cdd:PRK11176  425 NVHLFNDTIANNIAYARTEQ-YSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILI 503
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6755046   1197 LDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQKGIY 1265
Cdd:PRK11176  504 LDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVY 572
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
697-1263 1.47e-92

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: 309.77  E-value: 1.47e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   697 RILNLNLSEWPYLLVGVLCAVINGCIQPVFAIVFSRIV-GVFsrdDDHETKRQNCNLFSLFFLVMGLISFVTYFFQGFTF 775
Cdd:COG4988    7 RLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLaGLI---IGGAPLSALLPLLGLLLAVLLLRALLAWLRERAAF 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   776 gKAGEILTKRVRYMVFKSMLRQDISWFDDHknSTGSLTTRLasdassVKG--AMG---AR------LAVVTqnvanlgTG 844
Cdd:COG4988   84 -RAAARVKRRLRRRLLEKLLALGPAWLRGK--STGELATLL------TEGveALDgyfARylpqlfLAALV-------PL 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   845 VILSLVYG--WQLTLLLVVIIPLIVLGGIiemklLSGQALKDK--KQLEISGKIATEAIENFR---TIVSLTREQKF-ET 916
Cdd:COG4988  148 LILVAVFPldWLSGLILLVTAPLIPLFMI-----LVGKGAAKAsrRQWRALARLSGHFLDRLRgltTLKLFGRAKAEaER 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   917 MYAQSLQvpYRNA-MKkahVFGITF--SFT-QAMMYFSYAAC-FRFGAYLVAQQlMTFENVMLV-FSAVVFgamaagnts 990
Cdd:COG4988  223 IAEASED--FRKRtMK---VLRVAFlsSAVlEFFASLSIALVaVYIGFRLLGGS-LTLFAALFVlLLAPEF--------- 287
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   991 sFAP------DY---AKAKVSASHIIRIIEKTPEIDSYSTEGLkPTLLEGNVKFNGVQFNYPTRPniPVLQGLSLEVKKG 1061
Cdd:COG4988  288 -FLPlrdlgsFYharANGIAAAEKIFALLDAPEPAAPAGTAPL-PAAGPPSIELEDVSFSYPGGR--PALDGLSLTIPPG 363
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1062 QTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAENIAYGDnsRAVSHE 1141
Cdd:COG4988  364 ERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGR--PDASDE 441
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1142 EIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKARE 1221
Cdd:COG4988  442 ELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK 521
                        570       580       590       600
                 ....*....|....*....|....*....|....*....|..
gi 6755046  1222 GRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQKG 1263
Cdd:COG4988  522 GRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
138-624 2.54e-91

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: 306.31  E-value: 2.54e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   138 AAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVskindgigDKIGMFF---------QSITTFLAGFIIGFI 208
Cdd:COG4987   82 ATLRLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADV--------DALDNLYlrvllpllvALLVILAAVAFLAFF 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   209 SgWKLTLVILAVSPLIGLSSALWAKVLTSFTNKEL-QAYAKAGAVAEEVLAAIRTVIAFGGQQKELERYN---KNLEEAK 284
Cdd:COG4987  154 S-PALALVLALGLLLAGLLLPLLAARLGRRAGRRLaAARAALRARLTDLLQGAAELAAYGALDRALARLDaaeARLAAAQ 232
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   285 NvgiKKAITASISIGIAYLLVYASYALAFWYGTSLVLSNEYSiGEVLTVFFSILLGTFSIghLAPNIEAFAN---ARGAA 361
Cdd:COG4987  233 R---RLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALS-GPLLALLVLAALALFEA--LAPLPAAAQHlgrVRAAA 306
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   362 FEIFKIIDNEPSIDSFSTKGYKPDSimGNLEFKNVHFNYPSRSEvQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQR 441
Cdd:COG4987  307 RRLNELLDAPPAVTEPAEPAPAPGG--PSLELEDVSFRYPGAGR-PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLR 383
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   442 LYDPLEGVVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENIRYGREDVTMDEIEKAVKEANAYDFIMKLPHQFDT 521
Cdd:COG4987  384 FLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDT 463
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   522 LVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFD 601
Cdd:COG4987  464 WLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLE 543
                        490       500
                 ....*....|....*....|...
gi 6755046   602 GGVIVEQGNHDELMREKGIYFKL 624
Cdd:COG4987  544 DGRIVEQGTHEELLAQNGRYRQL 566
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
1024-1249 7.19e-89

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: 287.06  E-value: 7.19e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1024 LKPTLLEGNVKFNGVQFNYPTRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLN 1103
Cdd:cd03248    3 LAPDHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1104 VQWLRAHLGIVSQEPILFDCSIAENIAYGDNSraVSHEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIA 1183
Cdd:cd03248   83 HKYLHSKVSLVGQEPVLFARSLQDNIAYGLQS--CSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVA 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6755046  1184 IARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKV 1249
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 ...
149-629 3.41e-87

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: 298.58  E-value: 3.41e-87
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     149 KFFHAIMNQEIGWFDVHDVGELNTRLTDdVSKINDGIGDK-----IGMFFqsITTFLAgfIIGFISGwKLTLVILAVSPL 223
Cdd:TIGR01846  217 RLYRHLLGLPLGYFESRRVGDTVARVRE-LEQIRNFLTGSaltvvLDLLF--VVVFLA--VMFFYSP-TLTGVVIGSLVC 290
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     224 IGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQKELERYNKNLEEAKNVGIKKAITASISIGIAYL 303
Cdd:TIGR01846  291 YALLSVFVGPILRKRVEDKFERSAAATSFLVESVTGIETIKATATEPQFQNRWDRQLAAYVAASFRVTNLGNIAGQAIEL 370
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     304 LVYASYALAFWYGTSLVLSNEYSIGEVltVFFSILLGTFS--IGHLAPNIEAFANArGAAFEIFKIIDNEPSIDSFSTKG 381
Cdd:TIGR01846  371 IQKLTFAILLWFGAHLVIGGALSPGQL--VAFNMLAGRVTqpVLRLAQLWQDFQQT-GIALERLGDILNSPTEPRSAGLA 447
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     382 YKPDsIMGNLEFKNVHFNYPSRSEVqILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTIN 461
Cdd:TIGR01846  448 ALPE-LRGAITFENIRFRYAPDSPE-VLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIAD 525
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     462 VRYLREIIGVVSQEPVLFATTIAENIRYGREDVTMDEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIA 541
Cdd:TIGR01846  526 PAWLRRQMGVVLQENVLFSRSIRDNIALCNPGAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIA 605
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     542 RALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREKGIY 621
Cdd:TIGR01846  606 RALVGNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLY 685

                   ....*...
gi 6755046     622 FKLVMTQT 629
Cdd:TIGR01846  686 ARLWQQQS 693
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
785-1270 1.31e-86

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: 293.21  E-value: 1.31e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   785 RVRymVFKSMLRQDISWFddHKNSTGSLTTRLASDASSVKGAMgarLAVVTQNVANLGTGVILSLVYGW-QLTLLLVVII 863
Cdd:COG4987   91 RVR--LYRRLEPLAPAGL--ARLRSGDLLNRLVADVDALDNLY---LRVLLPLLVALLVILAAVAFLAFfSPALALVLAL 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   864 PLIVLGGIIemKLLSGQALK--DKKQLEISGKIATEAIENFRTIVSLT---REQKFETMYAQSLQVPYRNAMKKAHVFGI 938
Cdd:COG4987  164 GLLLAGLLL--PLLAARLGRraGRRLAAARAALRARLTDLLQGAAELAaygALDRALARLDAAEARLAAAQRRLARLSAL 241
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   939 TFSFTQAMMYFSYAACFRFGAYLVAQQlmTFENVMLVfsAVVFGAMAA----GNTSSFAPDYAKAKVSASHIIRIIEKTP 1014
Cdd:COG4987  242 AQALLQLAAGLAVVAVLWLAAPLVAAG--ALSGPLLA--LLVLAALALfealAPLPAAAQHLGRVRAAARRLNELLDAPP 317
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1015 EIDSYSTEGLKPTllEGNVKFNGVQFNYPTRPNiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFL 1094
Cdd:COG4987  318 AVTEPAEPAPAPG--GPSLELEDVSFRYPGAGR-PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITL 394
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1095 DGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAENIAYGDNsrAVSHEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQL 1174
Cdd:COG4987  395 GGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARP--DATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRL 472
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1175 SGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGT 1254
Cdd:COG4987  473 SGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGT 552
                        490
                 ....*....|....*.
gi 6755046  1255 HQQLLAQKGIYFSMVQ 1270
Cdd:COG4987  553 HEELLAQNGRYRQLYQ 568
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
391-628 2.20e-85

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: 277.83  E-value: 2.20e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   391 LEFKNVHFNYPSRSEVqILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIG 470
Cdd:cd03252    1 ITFEHVRFRYKPDGPV-ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   471 VVSQEPVLFATTIAENIRYGREDVTMDEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKI 550
Cdd:cd03252   80 VVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRI 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6755046   551 LLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREKGIYFKLVMTQ 628
Cdd:cd03252  160 LIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
ABC_6TM_Pgp_ABCB1_D2_like cd18578
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ...
46-374 6.98e-84

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: 276.64  E-value: 6.98e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    46 DKLCMILGTLAAIIHGTLLPLLMLVFGNMTDSFTkaeasilpsitnqsgpnstlIISNSSLEEEMAIYAYYYTGIGAGVL 125
Cdd:cd18578    7 EWPLLLLGLIGAIIAGAVFPVFAILFSKLISVFS--------------------LPDDDELRSEANFWALMFLVLAIVAG 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   126 IVAYIQVSLWCLAAGRQIHKIRQKFFHAIMNQEIGWFD--VHDVGELNTRLTDDVSKINDGIGDKIGMFFQSITTFLAGF 203
Cdd:cd18578   67 IAYFLQGYLFGIAGERLTRRLRKLAFRAILRQDIAWFDdpENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGL 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   204 IIGFISGWKLTLVILAVSPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQKELERYNKNLEEA 283
Cdd:cd18578  147 IIAFVYGWKLALVGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEP 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   284 KNVGIKKAITASISIGIAYLLVYASYALAFWYGTSLVLSNEYSIGEVLTVFFSILLGTFSIG---HLAPNIeafANARGA 360
Cdd:cd18578  227 LKKGLRRALISGLGFGLSQSLTFFAYALAFWYGGRLVANGEYTFEQFFIVFMALIFGAQSAGqafSFAPDI---AKAKAA 303
                        330
                 ....*....|....
gi 6755046   361 AFEIFKIIDNEPSI 374
Cdd:cd18578  304 AARIFRLLDRKPEI 317
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
384-605 1.84e-83

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: 272.04  E-value: 1.84e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   384 PDSIMGNLEFKNVHFNYPSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVR 463
Cdd:cd03248    5 PDHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHK 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   464 YLREIIGVVSQEPVLFATTIAENIRYGREDVTMDEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARA 543
Cdd:cd03248   85 YLHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARA 164
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6755046   544 LVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVI 605
Cdd:cd03248  165 LIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
ABC_membrane pfam00664
ABC transporter transmembrane region; This family represents a unit of six transmembrane ...
50-342 1.28e-82

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: 271.44  E-value: 1.28e-82
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046      50 MILGTLAAIIHGTLLPLLMLVFGNMTDSFTKaeasilpsitnqsgpnstliiSNSSLEEEMAIYAYYYTGIGAGVLIVAY 129
Cdd:pfam00664    1 LILAILLAILSGAISPAFPLVLGRILDVLLP---------------------DGDPETQALNVYSLALLLLGLAQFILSF 59
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     130 IQVSLWCLAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDKIGMFFQSITTFLAGFIIGFIS 209
Cdd:pfam00664   60 LQSYLLNHTGERLSRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYY 139
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     210 GWKLTLVILAVSPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQKELERYNKNLEEAKNVGIK 289
Cdd:pfam00664  140 GWKLTLVLLAVLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIK 219
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 6755046     290 KAITASISIGIAYLLVYASYALAFWYGTSLVLSNEYSIGE--VLTVFFSILLGTF 342
Cdd:pfam00664  220 KAVANGLSFGITQFIGYLSYALALWFGAYLVISGELSVGDlvAFLSLFAQLFGPL 274
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
847-1272 1.17e-81

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 279.92  E-value: 1.17e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    847 LSLVYGWQLTLLLVVI-IPLIVLGGIIEMKLLSGQALKDKKQLEISGKiATEAIENFRTIVSLTR-EQKFETM--YAQSL 922
Cdd:PRK13657  150 LALFMNWRLSLVLVVLgIVYTLITTLVMRKTKDGQAAVEEHYHDLFAH-VSDAIGNVSVVQSYNRiEAETQALrdIADNL 228
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    923 ---QVPYRNAMkkAHVFGIT-FSFTQAMMyfsyaACFRFGAYLVAQQLMTfenVMLVFSAVVFGAMAAG---NTSSFAPD 995
Cdd:PRK13657  229 laaQMPVLSWW--ALASVLNrAASTITML-----AILVLGAALVQKGQLR---VGEVVAFVGFATLLIGrldQVVAFINQ 298
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    996 YAKAKVSASHIIRIIEKTPEIDSysTEGLK-PTLLEGNVKFNGVQFNYPTRPniPVLQGLSLEVKKGQTLALVGSSGCGK 1074
Cdd:PRK13657  299 VFMAAPKLEEFFEVEDAVPDVRD--PPGAIdLGRVKGAVEFDDVSFSYDNSR--QGVEDVSFEAKPGQTVAIVGPTGAGK 374
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1075 STVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAENIAYGDNSraVSHEEIVRAAKEANIHQ 1154
Cdd:PRK13657  375 STLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPD--ATDEEMRAAAERAQAHD 452
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1155 FIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLST 1234
Cdd:PRK13657  453 FIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLST 532
                         410       420       430
                  ....*....|....*....|....*....|....*...
gi 6755046   1235 IQNADLIVVIENGKVKEHGTHQQLLAQKGIYFSMVQAG 1272
Cdd:PRK13657  533 VRNADRILVFDNGRVVESGSFDELVARGGRFAALLRAQ 570
NHLM_micro_ABC1 TIGR03796
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ...
694-1265 1.33e-81

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: 283.37  E-value: 1.33e-81
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     694 SFWRILNLNLSEWPYLLVGVLCAVINGCIQPVFAIVFSrivgvfsrddDHETKRQNCNLFSLFFLVMGLisfvTYFFQGF 773
Cdd:TIGR03796  144 ALWRRLRGSRGALLYLLLAGLLLVLPGLVIPAFSQIFV----------DEILVQGRQDWLRPLLLGMGL----TALLQGV 209
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     774 TFGKAGEILTKRVRYM-------VFKSMLRQDISWFDdhKNSTGSLTTRLASdASSVKGAMGARLAVVTQNVANLGTGVI 846
Cdd:TIGR03796  210 LTWLQLYYLRRLEIKLavgmsarFLWHILRLPVRFFA--QRHAGDIASRVQL-NDQVAEFLSGQLATTALDAVMLVFYAL 286
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     847 LSLVYGWQLTLLLVVI--IPLIVLGGIIEMKLLSGQALkdkkQLEiSGKIATEAIENFRTIVSLTRE-------QKFETM 917
Cdd:TIGR03796  287 LMLLYDPVLTLIGIAFaaINVLALQLVSRRRVDANRRL----QQD-AGKLTGVAISGLQSIETLKASglesdffSRWAGY 361
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     918 YAQSLqvpyrNAMKKAHVFGITFS-FTQAMMYFSYAACFRFGAYLVAQQLMT------FENVMLVFSAVVFGAMAAGNT- 989
Cdd:TIGR03796  362 QAKLL-----NAQQELGVLTQILGvLPTLLTSLNSALILVVGGLRVMEGQLTigmlvaFQSLMSSFLEPVNNLVGFGGTl 436
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     990 SSFAPDYAKAKVSASHIIRIIEKTPEIDSYSTEglKPTLLEGNVKFNGVQFNYpTRPNIPVLQGLSLEVKKGQTLALVGS 1069
Cdd:TIGR03796  437 QELEGDLNRLDDVLRNPVDPLLEEPEGSAATSE--PPRRLSGYVELRNITFGY-SPLEPPLIENFSLTLQPGQRVALVGG 513
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    1070 SGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAENIAYGDNSraVSHEEIVRAAKE 1149
Cdd:TIGR03796  514 SGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLWDPT--IPDADLVRACKD 591
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    1150 ANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALdkAREGRTCIVIA 1229
Cdd:TIGR03796  592 AAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNL--RRRGCTCIIVA 669
                          570       580       590
                   ....*....|....*....|....*....|....*.
gi 6755046    1230 HRLSTIQNADLIVVIENGKVKEHGTHQQLLAQKGIY 1265
Cdd:TIGR03796  670 HRLSTIRDCDEIIVLERGKVVQRGTHEELWAVGGAY 705
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
391-603 3.91e-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: 260.39  E-value: 3.91e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   391 LEFKNVHFNYPSRsEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIG 470
Cdd:cd03228    1 IEFKNVSFSYPGR-PKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   471 VVSQEPVLFATTIAENIrygredvtmdeiekavkeanaydfimklphqfdtlvgergaqLSGGQKQRIAIARALVRNPKI 550
Cdd:cd03228   80 YVPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPI 117
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 6755046   551 LLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGG 603
Cdd:cd03228  118 LILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
1033-1270 4.87e-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: 262.81  E-value: 4.87e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1033 VKFNGVQFNYptRPNIP-VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHL 1111
Cdd:cd03252    1 ITFEHVRFRY--KPDGPvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1112 GIVSQEPILFDCSIAENIAYGDNsrAVSHEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQ 1191
Cdd:cd03252   79 GVVLQENVLFNRSIRDNIALADP--GMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHN 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6755046  1192 PHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQKGIYFSMVQ 1270
Cdd:cd03252  157 PRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQ 235
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
1033-1248 2.39e-79

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: 258.08  E-value: 2.39e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1033 VKFNGVQFNYPTRPNiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLG 1112
Cdd:cd03228    1 IEFKNVSFSYPGRPK-PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1113 IVSQEPILFDCSIAENIaygdnsravsheeivraakeanihqfidslpdkyntrvgdkgtqLSGGQKQRIAIARALVRQP 1192
Cdd:cd03228   80 YVPQDPFLFSGTIRENI--------------------------------------------LSGGQRQRIAIARALLRDP 115
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 6755046  1193 HILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGK 1248
Cdd:cd03228  116 PILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
chvA TIGR01192
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ...
194-627 8.75e-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: 268.68  E-value: 8.75e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     194 QSITTFLAGFII---GFISGWKLTLVilavspLIGLSSALW--AKVLTSFTnKELQA-----YAKAGAVAEEVLAAIRTV 263
Cdd:TIGR01192  136 QHLATFVALFLLiptAFAMDWRLSIV------LMVLGILYIliAKLVMQRT-KNGQAavehhYHNVFKHVSDSISNVSVV 208
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     264 IAFG---GQQKELERYNKNLEEAKNVGIKKAITASisiGIAYLLVYASYALAFWYGTSLVLSNEYSIGEVLT-VFFSILL 339
Cdd:TIGR01192  209 HSYNrieAETSALKQFTNNLLSAQYPVLDWWALAS---GLNRMASTISMMCILVIGTVLVIKGELSVGEVIAfIGFANLL 285
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     340 gtfsIGHLaPNIEAFAN----ARGAAFEIFKIID-----NEPSiDSFSTKGYKpdsimGNLEFKNVHFNYPSRSevQILK 410
Cdd:TIGR01192  286 ----IGRL-DQMSGFITqifeARAKLEDFFDLEDsvfqrEEPA-DAPELPNVK-----GAVEFRHITFEFANSS--QGVF 352
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     411 GLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENIRYG 490
Cdd:TIGR01192  353 DVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESLRKSIATVFQDAGLFNRSIRENIRLG 432
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     491 REDVTMDEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQA 570
Cdd:TIGR01192  433 REGATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIARAILKNAPILVLDEATSALDVETEARVKN 512
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 6755046     571 ALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREKGIYFKLVMT 627
Cdd:TIGR01192  513 AIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQKDGRFYKLLRR 569
ABC_6TM_Pgp_ABCB1_D1_like cd18577
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ...
709-1006 2.21e-76

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: 255.09  E-value: 2.21e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   709 LLVGVLCAVINGCIQPVFAIVFSRIVGVFSR----DDDHETKRQNCNLFSLFFLVMGLISFVTYFFQGFTFGKAGEILTK 784
Cdd:cd18577    1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFTDfgsgESSPDEFLDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQAR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   785 RVRYMVFKSMLRQDISWFDdhKNSTGSLTTRLASDASSVKGAMGARLAVVTQNVANLGTGVILSLVYGWQLTLLLVVIIP 864
Cdd:cd18577   81 RIRKRYLKALLRQDIAWFD--KNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLP 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   865 LIVLGGIIEMKLLSGQALKDKKQLEISGKIATEAIENFRTIVSLTREQKFETMYAQSLQVPYRNAMKKAHVFGITFSFTQ 944
Cdd:cd18577  159 LIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLF 238
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6755046   945 AMMYFSYAACFRFGAYLVAQQLMTFENVMLVFSAVVFGAMAAGNTSSFAPDYAKAKVSASHI 1006
Cdd:cd18577  239 FIIFAMYALAFWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
NHLM_micro_ABC2 TIGR03797
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ...
794-1270 4.24e-76

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: 266.82  E-value: 4.24e-76
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     794 MLRQDISWFDDHknSTGSLTTRlasdASSVKgAMGARLAVVTQNVANLGTGVILSLV----YGWQLTLLLVVIIPLIVLG 869
Cdd:TIGR03797  219 LLRLPVSFFRQY--STGDLASR----AMGIS-QIRRILSGSTLTTLLSGIFALLNLGlmfyYSWKLALVAVALALVAIAV 291
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     870 -GIIEMKLLSgqalKDKKQLEISGKIATEAIENFRTIVSLtR----EQKFETMYAQ--SLQVpyRNAMKKAHVFGITFSF 942
Cdd:TIGR03797  292 tLVLGLLQVR----KERRLLELSGKISGLTVQLINGISKL-RvagaENRAFARWAKlfSRQR--KLELSAQRIENLLTVF 364
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     943 TQAMMYFSYAACFRFGAYLVAQQLMTFENVMLVFSAvvFGAMAAGNTS---------SFAPDYAKAKvsashiiRIIEKT 1013
Cdd:TIGR03797  365 NAVLPVLTSAALFAAAISLLGGAGLSLGSFLAFNTA--FGSFSGAVTQlsntlisilAVIPLWERAK-------PILEAL 435
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    1014 PEIDSYSTEglkPTLLEGNVKFNGVQFNYptRPNIP-VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSV 1092
Cdd:TIGR03797  436 PEVDEAKTD---PGKLSGAIEVDRVTFRY--RPDGPlILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSV 510
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    1093 FLDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAENIAyGDNSraVSHEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGT 1172
Cdd:TIGR03797  511 FYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIA-GGAP--LTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGG 587
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    1173 QLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRtcIVIAHRLSTIQNADLIVVIENGKVKEH 1252
Cdd:TIGR03797  588 TLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERLKVTR--IVIAHRLSTIRNADRIYVLDAGRVVQQ 665
                          490
                   ....*....|....*...
gi 6755046    1253 GTHQQLLAQKGIYFSMVQ 1270
Cdd:TIGR03797  666 GTYDELMAREGLFAQLAR 683
type_I_sec_HlyB TIGR01846
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ...
1029-1270 6.35e-74

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: 260.83  E-value: 6.35e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    1029 LEGNVKFNGVQFNYptRPNIP-VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWL 1107
Cdd:TIGR01846  452 LRGAITFENIRFRY--APDSPeVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWL 529
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    1108 RAHLGIVSQEPILFDCSIAENIAYGDNsrAVSHEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARA 1187
Cdd:TIGR01846  530 RRQMGVVLQENVLFSRSIRDNIALCNP--GAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARA 607
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    1188 LVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQKGIYFS 1267
Cdd:TIGR01846  608 LVGNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYAR 687

                   ...
gi 6755046    1268 MVQ 1270
Cdd:TIGR01846  688 LWQ 690
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
709-1246 3.03e-71

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 262.66  E-value: 3.03e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    709 LLVGVLCAVINGCIQPVFAIVFSRIVGVFSRDDDhetkrQNCNLFSLffLVMGLISFVTYFFQGFTFGKAGEILTKRVRY 788
Cdd:PTZ00265   62 LGVSFVCATISGGTLPFFVSVFGVIMKNMNLGEN-----VNDIIFSL--VLIGIFQFILSFISSFCMDVVTTKILKTLKL 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    789 MVFKSMLRQDISWfddHKNSTGS-LTTRLASDASSVKGAMGAR-LAVVTQNVANLGTgVILSLVYGWQLTLLLVVIIPLI 866
Cdd:PTZ00265  135 EFLKSVFYQDGQF---HDNNPGSkLTSDLDFYLEQVNAGIGTKfITIFTYASAFLGL-YIWSLFKNARLTLCITCVFPLI 210
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    867 VLGGIIEMKLLSgqaLKDKKQLEISGK---IATEAIENFRTIVSLTRE----QKF---ETMYAQSLQVPyrNAMKKAHVf 936
Cdd:PTZ00265  211 YICGVICNKKVK---INKKTSLLYNNNtmsIIEEALVGIRTVVSYCGEktilKKFnlsEKLYSKYILKA--NFMESLHI- 284
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    937 GITFSFTQAmmyfSYAACFRFGAYLVAQQLMTFENVMLVFSAVVFGAMAAGNTSSFA--------PDYAKAKVSASHIIR 1008
Cdd:PTZ00265  285 GMINGFILA----SYAFGFWYGTRIIISDLSNQQPNNDFHGGSVISILLGVLISMFMltiilpniTEYMKSLEATNSLYE 360
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1009 IIEKTPEIDSySTEGLKPTLLEgNVKFNGVQFNYPTRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPM 1088
Cdd:PTZ00265  361 IINRKPLVEN-NDDGKKLKDIK-KIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPT 438
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1089 AGSVFL-DGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAENIAY------------------------GDNSR------- 1136
Cdd:PTZ00265  439 EGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYslyslkdlealsnyynedgndsqeNKNKRnscrakc 518
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1137 ------------------------AVSHEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQP 1192
Cdd:PTZ00265  519 agdlndmsnttdsneliemrknyqTIKDSEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNP 598
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 6755046   1193 HILLLDEATSALDTESEKVVQEALD--KAREGRTCIVIAHRLSTIQNADLIVVIEN 1246
Cdd:PTZ00265  599 KILILDEATSSLDNKSEYLVQKTINnlKGNENRITIIIAHRLSTIRYANTIFVLSN 654
ABC_membrane pfam00664
ABC transporter transmembrane region; This family represents a unit of six transmembrane ...
709-984 3.64e-70

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: 236.39  E-value: 3.64e-70
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     709 LLVGVLCAVINGCIQPVFAIVFSRIVGVFSRDDDHETkrQNCNLFSLFFLVMGLISFVTYFFQGFTFGKAGEILTKRVRY 788
Cdd:pfam00664    1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPET--QALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRR 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     789 MVFKSMLRQDISWFDdhKNSTGSLTTRLASDASSVKGAMGARLAVVTQNVANLGTGVILSLVYGWQLTLLLVVIIPLIVL 868
Cdd:pfam00664   79 KLFKKILRQPMSFFD--TNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYIL 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     869 GGIIEMKLLSGQALKDKKQLEISGKIATEAIENFRTIVSLTREQKFETMYAQSLQVPYRNAMKKAHVFGITFSFTQAMMY 948
Cdd:pfam00664  157 VSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGY 236
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 6755046     949 FSYAACFRFGAYLVAQQLMTFEN--VMLVFSAVVFGAM 984
Cdd:pfam00664  237 LSYALALWFGAYLVISGELSVGDlvAFLSLFAQLFGPL 274
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
389-609 2.06e-69

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: 232.09  E-value: 2.06e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   389 GNLEFKNVHFNYPSrSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREI 468
Cdd:cd03245    1 GRIEFRNVSFSYPN-QEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   469 IGVVSQEPVLFATTIAENIRYGREDVTMDEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNP 548
Cdd:cd03245   80 IGYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDP 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6755046   549 KILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQG 609
Cdd:cd03245  160 PILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
1031-1249 2.78e-69

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: 231.71  E-value: 2.78e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1031 GNVKFNGVQFNYPTRPnIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAH 1110
Cdd:cd03245    1 GRIEFRNVSFSYPNQE-IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1111 LGIVSQEPILFDCSIAENIAYGDnsRAVSHEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVR 1190
Cdd:cd03245   80 IGYVPQDVTLFYGTLRDNITLGA--PLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLN 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 6755046  1191 QPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKV 1249
Cdd:cd03245  158 DPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
371-1270 9.37e-69

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: 254.87  E-value: 9.37e-69
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     371 EPsiDSFSTKGYKPDSimGN-LEFKNVHFNYpSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGV 449
Cdd:TIGR00957  620 EP--DSIERRTIKPGE--GNsITVHNATFTW-ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGH 694
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     450 VSIDGqdirtiNVRYlreiigvVSQEPVLFATTIAENIRYGREdvTMDEIEKAVKEANAY--DFIMkLPHQFDTLVGERG 527
Cdd:TIGR00957  695 VHMKG------SVAY-------VPQQAWIQNDSLRENILFGKA--LNEKYYQQVLEACALlpDLEI-LPSGDRTEIGEKG 758
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     528 AQLSGGQKQRIAIARALVRNPKILLLDEATSALDTEseaVVQAALDKA------REGRTTIVIAHRLSTVRNADVIAGFD 601
Cdd:TIGR00957  759 VNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAH---VGKHIFEHVigpegvLKNKTRILVTHGISYLPQVDVIIVMS 835
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     602 GGVIVEQGNHDELMREKGIYFKLVMTQTRGNE---IEPGNNAYGSQSDTDASELTSEESKSPLIRRSIYR----SVHRKQ 674
Cdd:TIGR00957  836 GGKISEMGSYQELLQRDGAFAEFLRTYAPDEQqghLEDSWTALVSGEGKEAKLIENGMLVTDVVGKQLQRqlsaSSSDSG 915
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     675 DQERRLSMKEAVDEDVPLVSFWRILNLNLSE---------WPYLLVGVLCAVINGCI----QPVFAIVFSRIVGVFSRDD 741
Cdd:TIGR00957  916 DQSRHHGSSAELQKAEAKEETWKLMEADKAQtgqvelsvyWDYMKAIGLFITFLSIFlfvcNHVSALASNYWLSLWTDDP 995
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     742 DHETKRQNCNLFSLFFLVMGLISFVTYFFQGFTFGKAGEILTKRVRYMVFKSMLRQDISWFDdhKNSTGSLTTRLASDAS 821
Cdd:TIGR00957  996 MVNGTQNNTSLRLSVYGALGILQGFAVFGYSMAVSIGGIQASRVLHQDLLHNKLRSPMSFFE--RTPSGNLVNRFSKELD 1073
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     822 SVKGAMGARLAVVTQNVANLGTGVILSLVygwQLTLLLVVIIPLIVLGGIIE-MKLLSGQALKDKKQLEISGKIA--TEA 898
Cdd:TIGR00957 1074 TVDSMIPPVIKMFMGSLFNVIGALIVILL---ATPIAAVIIPPLGLLYFFVQrFYVASSRQLKRLESVSRSPVYShfNET 1150
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     899 IENFRTIVSLTREQKFEtmYAQSLQVpyrNAMKKAhvfgitfsftqammYFSYAACFRFgaylVAQQLMTFENVMLVFSA 978
Cdd:TIGR00957 1151 LLGVSVIRAFEEQERFI--HQSDLKV---DENQKA--------------YYPSIVANRW----LAVRLECVGNCIVLFAA 1207
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     979 VvfgaMAAGNTSSFAPDYAKAKVSAS--------HIIRI-------IEKTPEIDSYS-TEGLKPTLLE-----------G 1031
Cdd:TIGR00957 1208 L----FAVISRHSLSAGLVGLSVSYSlqvtfylnWLVRMssemetnIVAVERLKEYSeTEKEAPWQIQetappsgwpprG 1283
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    1032 NVKFNGVQFNYptRPNIP-VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAH 1110
Cdd:TIGR00957 1284 RVEFRNYCLRY--REDLDlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFK 1361
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    1111 LGIVSQEPILFDCSIAENIaygDNSRAVSHEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVR 1190
Cdd:TIGR00957 1362 ITIIPQDPVLFSGSLRMNL---DPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLR 1438
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    1191 QPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQKGIYFSMVQ 1270
Cdd:TIGR00957 1439 KTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSMAK 1518
NHLM_micro_ABC2 TIGR03797
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ...
160-628 6.32e-68

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: 242.94  E-value: 6.32e-68
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     160 GWFDVHDVGELNTRlTDDVSKINDGIGDKIgmffqsITTFLAGFI----IG--FISGWKLTLV---ILAVSPLIGLSSAL 230
Cdd:TIGR03797  225 SFFRQYSTGDLASR-AMGISQIRRILSGST------LTTLLSGIFallnLGlmFYYSWKLALVavaLALVAIAVTLVLGL 297
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     231 WAkvltsfTNKELQAYAKAGAVAEEVLAAIRTVIAF---GGQQKELERYNKNLEEAKNVGIKKAITASI-SIGIAYLLVY 306
Cdd:TIGR03797  298 LQ------VRKERRLLELSGKISGLTVQLINGISKLrvaGAENRAFARWAKLFSRQRKLELSAQRIENLlTVFNAVLPVL 371
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     307 ASYALaFWYGTSLVLSNEYSIGEVLTvfFSILLGTFSIGhlapnIEAFANARGAAFEIF-------KIIDNEPSIDSFST 379
Cdd:TIGR03797  372 TSAAL-FAAAISLLGGAGLSLGSFLA--FNTAFGSFSGA-----VTQLSNTLISILAVIplwerakPILEALPEVDEAKT 443
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     380 KgykPDSIMGNLEFKNVHFNYPSRSEvQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRT 459
Cdd:TIGR03797  444 D---PGKLSGAIEVDRVTFRYRPDGP-LILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAG 519
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     460 INVRYLREIIGVVSQEPVLFATTIAENIrYGREDVTMDEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIA 539
Cdd:TIGR03797  520 LDVQAVRRQLGVVLQNGRLMSGSIFENI-AGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLL 598
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     540 IARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRttIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREKG 619
Cdd:TIGR03797  599 IARALVRKPRILLFDEATSALDNRTQAIVSESLERLKVTR--IVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREG 676

                   ....*....
gi 6755046     620 IYFKLVMTQ 628
Cdd:TIGR03797  677 LFAQLARRQ 685
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
190-597 2.43e-66

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: 234.10  E-value: 2.43e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     190 GMFFQSITTFLAGFIIGFISgWKLTLVILAVSPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFG-- 267
Cdd:TIGR02857  124 QLVLAVIVPLAILAAVFPQD-WISGLILLLTAPLIPIFMILIGWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLFGra 202
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     268 -GQQKELERYNKNLEEAKNVGIKKAITASI------SIGIAYLLVYasyalafwYGTSLVlsneysiGEVLTVF--FSIL 338
Cdd:TIGR02857  203 kAQAAAIRRSSEEYRERTMRVLRIAFLSSAvlelfaTLSVALVAVY--------IGFRLL-------AGDLDLAtgLFVL 267
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     339 LgtfsighLAPniEAF-------------ANARGAAFEIFKIIDNEPSIdsFSTKGYKPDSIMGNLEFKNVHFNYPSRSE 405
Cdd:TIGR02857  268 L-------LAP--EFYlplrqlgaqyharADGVAAAEALFAVLDAAPRP--LAGKAPVTAAPASSLEFSGVSVAYPGRRP 336
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     406 VqiLKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTIAE 485
Cdd:TIGR02857  337 A--LRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAE 414
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     486 NIRYGREDVTMDEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESE 565
Cdd:TIGR02857  415 NIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETE 494
                          410       420       430
                   ....*....|....*....|....*....|..
gi 6755046     566 AVVQAALDKAREGRTTIVIAHRLSTVRNADVI 597
Cdd:TIGR02857  495 AEVLEALRALAQGRTVLLVTHRLALAALADRI 526
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
389-610 1.63e-65

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: 220.83  E-value: 1.63e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   389 GNLEFKNVHFNYPSRSEVqILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREI 468
Cdd:cd03244    1 GDIEFKNVSLRYRPNLPP-VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   469 IGVVSQEPVLFATTIAENI----RYgredvTMDEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARAL 544
Cdd:cd03244   80 ISIIPQDPVLFSGTIRSNLdpfgEY-----SDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARAL 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6755046   545 VRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGN 610
Cdd:cd03244  155 LRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
1030-1261 1.81e-65

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: 232.72  E-value: 1.81e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1030 EGNVKFNGVQFNYPTRPNiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRA 1109
Cdd:COG4618  328 KGRLSVENLTVVPPGSKR-PILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGR 406
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1110 HLGIVSQEPILFDCSIAENIA-YGDnsraVSHEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARAL 1188
Cdd:COG4618  407 HIGYLPQDVELFDGTIAENIArFGD----ADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARAL 482
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6755046  1189 VRQPHILLLDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQ 1261
Cdd:COG4618  483 YGDPRLVVLDEPNSNLDDEGEAALAAAIRALKArGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
1031-1254 5.98e-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: 216.59  E-value: 5.98e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1031 GNVKFNGVQFNYptRPNI-PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRA 1109
Cdd:cd03244    1 GDIEFKNVSLRY--RPNLpPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1110 HLGIVSQEPILFDCSIAENIA----YGDnsravshEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIA 1185
Cdd:cd03244   79 RISIIPQDPVLFSGTIRSNLDpfgeYSD-------EELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLA 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6755046  1186 RALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGT 1254
Cdd:cd03244  152 RALLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
134-621 6.86e-64

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


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 228.44  E-value: 6.86e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    134 LWCLAAGRQIH-KIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDKIGMFFQSITTFLAGFIIGFIS-GW 211
Cdd:PRK10789   58 VLLFGASYQLAvELREDFYRQLSRQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVMGCAVLIVMSTQiSW 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    212 KLTLVILAVSPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQKELERYNKNLEEA--KNVGIK 289
Cdd:PRK10789  138 QLTLLALLPMPVMAIMIKRYGDQLHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTgkKNMRVA 217
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    290 KA-----ITASISIGIAYLLvyasyalAFWYGTSLVLSNEYSIGEvLTVFFsILLGTFSIGHLAP----NIEAfanaRGA 360
Cdd:PRK10789  218 RIdarfdPTIYIAIGMANLL-------AIGGGSWMVVNGSLTLGQ-LTSFV-MYLGLMIWPMLALawmfNIVE----RGS 284
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    361 AF--EIFKIIDNEPSIDSfstkGYKP-DSIMGNLEFKNVHFNYPsRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQ 437
Cdd:PRK10789  285 AAysRIRAMLAEAPVVKD----GSEPvPEGRGELDVNIRQFTYP-QTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLS 359
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    438 LMQRLYDPLEGVVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENIRYGREDVTMDEIEKAVKEANAYDFIMKLPH 517
Cdd:PRK10789  360 LIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQ 439
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    518 QFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVI 597
Cdd:PRK10789  440 GYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEI 519
                         490       500
                  ....*....|....*....|....
gi 6755046    598 AGFDGGVIVEQGNHDELMREKGIY 621
Cdd:PRK10789  520 LVMQHGHIAQRGNHDQLAQQSGWY 543
PLN03232 PLN03232
ABC transporter C family member; Provisional
391-1271 6.68e-63

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 236.03  E-value: 6.68e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    391 LEFKNVHFNYPSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEgVVSIDgqdirtinvryLREIIG 470
Cdd:PLN03232  615 ISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAE-TSSVV-----------IRGSVA 682
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    471 VVSQEPVLFATTIAENIRYGrEDVTMDEIEKAVKeanaydfIMKLPHQFD-------TLVGERGAQLSGGQKQRIAIARA 543
Cdd:PLN03232  683 YVPQVSWIFNATVRENILFG-SDFESERYWRAID-------VTALQHDLDllpgrdlTEIGERGVNISGGQKQRVSMARA 754
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    544 LVRNPKILLLDEATSALDTE-SEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREkGIYF 622
Cdd:PLN03232  755 VYSNSDIYIFDDPLSALDAHvAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKS-GSLF 833
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    623 KLVMtqtrgneiEPGNNAYGSQSDTDASELTSEESKSPLIRRSIYRSVHRKQDQERRLSMKEAVDEDVPLVSfWRIL--- 699
Cdd:PLN03232  834 KKLM--------ENAGKMDATQEVNTNDENILKLGPTVTIDVSERNLGSTKQGKRGRSVLVKQEERETGIIS-WNVLmry 904
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    700 NLNLSEWPYLLVGVLCAVINgciqPVFAIVFSRIVGVFSRDDDHETKRQncnlfSLFFLVMGLISF----VTyFFQGFTF 775
Cdd:PLN03232  905 NKAVGGLWVVMILLVCYLTT----EVLRVSSSTWLSIWTDQSTPKSYSP-----GFYIVVYALLGFgqvaVT-FTNSFWL 974
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    776 GKAGEILTKRVRYMVFKSMLRQDISWFddHKNSTGSLTTRLASDASSVKgamgarlavvtQNVANLGTGVILSLvygWQL 855
Cdd:PLN03232  975 ISSSLHAAKRLHDAMLNSILRAPMLFF--HTNPTGRVINRFSKDIGDID-----------RNVANLMNMFMNQL---WQL 1038
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    856 --TLLLVVIIPLIVLGGIIEMKLLSGQAL-------KDKKQLEISGKIAT-----EAIENFRTIVSLTREQKFETMYAQS 921
Cdd:PLN03232 1039 lsTFALIGTVSTISLWAIMPLLILFYAAYlyyqstsREVRRLDSVTRSPIyaqfgEALNGLSSIRAYKAYDRMAKINGKS 1118
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    922 LQVPYRNAMKKAHVFG---ITFSFTQAMMYFSYA--ACFRFG--------AYLVAQQLMTFENVMLVFSAVVFGAMAAGN 988
Cdd:PLN03232 1119 MDNNIRFTLANTSSNRwltIRLETLGGVMIWLTAtfAVLRNGnaenqagfASTMGLLLSYTLNITTLLSGVLRQASKAEN 1198
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    989 TSSFAPDYAKAKVSASHIIRIIEKTPEIDSYSTEGLkptllegnVKFNGVQFNYptRPNIP-VLQGLSLEVKKGQTLALV 1067
Cdd:PLN03232 1199 SLNSVERVGNYIDLPSEATAIIENNRPVSGWPSRGS--------IKFEDVHLRY--RPGLPpVLHGLSFFVSPSEKVGVV 1268
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1068 GSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAENI-AYGDNSRAvsheEIVRA 1146
Cdd:PLN03232 1269 GRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIdPFSEHNDA----DLWEA 1344
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1147 AKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCI 1226
Cdd:PLN03232 1345 LERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTML 1424
                         890       900       910       920
                  ....*....|....*....|....*....|....*....|....*.
gi 6755046   1227 VIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQKG-IYFSMVQA 1271
Cdd:PLN03232 1425 VIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTsAFFRMVHS 1470
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
215-617 7.54e-63

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: 225.01  E-value: 7.54e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   215 LVILAVSPLIGLSSALWAKVLTS-------FTNKEL----QAYAKAGAVAEEVLAAIRTVIAFG----GQQKELERYNKN 279
Cdd:COG4618  148 AVLFLFHPLLGLLALVGALVLVAlallnerLTRKPLkeanEAAIRANAFAEAALRNAEVIEAMGmlpaLRRRWQRANARA 227
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   280 LEEAKNVGIKKAITASISIGIAYLLVYASYALAFWygtsLVLSNEYSIGevltVFF--SILLGTFsighLAPnIE----- 352
Cdd:COG4618  228 LALQARASDRAGGFSALSKFLRLLLQSAVLGLGAY----LVIQGEITPG----AMIaaSILMGRA----LAP-IEqaigg 294
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   353 --AFANARGAAFEIFKIIDNEPSidsfstkgyKPDSIM-----GNLEFKNVHFNYPSrSEVQILKGLNLKVKSGQTVALV 425
Cdd:COG4618  295 wkQFVSARQAYRRLNELLAAVPA---------EPERMPlprpkGRLSVENLTVVPPG-SKRPILRGVSFSLEPGEVLGVI 364
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   426 GNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENI-RYGreDVTMDEIEKAVK 504
Cdd:COG4618  365 GPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIaRFG--DADPEKVVAAAK 442
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   505 EANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKARE-GRTTIV 583
Cdd:COG4618  443 LAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKArGATVVV 522
                        410       420       430
                 ....*....|....*....|....*....|....
gi 6755046   584 IAHRLSTVRNADVIAGFDGGVIVEQGNHDELMRE 617
Cdd:COG4618  523 ITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
963-1270 1.16e-62

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 224.70  E-value: 1.16e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    963 AQQLMTFEN-----VMLVFSA---------------VVFGAMAA--------------GNTSSfapdyakakvSASHIIR 1008
Cdd:PRK11160  247 SQALMILANgltvvLMLWLAAggvggnaqpgalialFVFAALAAfealmpvagafqhlGQVIA----------SARRINE 316
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1009 IIEKTPEIDSYSTEGLKPTllEGNVKFNGVQFNYPTRPNiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPM 1088
Cdd:PRK11160  317 ITEQKPEVTFPTTSTAAAD--QVSLTLNNVSFTYPDQPQ-PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQ 393
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1089 AGSVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAENIAYgdnsravsheeivrAAKEANIHQFIDSL--------- 1159
Cdd:PRK11160  394 QGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLL--------------AAPNASDEALIEVLqqvglekll 459
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1160 --PDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQN 1237
Cdd:PRK11160  460 edDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQ 539
                         330       340       350
                  ....*....|....*....|....*....|...
gi 6755046   1238 ADLIVVIENGKVKEHGTHQQLLAQKGIYFSMVQ 1270
Cdd:PRK11160  540 FDRICVMDNGQIIEQGTHQELLAQQGRYYQLKQ 572
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
126-625 2.17e-62

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: 227.31  E-value: 2.17e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     126 IVAYIQVSLWCLAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDdVSKINDGIGDKIGMFFQSITTFLA-GFI 204
Cdd:TIGR01193  211 ILSYIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGEIVSRFTD-ASSIIDALASTILSLFLDMWILVIvGLF 289
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     205 IGFISGwKLTLVILAVSPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQK-------ELERY- 276
Cdd:TIGR01193  290 LVRQNM-LLFLLSLLSIPVYAVIIILFKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEAEryskidsEFGDYl 368
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     277 NKNLEEAKNVGIKKAITASISIGIAYLLVyasyalafWYGTSLVLSNEYSIGEVLTvfFSILLGTF-----SIGHLAPNI 351
Cdd:TIGR01193  369 NKSFKYQKADQGQQAIKAVTKLILNVVIL--------WTGAYLVMRGKLTLGQLIT--FNALLSYFltpleNIINLQPKL 438
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     352 EAFANARGAAFEIFkIIDNEpsidsFSTKGYKPDSIM--GNLEFKNVHFNYPSRSEvqILKGLNLKVKSGQTVALVGNSG 429
Cdd:TIGR01193  439 QAARVANNRLNEVY-LVDSE-----FINKKKRTELNNlnGDIVINDVSYSYGYGSN--ILSDISLTIKMNSKTTIVGMSG 510
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     430 CGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENIRYG-REDVTMDEIEKAVKEANA 508
Cdd:TIGR01193  511 SGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGaKENVSQDEIWAACEIAEI 590
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     509 YDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREgRTTIVIAHRL 588
Cdd:TIGR01193  591 KDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQD-KTIIFVAHRL 669
                          490       500       510
                   ....*....|....*....|....*....|....*..
gi 6755046     589 STVRNADVIAGFDGGVIVEQGNHDELMREKGIYFKLV 625
Cdd:TIGR01193  670 SVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLI 706
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
995-1244 6.86e-62

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: 221.39  E-value: 6.86e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     995 DYAKAKVSASHIIRIIEKTPEIDSYSTEglKPTLLEGNVKFNGVQFNYPTRPniPVLQGLSLEVKKGQTLALVGSSGCGK 1074
Cdd:TIGR02857  286 ARADGVAAAEALFAVLDAAPRPLAGKAP--VTAAPASSLEFSGVSVAYPGRR--PALRPVSFTVPPGERVALVGPSGAGK 361
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    1075 STVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAENIAYGDnsRAVSHEEIVRAAKEANIHQ 1154
Cdd:TIGR02857  362 STLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLAR--PDASDAEIREALERAGLDE 439
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    1155 FIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLST 1234
Cdd:TIGR02857  440 FVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLAL 519
                          250
                   ....*....|
gi 6755046    1235 IQNADLIVVI 1244
Cdd:TIGR02857  520 AALADRIVVL 529
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
757-1270 2.11e-61

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


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 221.52  E-value: 2.11e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    757 FLVMGLISFVTYFFQGFTFGKAGEILTKRVRYMVFKSMLRQDISWFDDHknSTGSLTTRLASDASSVKGAMGARLAVVTQ 836
Cdd:PRK10790   71 YVGLQLLAAGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSAFDTQ--PVGQLISRVTNDTEVIRDLYVTVVATVLR 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    837 NVANLGTGVILSLVYGWQLTLLLVVIIP--LIVLGgiiemkllsgqalkdkkqleISGKIATEAIENFRTIVSLTREQKF 914
Cdd:PRK10790  149 SAALIGAMLVAMFSLDWRMALVAIMIFPavLVVMV--------------------IYQRYSTPIVRRVRAYLADINDGFN 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    915 ETMYAQSLQVPYRNAMKkahvFGITFSFTQAMMYFSYAACFRFGAYLVAQQLMTFENVMLVFSAVVFGAMAAGnTSSFAP 994
Cdd:PRK10790  209 EVINGMSVIQQFRQQAR----FGERMGEASRSHYMARMQTLRLDGFLLRPLLSLFSALILCGLLMLFGFSASG-TIEVGV 283
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    995 DYA-----------------------KAKVSASHIIRIIEKTPEidSYSTEGLkpTLLEGNVKFNGVQFNYptRPNIPVL 1051
Cdd:PRK10790  284 LYAfisylgrlneplielttqqsmlqQAVVAGERVFELMDGPRQ--QYGNDDR--PLQSGRIDIDNVSFAY--RDDNLVL 357
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1052 QGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAENIAY 1131
Cdd:PRK10790  358 QNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTL 437
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1132 GdnsRAVSHEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKV 1211
Cdd:PRK10790  438 G---RDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQA 514
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 6755046   1212 VQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQKGIYFSMVQ 1270
Cdd:PRK10790  515 IQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQ 573
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
759-1268 4.09e-60

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


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 217.27  E-value: 4.09e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    759 VMGLISFVTY----FFQGFTFGkAGEILTKRVRYMVFKSMLRQDISWFDDHKnsTGSLTTRLASDASSVKGAMG-ARLAV 833
Cdd:PRK10789   41 TMVLIAVVVYllryVWRVLLFG-ASYQLAVELREDFYRQLSRQHPEFYLRHR--TGDLMARATNDVDRVVFAAGeGVLTL 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    834 VTQNVANLGTGVILSLVYGWQLTLLLVVIIPLIVL-----GGIIEMKLLSGQA----LKDKKQleisgkiatEAIENFRT 904
Cdd:PRK10789  118 VDSLVMGCAVLIVMSTQISWQLTLLALLPMPVMAImikryGDQLHERFKLAQAafssLNDRTQ---------ESLTSIRM 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    905 IVSLTREQKFETMYAQSLQVPYRNAMKKAHV---FGITFSFTQAMmyfSYAACFRFGAYLVAQqlmtfenvmlvfsavvf 981
Cdd:PRK10789  189 IKAFGLEDRQSALFAADAEDTGKKNMRVARIdarFDPTIYIAIGM---ANLLAIGGGSWMVVN----------------- 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    982 GAMAAGNTSSFA--------PDYAKA-------KVSA--SHIIRIIEKTPEIDsystEGLKPTLLE-GNVKFNGVQFNYP 1043
Cdd:PRK10789  249 GSLTLGQLTSFVmylglmiwPMLALAwmfniveRGSAaySRIRAMLAEAPVVK----DGSEPVPEGrGELDVNIRQFTYP 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1044 TRPNiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDC 1123
Cdd:PRK10789  325 QTDH-PALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSD 403
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1124 SIAENIAYGdnSRAVSHEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSA 1203
Cdd:PRK10789  404 TVANNIALG--RPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSA 481
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6755046   1204 LDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQKGIYFSM 1268
Cdd:PRK10789  482 VDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDM 546
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
752-1271 1.18e-58

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: 216.14  E-value: 1.18e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     752 LFSLFFLVMGLISFVTYFFQGFTFGKAGEILTKRVRYMVFKSMLRQDISWFDDHKnsTGSLTTRLaSDASSVKGAMGARL 831
Cdd:TIGR01193  197 IISIGLIIAYIIQQILSYIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRR--TGEIVSRF-TDASSIIDALASTI 273
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     832 AVVTQNVANLgtgVILSLVYGWQ---LTLLLVVIIPLIVLGGIIEMKLLSGQalkDKKQLEISGKIATEAIENF---RTI 905
Cdd:TIGR01193  274 LSLFLDMWIL---VIVGLFLVRQnmlLFLLSLLSIPVYAVIIILFKRTFNKL---NHDAMQANAVLNSSIIEDLngiETI 347
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     906 VSLTREQ--------KFETMYAQSLQVPYRNAMKKAHVFGITFSFTQAMMYFsyaacfrfGAYLVAQQLMTFENVmLVFS 977
Cdd:TIGR01193  348 KSLTSEAeryskidsEFGDYLNKSFKYQKADQGQQAIKAVTKLILNVVILWT--------GAYLVMRGKLTLGQL-ITFN 418
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     978 AVV-FGAMAAGNTSSFAPDYAKAKVSAshiIRIIE----KTPEIDSYSTEGLkpTLLEGNVKFNGVQFNYPTrpNIPVLQ 1052
Cdd:TIGR01193  419 ALLsYFLTPLENIINLQPKLQAARVAN---NRLNEvylvDSEFINKKKRTEL--NNLNGDIVINDVSYSYGY--GSNILS 491
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    1053 GLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAENIAYG 1132
Cdd:TIGR01193  492 DISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLG 571
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    1133 dNSRAVSHEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVV 1212
Cdd:TIGR01193  572 -AKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKI 650
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 6755046    1213 QEALDKAREgRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQKGIYFSMVQA 1271
Cdd:TIGR01193  651 VNNLLNLQD-KTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLIHN 708
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
168-588 5.13e-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: 209.91  E-value: 5.13e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     168 GELNTRLTDDVskinDGIGDkigMFFQSITTFLAGFIIGFISgwklTLVILAVSP---LIGLSSALWAKVLTSFT----- 239
Cdd:TIGR02868  110 GDLLGRLGADV----DALQD---LYVRVIVPAGVALVVGAAA----VAAIAVLSVpaaLILAAGLLLAGFVAPLVslraa 178
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     240 -NKELQAYAKAGAVAEEVLAAIR---TVIAFGGQQKELERYNKNLEEAKNVGIKKAITASISIGIAYLLVYASYALAFWY 315
Cdd:TIGR02868  179 rAAEQALARLRGELAAQLTDALDgaaELVASGALPAALAQVEEADRELTRAERRAAAATALGAALTLLAAGLAVLGALWA 258
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     316 GTSLVLSNEYSiGEVLTVFFSILLGTFSI-GHLAPNIEAFANARGAAFEIFKIIDNEPSIDSFSTKGYKPDSIMG-NLEF 393
Cdd:TIGR02868  259 GGPAVADGRLA-PVTLAVLVLLPLAAFEAfAALPAAAQQLTRVRAAAERIVEVLDAAGPVAEGSAPAAGAVGLGKpTLEL 337
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     394 KNVHFNYPSRSEVqiLKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIGVVS 473
Cdd:TIGR02868  338 RDLSAGYPGAPPV--LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCA 415
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     474 QEPVLFATTIAENIRYGREDVTMDEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLL 553
Cdd:TIGR02868  416 QDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLL 495
                          410       420       430
                   ....*....|....*....|....*....|....*
gi 6755046     554 DEATSALDTESEAVVQAALDKAREGRTTIVIAHRL 588
Cdd:TIGR02868  496 DEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
360-624 4.12e-56

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 205.44  E-value: 4.12e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    360 AAFEIFKIIDNEPSIdSFSTKGyKPDSIMGNLEFKNVHFNYPSRSEvQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLM 439
Cdd:PRK11160  310 SARRINEITEQKPEV-TFPTTS-TAAADQVSLTLNNVSFTYPDQPQ-PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLL 386
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    440 QRLYDPLEGVVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENIRYGREDVTmDEIEKAVKEANAYDFIMKLPHQF 519
Cdd:PRK11160  387 TRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNAS-DEALIEVLQQVGLEKLLEDDKGL 465
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    520 DTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAG 599
Cdd:PRK11160  466 NAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICV 545
                         250       260
                  ....*....|....*....|....*
gi 6755046    600 FDGGVIVEQGNHDELMREKGIYFKL 624
Cdd:PRK11160  546 MDNGQIIEQGTHQELLAQQGRYYQL 570
PLN03130 PLN03130
ABC transporter C family member; Provisional
394-1271 2.04e-55

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 212.29  E-value: 2.04e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    394 KNVHFNYPSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIdgqdirtinvryLREIIGVVS 473
Cdd:PLN03130  618 KNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV------------IRGTVAYVP 685
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    474 QEPVLFATTIAENIRYGREdVTMDEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLL 553
Cdd:PLN03130  686 QVSWIFNATVRDNILFGSP-FDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIF 764
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    554 DEATSALDTE-SEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREkGIYFKLVMTQtrGN 632
Cdd:PLN03130  765 DDPLSALDAHvGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNN-GPLFQKLMEN--AG 841
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    633 EIEPGNNAYGSQSDTDASELTSEESKSPLIRRSiyrSVHRKQDQERRLSMKEAVDEDVPLVSfWRIL----NLNLSEWpy 708
Cdd:PLN03130  842 KMEEYVEENGEEEDDQTSSKPVANGNANNLKKD---SSSKKKSKEGKSVLIKQEERETGVVS-WKVLerykNALGGAW-- 915
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    709 lLVGVL--CAVINgciqPVFAIVFSRIVGVFSrddDHETKRQNCNLFslFFLVMGLISF----VTyFFQGFTFGKAGEIL 782
Cdd:PLN03130  916 -VVMILflCYVLT----EVFRVSSSTWLSEWT---DQGTPKTHGPLF--YNLIYALLSFgqvlVT-LLNSYWLIMSSLYA 984
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    783 TKRVRYMVFKSMLRQDISWFddHKNSTGSLTTRLASDassvkgamgarLAVVTQNVANLgtgVILSLVYGWQL--TLLLV 860
Cdd:PLN03130  985 AKRLHDAMLGSILRAPMSFF--HTNPLGRIINRFAKD-----------LGDIDRNVAVF---VNMFLGQIFQLlsTFVLI 1048
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    861 VIIPLIVLGGIIEMKLLSGQAL-------KDKKQLEisgkiateaienfrtivSLTREqkfeTMYAQ--------SLQVP 925
Cdd:PLN03130 1049 GIVSTISLWAIMPLLVLFYGAYlyyqstaREVKRLD-----------------SITRS----PVYAQfgealnglSTIRA 1107
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    926 YRNAMKKAHVFGITFS----FTQAMMYfsyaacfrfGAYLVAQQLMTFENVMLVFSA--VVFGAMAAGNTSSFAPDYAKA 999
Cdd:PLN03130 1108 YKAYDRMAEINGRSMDnnirFTLVNMS---------SNRWLAIRLETLGGLMIWLTAsfAVMQNGRAENQAAFASTMGLL 1178
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1000 KVSASHIIRIIEKTPEIDSYSTEGLK---------------PTLLEGN-----------VKFNGVQFNYptRPNIP-VLQ 1052
Cdd:PLN03130 1179 LSYALNITSLLTAVLRLASLAENSLNavervgtyidlpseaPLVIENNrpppgwpssgsIKFEDVVLRY--RPELPpVLH 1256
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1053 GLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAENI-AY 1131
Cdd:PLN03130 1257 GLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLdPF 1336
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1132 GDNSRAvsheEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKV 1211
Cdd:PLN03130 1337 NEHNDA----DLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDAL 1412
                         890       900       910       920       930       940
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6755046   1212 VQEALDKarEGRTC--IVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQKGIYFS-MVQA 1271
Cdd:PLN03130 1413 IQKTIRE--EFKSCtmLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFSkMVQS 1473
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
129-635 4.08e-55

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


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 203.03  E-value: 4.08e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    129 YIQVSLWCLAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDKIGMFFQSITTFLAGFIIGFI 208
Cdd:PRK10790   83 YAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFS 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    209 SGWKLTLVILAVSPLIGLSSALWAKVLTSFTNKeLQAY-AKAGAVAEEVLAAIRTVIAFGGQQkeleRYNKNLEEAKNVG 287
Cdd:PRK10790  163 LDWRMALVAIMIFPAVLVVMVIYQRYSTPIVRR-VRAYlADINDGFNEVINGMSVIQQFRQQA----RFGERMGEASRSH 237
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    288 IKKAITA----------SISIGIAYLLVyasyALAFWYGtslvLSNEYSIG-EVLTVFFSILlgtfsiGHL-APNIE--- 352
Cdd:PRK10790  238 YMARMQTlrldgfllrpLLSLFSALILC----GLLMLFG----FSASGTIEvGVLYAFISYL------GRLnEPLIEltt 303
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    353 ---AFANARGAAFEIFKIIDNEpsidsfsTKGYKPDSIM---GNLEFKNVHFNYpsRSEVQILKGLNLKVKSGQTVALVG 426
Cdd:PRK10790  304 qqsMLQQAVVAGERVFELMDGP-------RQQYGNDDRPlqsGRIDIDNVSFAY--RDDNLVLQNINLSVPSRGFVALVG 374
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    427 NSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENIRYGReDVTMDEIEKAVKEA 506
Cdd:PRK10790  375 HTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGR-DISEEQVWQALETV 453
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    507 NAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAH 586
Cdd:PRK10790  454 QLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAH 533
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*....
gi 6755046    587 RLSTVRNADVIAGFDGGVIVEQGNHDELMREKGIYFKLVMTQTRGNEIE 635
Cdd:PRK10790  534 RLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQLQLAGEELA 582
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
294-621 9.23e-55

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 202.00  E-value: 9.23e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    294 ASISIgiAYLLVY--ASY--ALAF-WYGTS---------LVLSNEysigevltvFFSIL--LGTFSigHlapnieAFANA 357
Cdd:PRK11174  257 ASISI--ALVAVYfgFSYlgELNFgHYGTGvtlfagffvLILAPE---------FYQPLrdLGTFY--H------AKAQA 317
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    358 RGAAFEIFKIIDNEpsiDSFSTKGYKPDSIMGNLEFKNVHFNYPSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTtvq 437
Cdd:PRK11174  318 VGAAESLVTFLETP---LAHPQQGEKELASNDPVTIEAEDLEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTS--- 391
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    438 LMQRL--YDPLEGVVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENIRYGREDVTMDEIEKAVKEANAYDFIMKL 515
Cdd:PRK11174  392 LLNALlgFLPYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLL 471
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    516 PHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNAD 595
Cdd:PRK11174  472 PQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWD 551
                         330       340
                  ....*....|....*....|....*.
gi 6755046    596 VIAGFDGGVIVEQGNHDELMREKGIY 621
Cdd:PRK11174  552 QIWVMQDGQIVQQGDYAELSQAGGLF 577
type_I_sec_PrtD TIGR01842
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ...
1043-1261 2.12e-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: 196.80  E-value: 2.12e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    1043 PTRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGIVSQEPILFD 1122
Cdd:TIGR01842  326 PPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFP 405
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    1123 CSIAENIA-YGDNSRAvshEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEAT 1201
Cdd:TIGR01842  406 GTVAENIArFGENADP---EKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPN 482
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6755046    1202 SALDTESEKVVQEALDKAR-EGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQ 1261
Cdd:TIGR01842  483 SNLDEEGEQALANAIKALKaRGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
1054-1268 6.71e-53

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 196.22  E-value: 6.71e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1054 LSLEVKKGQTLALVGSSGCGKSTVVQLLERFYdPMAGSVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAENIAYGD 1133
Cdd:PRK11174  369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGN 447
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1134 NSraVSHEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQ 1213
Cdd:PRK11174  448 PD--ASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVM 525
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 6755046   1214 EALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQKGIYFSM 1268
Cdd:PRK11174  526 QALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATL 580
type_I_sec_PrtD TIGR01842
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ...
316-617 2.90e-51

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: 190.64  E-value: 2.90e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     316 GTSLVLSNEYSIGEVLTVffSILLGTF--SIGHLAPNIEAFANARGAAFEIFKIIDNEPSidsfstkgykPDSIM----- 388
Cdd:TIGR01842  246 GAYLAIDGEITPGMMIAG--SILVGRAlaPIDGAIGGWKQFSGARQAYKRLNELLANYPS----------RDPAMplpep 313
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     389 -GNLEFKNVHFnYPSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLRE 467
Cdd:TIGR01842  314 eGHLSVENVTI-VPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGK 392
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     468 IIGVVSQEPVLFATTIAENIRYGREDVTMDEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRN 547
Cdd:TIGR01842  393 HIGYLPQDVELFPGTVAENIARFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGD 472
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6755046     548 PKILLLDEATSALDTESEAVVQAALDKAR-EGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMRE 617
Cdd:TIGR01842  473 PKLVVLDEPNSNLDEEGEQALANAIKALKaRGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
391-618 6.51e-51

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: 179.45  E-value: 6.51e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   391 LEFKNVHFNYPSrsEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIG 470
Cdd:COG1122    1 IELENLSFSYPG--GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   471 VVSQEPV--LFATTIAENIRYGRE--DVTMDEIEKAVKEA----NAYDFIMKLPHqfdtlvgergaQLSGGQKQRIAIAR 542
Cdd:COG1122   79 LVFQNPDdqLFAPTVEEDVAFGPEnlGLPREEIRERVEEAlelvGLEHLADRPPH-----------ELSGGQKQRVAIAG 147
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6755046   543 ALVRNPKILLLDEATSALDTESEAVVQAALDK-AREGRTTIVIAHRLSTV-RNADVIAGFDGGVIVEQGNHDELMREK 618
Cdd:COG1122  148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREVFSDY 225
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
391-616 1.03e-50

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: 188.19  E-value: 1.03e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   391 LEFKNVHFNYPSRS--EVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREI 468
Cdd:COG1123  261 LEVRNLSKRYPVRGkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLREL 340
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   469 ---IGVVSQEPV--LFAT-TIAENIRYG---REDVTMDEIEKAVKEANA-----YDFIMKLPHQFdtlvgergaqlSGGQ 534
Cdd:COG1123  341 rrrVQMVFQDPYssLNPRmTVGDIIAEPlrlHGLLSRAERRERVAELLErvglpPDLADRYPHEL-----------SGGQ 409
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   535 KQRIAIARALVRNPKILLLDEATSALDteseAVVQAA-LD-----KAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVE 607
Cdd:COG1123  410 RQRVAIARALALEPKLLILDEPTSALD----VSVQAQiLNllrdlQRELGLTYLFISHDLAVVRYiADRVAVMYDGRIVE 485

                 ....*....
gi 6755046   608 QGNHDELMR 616
Cdd:COG1123  486 DGPTEEVFA 494
ABC_6TM_TAP_ABCB8_10_like cd18557
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ...
48-361 2.28e-50

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: 180.06  E-value: 2.28e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    48 LCMILGTLAAIihgtLLPLLmlvFGNMTDSFTKAeaSILPSITNQSGPNSTLIISNSSLeeeMAIYAYYYTgigagvliv 127
Cdd:cd18557    3 LFLLISSAAQL----LLPYL---IGRLIDTIIKG--GDLDVLNELALILLAIYLLQSVF---TFVRYYLFN--------- 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   128 ayiqvslwcLAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDKIGMFFQSITTFLAGFIIGF 207
Cdd:cd18557   62 ---------IAGERIVARLRRDLFSSLLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILF 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   208 ISGWKLTLVILAVSPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQKELERYNKNLEEAKNVG 287
Cdd:cd18557  133 ILSWKLTLVLLLVIPLLLIASKIYGRYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLA 212
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6755046   288 IKKAITASISIGIAYLLVYASYALAFWYGTSLVLSNEYSIGEVLT-VFFSILLgTFSIGHLAPNIEAFANARGAA 361
Cdd:cd18557  213 RKKALANALFQGITSLLIYLSLLLVLWYGGYLVLSGQLTVGELTSfILYTIMV-ASSVGGLSSLLADIMKALGAS 286
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
391-614 3.56e-49

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: 174.29  E-value: 3.56e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   391 LEFKNVHFNYpsrSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYD-----PLEGVVSIDGQDIRTINVR-- 463
Cdd:cd03260    1 IELRDLNVYY---GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDvl 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   464 YLREIIGVVSQEPVLFATTIAENIRYG------REDVTMDEI-EKAVKEANAYDFIMKLPHqfdtlvgerGAQLSGGQKQ 536
Cdd:cd03260   78 ELRRRVGMVFQKPNPFPGSIYDNVAYGlrlhgiKLKEELDERvEEALRKAALWDEVKDRLH---------ALGLSGGQQQ 148
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6755046   537 RIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTV-RNADVIAGFDGGVIVEQGNHDEL 614
Cdd:cd03260  149 RLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAaRVADRTAFLLNGRLVEFGPTEQI 227
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
1033-1262 4.54e-49

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: 174.06  E-value: 4.54e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1033 VKFNGVQFNYPtrPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLG 1112
Cdd:COG1122    1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1113 IVSQEPI--LFDCSIAENIAYGDNSRAVSHEEIVRAAKEA----NIHQFIDSLPDkyntrvgdkgtQLSGGQKQRIAIAR 1186
Cdd:COG1122   79 LVFQNPDdqLFAPTVEEDVAFGPENLGLPREEIRERVEEAlelvGLEHLADRPPH-----------ELSGGQKQRVAIAG 147
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6755046  1187 ALVRQPHILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTI-QNADLIVVIENGKVKEHGTHQQLLAQK 1262
Cdd:COG1122  148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREVFSDY 225
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
392-603 8.03e-49

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: 172.65  E-value: 8.03e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   392 EFKNVHFNYPSRSEvQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIGV 471
Cdd:cd03225    1 ELKNLSFSYPDGAR-PALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   472 VSQEP--VLFATTIAENIRYGRE--DVTMDEIEKAVKEANAydfIMKLPHQFDTLVgergAQLSGGQKQRIAIARALVRN 547
Cdd:cd03225   80 VFQNPddQFFGPTVEEEVAFGLEnlGLPEEEIEERVEEALE---LVGLEGLRDRSP----FTLSGGQKQRVAIAGVLAMD 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 6755046   548 PKILLLDEATSALDTESEAVVQAALDK-AREGRTTIVIAHRLSTVRN-ADVIAGFDGG 603
Cdd:cd03225  153 PDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLElADRVIVLEDG 210
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
391-605 1.00e-48

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: 170.86  E-value: 1.00e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   391 LEFKNVHFNYPSRSEVqILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIG 470
Cdd:cd03246    1 LEVENVSFRYPGAEPP-VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   471 VVSQEPVLFATTIAENIrygredvtmdeiekavkeanaydfimklphqfdtlvgergaqLSGGQKQRIAIARALVRNPKI 550
Cdd:cd03246   80 YLPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRI 117
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 6755046   551 LLLDEATSALDTESEAVVQAALDKARE-GRTTIVIAHRLSTVRNADVIAGFDGGVI 605
Cdd:cd03246  118 LVLDEPNSHLDVEGERALNQAIAALKAaGATRIVIAHRPETLASADRILVLEDGRV 173
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
1037-1249 9.65e-48

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: 9.65e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1037 GVQFNYPTRPNiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGIVSQ 1116
Cdd:cd03246    5 NVSFRYPGAEP-PVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQ 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1117 EPILFDCSIAENIaygdnsravsheeivraakeanihqfidslpdkyntrvgdkgtqLSGGQKQRIAIARALVRQPHILL 1196
Cdd:cd03246   84 DDELFSGSIAENI--------------------------------------------LSGGQRQRLGLARALYGNPRILV 119
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 6755046  1197 LDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIVVIENGKV 1249
Cdd:cd03246  120 LDEPNSHLDVEGERALNQAIAALKAaGATRIVIAHRPETLASADRILVLEDGRV 173
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
1050-1258 3.04e-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: 3.04e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD-----PMAGSVFLDGKEI--KQLNVQWLRAHLGIVSQEPILFD 1122
Cdd:cd03260   15 ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIydLDVDVLELRRRVGMVFQKPNPFP 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1123 CSIAENIAYGDNSRAVS----HEEIVRAA-KEANihqfidsLPDKYNTRVgdKGTQLSGGQKQRIAIARALVRQPHILLL 1197
Cdd:cd03260   95 GSIYDNVAYGLRLHGIKlkeeLDERVEEAlRKAA-------LWDEVKDRL--HALGLSGGQQQRLCLARALANEPEVLLL 165
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6755046  1198 DEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQL 1258
Cdd:cd03260  166 DEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
1034-1248 6.69e-47

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: 167.26  E-value: 6.69e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1034 KFNGVQFNYPTRpNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGI 1113
Cdd:cd03225    1 ELKNLSFSYPDG-ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1114 VSQEP--ILFDCSIAENIAYGDNSRAVSHEEIVRAAKEANIHQFIDSLPDKyNTRvgdkgtQLSGGQKQRIAIARALVRQ 1191
Cdd:cd03225   80 VFQNPddQFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDR-SPF------TLSGGQKQRVAIAGVLAMD 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 6755046  1192 PHILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVIENGK 1248
Cdd:cd03225  153 PDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
1034-1249 1.19e-46

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 166.53  E-value: 1.19e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1034 KFNGVQFNYPTRPnipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGI 1113
Cdd:COG4619    2 ELEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1114 VSQEPILFDCSIAENIAYGDNSRavsHEEIVRAAKEANIHQFidSLPDKY-NTRVgdkgTQLSGGQKQRIAIARALVRQP 1192
Cdd:COG4619   79 VPQEPALWGGTVRDNLPFPFQLR---ERKFDRERALELLERL--GLPPDIlDKPV----ERLSGGERQRLALIRALLLQP 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1193 HILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVIENGKV 1249
Cdd:COG4619  150 DVLLLDEPTSALDPENTRRVEELLREylAEEGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
1033-1261 3.99e-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: 3.99e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1033 VKFNGVQFNYPTRPN--IPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLN---VQWL 1107
Cdd:COG1123  261 LEVRNLSKRYPVRGKggVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLREL 340
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1108 RAHLGIVSQEPIL-FDC--SIAENIAYG-DNSRAVSHEEIVRAAKEAnIHQ------FIDSLPDkyntrvgdkgtQLSGG 1177
Cdd:COG1123  341 RRRVQMVFQDPYSsLNPrmTVGDIIAEPlRLHGLLSRAERRERVAEL-LERvglppdLADRYPH-----------ELSGG 408
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1178 QKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALD--KAREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGT 1254
Cdd:COG1123  409 QRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRdlQRELGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGP 488

                 ....*..
gi 6755046  1255 HQQLLAQ 1261
Cdd:COG1123  489 TEEVFAN 495
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
409-558 7.54e-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: 162.05  E-value: 7.54e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     409 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIGVVSQEPVLF-ATTIAENI 487
Cdd:pfam00005    1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENL 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6755046     488 RYGREdvtMDEIEKAVKEANAYDFI--MKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATS 558
Cdd:pfam00005   81 RLGLL---LKGLSKREKDARAEEALekLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
391-609 8.04e-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: 164.60  E-value: 8.04e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   391 LEFKNVHFNYPSR-SEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREI- 468
Cdd:cd03257    2 LEVKNLSVSFPTGgGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIRr 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   469 --IGVVSQEPVL-------FATTIAENIRYGREDVTMDEIEKAVKEA-----NAYDFIMKLPHQfdtlvgergaqLSGGQ 534
Cdd:cd03257   82 keIQMVFQDPMSslnprmtIGEQIAEPLRIHGKLSKKEARKEAVLLLlvgvgLPEEVLNRYPHE-----------LSGGQ 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6755046   535 KQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKARE--GRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQG 609
Cdd:cd03257  151 RQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
972-1232 1.65e-45

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: 172.93  E-value: 1.65e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     972 VMLVFSAvvFGAMAAgnTSSFAPDYAKAKVSASHIIRIIEKTPEIDSYSTEGLKPTLLEG-NVKFNGVQFNYPTRPniPV 1050
Cdd:TIGR02868  277 VLLPLAA--FEAFAA--LPAAAQQLTRVRAAAERIVEVLDAAGPVAEGSAPAAGAVGLGKpTLELRDLSAGYPGAP--PV 350
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    1051 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAEN-- 1128
Cdd:TIGR02868  351 LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENlr 430
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    1129 IAYGDnsraVSHEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTES 1208
Cdd:TIGR02868  431 LARPD----ATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAET 506
                          250       260
                   ....*....|....*....|....
gi 6755046    1209 EKVVQEALDKAREGRTCIVIAHRL 1232
Cdd:TIGR02868  507 ADELLEDLLAALSGRTVVLITHHL 530
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
1031-1254 1.80e-45

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: 162.97  E-value: 1.80e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1031 GNVKFNGVQFNYptRPNIP-VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRA 1109
Cdd:cd03369    5 GEIEVENLSVRY--APDLPpVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1110 HLGIVSQEPILFDCSIAENIaygDNSRAVSHEEIVRAakeanihqfidslpdkynTRVGDKGTQLSGGQKQRIAIARALV 1189
Cdd:cd03369   83 SLTIIPQDPTLFSGTIRSNL---DPFDEYSDEEIYGA------------------LRVSEGGLNLSQGQRQLLCLARALL 141
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6755046  1190 RQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGT 1254
Cdd:cd03369  142 KRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
1035-1253 2.41e-45

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: 161.71  E-value: 2.41e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1035 FNGVQFNYPTRpNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQwLRAHLGIV 1114
Cdd:cd03247    3 INNVSFSYPEQ-EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-LSSLISVL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1115 SQEPILFDCSIAENIaygdnsravsheeivraakeanihqfidslpdkyntrvgdkGTQLSGGQKQRIAIARALVRQPHI 1194
Cdd:cd03247   81 NQRPYLFDTTLRNNL-----------------------------------------GRRFSGGERQRLALARILLQDAPI 119
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 6755046  1195 LLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHG 1253
Cdd:cd03247  120 VLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
391-586 3.85e-45

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 162.29  E-value: 3.85e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   391 LEFKNVHFNYPSRsevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIG 470
Cdd:COG4619    1 LELEGLSFRVGGK---PILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   471 VVSQEPVLFATTIAENI----RYGREDVTMDEIEKAVKEANaydfimkLPHQF-DTLVGErgaqLSGGQKQRIAIARALV 545
Cdd:COG4619   78 YVPQEPALWGGTVRDNLpfpfQLRERKFDRERALELLERLG-------LPPDIlDKPVER----LSGGERQRLALIRALL 146
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 6755046   546 RNPKILLLDEATSALDTESEAVVQAALDK--AREGRTTIVIAH 586
Cdd:COG4619  147 LQPDVLLLDEPTSALDPENTRRVEELLREylAEEGRAVLWVSH 189
PTZ00243 PTZ00243
ABC transporter; Provisional
408-1275 3.90e-45

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 179.20  E-value: 3.90e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    408 ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVsidgqdirtinvrYLREIIGVVSQEPVLFATTIAENI 487
Cdd:PTZ00243  675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-------------WAERSIAYVPQQAWIMNATVRGNI 741
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    488 RYGREDVTMDeIEKAVK----EANaydfIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTE 563
Cdd:PTZ00243  742 LFFDEEDAAR-LADAVRvsqlEAD----LAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAH 816
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    564 -SEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREKgIYFKLvmtqtRGNEIEpGNNAYG 642
Cdd:PTZ00243  817 vGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMRTS-LYATL-----AAELKE-NKDSKE 889
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    643 SQSDTDASELTSEESKSPLIRRSIYRSVHRKQDQE---------RRLSMKEAVDEDVP---------------------- 691
Cdd:PTZ00243  890 GDADAEVAEVDAAPGGAVDHEPPVAKQEGNAEGGDgaaldaaagRLMTREEKASGSVPwstyvaylrfcgglhaagfvla 969
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    692 --------------LVSFWRILNLNLSEWPYLLVGVLCAVINGCIQPV-FAIVFS------------------------- 731
Cdd:PTZ00243  970 tfavtelvtvssgvWLSMWSTRSFKLSAATYLYVYLGIVLLGTFSVPLrFFLSYEamrrgsrnmhrdllrsvsrgtmsff 1049
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    732 ------RIVGVFSRDDDHETKRQNCNLFSLFFLVMGLIS--FVTYFFQGFTFGKAGEILTKRVRYMVFKSMLRQDISWFD 803
Cdd:PTZ00243 1050 dttplgRILNRFSRDIDILDNTLPMSYLYLLQCLFSICSsiLVTSASQPFVLVALVPCGYLYYRLMQFYNSANREIRRIK 1129
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    804 DHKNS----------TGSLTTRLASDASSVKGAMGARLAVV-----TQNVANLGTGVilslvygwQLTLLLVVIIPLIVL 868
Cdd:PTZ00243 1130 SVAKSpvftlleealQGSATITAYGKAHLVMQEALRRLDVVyscsyLENVANRWLGV--------RVEFLSNIVVTVIAL 1201
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    869 GGIIEMKLLSGQalKDKKQLEISGKIATEAIENFRTIVsltreQKFETMYAQSLQVpyrnamkkahvfgitfsftQAMMY 948
Cdd:PTZ00243 1202 IGVIGTMLRATS--QEIGLVSLSLTMAMQTTATLNWLV-----RQVATVEADMNSV-------------------ERLLY 1255
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    949 FSYAacfrfgaylVAQQLMTfENVMLVFSAVVFGAMAAGNTSSFAPDYAKAKVSASHIIRiiektpeidsysteglkptl 1028
Cdd:PTZ00243 1256 YTDE---------VPHEDMP-ELDEEVDALERRTGMAADVTGTVVIEPASPTSAAPHPVQ-------------------- 1305
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1029 lEGNVKFNGVQFNYptRPNIP-VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWL 1107
Cdd:PTZ00243 1306 -AGSLVFEGVQMRY--REGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLREL 1382
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1108 RAHLGIVSQEPILFDCSIAENIaygDNSRAVSHEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARA 1187
Cdd:PTZ00243 1383 RRQFSMIPQDPVLFDGTVRQNV---DPFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARA 1459
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1188 LV-RQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQL-LAQKGIY 1265
Cdd:PTZ00243 1460 LLkKGSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELvMNRQSIF 1539
                         970
                  ....*....|
gi 6755046   1266 FSMVQAGAKR 1275
Cdd:PTZ00243 1540 HSMVEALGRS 1549
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
391-614 4.83e-45

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: 162.75  E-value: 4.83e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   391 LEFKNVHFNYPSR-SEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREI- 468
Cdd:cd03258    2 IELKNVSKVFGDTgGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKAr 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   469 --IGVVSQEPVLFAT-TIAENIRYGRE--DVTMDEIEKAVKE----------ANAYdfimklPhqfdtlvgergAQLSGG 533
Cdd:cd03258   82 rrIGMIFQHFNLLSSrTVFENVALPLEiaGVPKAEIEERVLEllelvgledkADAY------P-----------AQLSGG 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   534 QKQRIAIARALVRNPKILLLDEATSALDTES-EAVVQAALDKAREGRTTIV-IAHRLSTVRN-ADVIAGFDGGVIVEQGN 610
Cdd:cd03258  145 QKQRVGIARALANNPKVLLCDEATSALDPETtQSILALLRDINRELGLTIVlITHEMEVVKRiCDRVAVMEKGEVVEEGT 224

                 ....
gi 6755046   611 HDEL 614
Cdd:cd03258  225 VEEV 228
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
389-609 1.20e-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: 160.66  E-value: 1.20e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   389 GNLEFKNVHFNYPSRSEvQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREI 468
Cdd:cd03369    5 GEIEVENLSVRYAPDLP-PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSS 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   469 IGVVSQEPVLFATTIAENI-RYGREDvtMDEIEKAVKeanaydfimklphqfdtlVGERGAQLSGGQKQRIAIARALVRN 547
Cdd:cd03369   84 LTIIPQDPTLFSGTIRSNLdPFDEYS--DEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLKR 143
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6755046   548 PKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQG 609
Cdd:cd03369  144 PRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYD 205
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
1033-1251 2.42e-44

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 160.59  E-value: 2.42e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1033 VKFNGVQFNYPTRPN-IPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQL---LERfydPMAGSVFLDGKEIKQLN----V 1104
Cdd:COG1136    5 LELRNLTKSYGTGEGeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNIlggLDR---PTSGEVLIDGQDISSLSerelA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1105 QWLRAHLGIVSQEPILFDC-SIAENIA----YGDNSRAVSHEEIVRAAKEANIHQFIDSLPDkyntrvgdkgtQLSGGQK 1179
Cdd:COG1136   82 RLRRRHIGFVFQFFNLLPElTALENVAlpllLAGVSRKERRERARELLERVGLGDRLDHRPS-----------QLSGGQQ 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6755046  1180 QRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQNADLIVVIENGKVKE 1251
Cdd:COG1136  151 QRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRElnRELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
391-610 5.12e-44

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 163.32  E-value: 5.12e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   391 LEFKNVHFNYPSRS-EVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREI- 468
Cdd:COG1135    2 IELENLSKTFPTKGgPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAAr 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   469 --IGVVSQEPVLFAT-TIAENIRYGRE--DVTMDEIEKAVKE----------ANAYdfimklPhqfdtlvgergAQLSGG 533
Cdd:COG1135   82 rkIGMIFQHFNLLSSrTVAENVALPLEiaGVPKAEIRKRVAEllelvglsdkADAY------P-----------SQLSGG 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   534 QKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKARE--GRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGN 610
Cdd:COG1135  145 QKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRelGLTIVLITHEMDVVRRiCDRVAVLENGRIVEQGP 224
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
391-609 6.14e-44

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: 157.47  E-value: 6.14e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   391 LEFKNVHFNYPSrSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINvRYLREIIG 470
Cdd:cd03247    1 LSINNVSFSYPE-QEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLIS 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   471 VVSQEPVLFATTIAENIrygredvtmdeiekavkeanaydfimklphqfdtlvgerGAQLSGGQKQRIAIARALVRNPKI 550
Cdd:cd03247   79 VLNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPI 119
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 6755046   551 LLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQG 609
Cdd:cd03247  120 VLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
391-616 7.17e-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: 167.77  E-value: 7.17e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   391 LEFKNVHFNYPSRsEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDP---LEGVVSIDGQDIRTINVRYLRE 467
Cdd:COG1123    5 LEVRDLSVRYPGG-DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLDGRDLLELSEALRGR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   468 IIGVVSQEP--VLFATTIAENIRYGRE--DVTMDEIEKAVKEANAydfIMKLPHQFDtlvgERGAQLSGGQKQRIAIARA 543
Cdd:COG1123   84 RIGMVFQDPmtQLNPVTVGDQIAEALEnlGLSRAEARARVLELLE---AVGLERRLD----RYPHQLSGGQRQRVAIAMA 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6755046   544 LVRNPKILLLDEATSALDTESEAVVQAALDK--AREGRTTIVIAHRLSTV-RNADVIAGFDGGVIVEQGNHDELMR 616
Cdd:COG1123  157 LALDPDLLIADEPTTALDVTTQAEILDLLRElqRERGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILA 232
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
1033-1253 9.38e-44

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: 158.45  E-value: 9.38e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1033 VKFNGVQFNYPtrpNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQwlRAHLG 1112
Cdd:cd03259    1 LELKGLSKTYG---SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1113 IVSQEPILFD-CSIAENIAYGDNSRAVSHEEIVRAAKEA----NIHQFIDSLPDkyntrvgdkgtQLSGGQKQRIAIARA 1187
Cdd:cd03259   76 MVFQDYALFPhLTVAENIAFGLKLRGVPKAEIRARVRELlelvGLEGLLNRYPH-----------ELSGGQQQRVALARA 144
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6755046  1188 LVRQPHILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVIENGKVKEHG 1253
Cdd:cd03259  145 LAREPSLLLLDEPLSALDAKLREELREELKElqRELGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
ECF_ATPase_1 TIGR04520
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
391-620 1.96e-43

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: 159.52  E-value: 1.96e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     391 LEFKNVHFNYPSrSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTI-NVRYLREII 469
Cdd:TIGR04520    1 IEVENVSFSYPE-SEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEeNLWEIRKKV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     470 GVVSQEP--VLFATTIAENIRYGRED--VTMDEIEKAVKEA----NAYDFIMKLPHQfdtlvgergaqLSGGQKQRIAIA 541
Cdd:TIGR04520   80 GMVFQNPdnQFVGATVEDDVAFGLENlgVPREEMRKRVDEAlklvGMEDFRDREPHL-----------LSGGQKQRVAIA 148
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     542 RALVRNPKILLLDEATSALDTES-EAVVQAALD-KAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQG------NHDE 613
Cdd:TIGR04520  149 GVLAMRPDIIILDEATSMLDPKGrKEVLETIRKlNKEEGITVISITHDMEEAVLADRVIVMNKGKIVAEGtpreifSQVE 228

                   ....*..
gi 6755046     614 LMREKGI 620
Cdd:TIGR04520  229 LLKEIGL 235
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
391-616 2.38e-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: 158.43  E-value: 2.38e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   391 LEFKNVHFNYPSRSE-VQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREII 469
Cdd:COG1124    2 LEVRNLSVSYGQGGRrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   470 GVVSQEP---------VlfATTIAENIRYGREDVTMDEIEKAVKEAN-AYDFIMKLPHQfdtlvgergaqLSGGQKQRIA 539
Cdd:COG1124   82 QMVFQDPyaslhprhtV--DRILAEPLRIHGLPDREERIAELLEQVGlPPSFLDRYPHQ-----------LSGGQRQRVA 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   540 IARALVRNPKILLLDEATSALDteseAVVQAA-LD-----KAREGRTTIVIAHRLSTV-RNADVIAGFDGGVIVEQGNHD 612
Cdd:COG1124  149 IARALILEPELLLLDEPTSALD----VSVQAEiLNllkdlREERGLTYLFVSHDLAVVaHLCDRVAVMQNGRIVEELTVA 224

                 ....
gi 6755046   613 ELMR 616
Cdd:COG1124  225 DLLA 228
ABC_6TM_AtABCB27_like cd18780
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ...
53-364 2.68e-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: 159.72  E-value: 2.68e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    53 GTLAAIIHGTLLPLLMLVFGNMTDSftkaeasilpsITNQSGPNSTliisnsSLEEEMAIYAYYYTGIGAGVLIVAYIQV 132
Cdd:cd18780    1 GTIALLVSSGTNLALPYFFGQVIDA-----------VTNHSGSGGE------EALRALNQAVLILLGVVLIGSIATFLRS 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   133 SLWCLAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDKIGMFFQSITTFLAGFIIGFISGWK 212
Cdd:cd18780   64 WLFTLAGERVVARLRKRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWK 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   213 LTLVILAVSPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQKELERYNKNLEEAKNVGIKKAI 292
Cdd:cd18780  144 LTLVMLSVVPPLSIGAVIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLAR 223
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6755046   293 TASISIGIAYLLVYASYALAFWYGTSLVLSNEYSIGEvLTVF--FSILLGtFSIGHLAPNIEAFANARGAAFEI 364
Cdd:cd18780  224 ASGGFNGFMGAAAQLAIVLVLWYGGRLVIDGELTTGL-LTSFllYTLTVA-MSFAFLSSLYGDFMQAVGASVRV 295
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
391-614 2.91e-43

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


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 157.85  E-value: 2.91e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   391 LEFKNVHFNYpsrSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDI--RTINVRYLREI 468
Cdd:COG1126    2 IEIENLHKSF---GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKLRRK 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   469 IGVVSQEPVLFA-TTIAENIRYGREDVT-MDEiEKAVKEANAY-------DFIMKLPHQfdtlvgergaqLSGGQKQRIA 539
Cdd:COG1126   79 VGMVFQQFNLFPhLTVLENVTLAPIKVKkMSK-AEAEERAMELlervglaDKADAYPAQ-----------LSGGQQQRVA 146
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6755046   540 IARALVRNPKILLLDEATSALDTE--SEaVVQAALDKAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDEL 614
Cdd:COG1126  147 IARALAMEPKVMLFDEPTSALDPElvGE-VLDVMRDLAKEGMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGPPEEF 223
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
391-609 7.55e-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: 155.76  E-value: 7.55e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   391 LEFKNVHFNYPSrseVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRylREIIG 470
Cdd:cd03259    1 LELKGLSKTYGS---VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   471 VVSQEPVLFAT-TIAENIRYGREDVTM--DEIEKAVKEANAydfIMKLPHQFDTLVgergAQLSGGQKQRIAIARALVRN 547
Cdd:cd03259   76 MVFQDYALFPHlTVAENIAFGLKLRGVpkAEIRARVRELLE---LVGLEGLLNRYP----HELSGGQQQRVALARALARE 148
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6755046   548 PKILLLDEATSALDTESEAVVQAALDK--AREGRTTIVIAHRLS-TVRNADVIAGFDGGVIVEQG 609
Cdd:cd03259  149 PSLLLLDEPLSALDAKLREELREELKElqRELGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
391-616 8.33e-43

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: 156.68  E-value: 8.33e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   391 LEFKNVHFnypSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREI-- 468
Cdd:COG1127    6 IEVRNLTK---SFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELrr 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   469 -IGVVSQEPVLF-ATTIAENIRYG-RE--DVTMDEIEKAVkeanaydfIMKLphqfdTLVGERGA------QLSGGQKQR 537
Cdd:COG1127   83 rIGMLFQGGALFdSLTVFENVAFPlREhtDLSEAEIRELV--------LEKL-----ELVGLPGAadkmpsELSGGMRKR 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   538 IAIARALVRNPKILLLDEATSALDTESEAVVQAALDKARE--GRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDEL 614
Cdd:COG1127  150 VALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDelGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEEL 229

                 ..
gi 6755046   615 MR 616
Cdd:COG1127  230 LA 231
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
391-617 1.05e-42

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 155.99  E-value: 1.05e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   391 LEFKNVHFNYpsrSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYlREIIG 470
Cdd:COG1131    1 IEVRGLTKRY---GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEV-RRRIG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   471 VVSQEPVLFAT-TIAENIRYGRE--DVTMDEIEKAVKEANAydfIMKLPHQFDTLVGergaQLSGGQKQRIAIARALVRN 547
Cdd:COG1131   77 YVPQEPALYPDlTVRENLRFFARlyGLPRKEARERIDELLE---LFGLTDAADRKVG----TLSGGMKQRLGLALALLHD 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6755046   548 PKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIA-HRLSTV-RNADVIAGFDGGVIVEQGNHDELMRE 617
Cdd:COG1131  150 PELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLStHYLEEAeRLCDRVAIIDKGRIVADGTPDELKAR 221
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
1042-1253 1.06e-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: 155.74  E-value: 1.06e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1042 YPTRPN-IPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWL---RAHLGIVSQE 1117
Cdd:cd03257   11 FPTGGGsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirRKEIQMVFQD 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1118 PI-----LFdcSIAENIA-----YGDNSRAvshEEIVRAAKEANIH-----QFIDSLPDkyntrvgdkgtQLSGGQKQRI 1182
Cdd:cd03257   91 PMsslnpRM--TIGEQIAeplriHGKLSKK---EARKEAVLLLLVGvglpeEVLNRYPH-----------ELSGGQRQRV 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6755046  1183 AIARALVRQPHILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHG 1253
Cdd:cd03257  155 AIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
1051-1202 1.21e-42

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: 152.80  E-value: 1.21e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    1051 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGIVSQEPILF-DCSIAENI 1129
Cdd:pfam00005    1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENL 80
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6755046    1130 AYGDNSRAVSHEEIVRAAKEAnIHQFidSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATS 1202
Cdd:pfam00005   81 RLGLLLKGLSKREKDARAEEA-LEKL--GLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
ABC_6TM_TAP cd18572
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ...
97-361 1.72e-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: 157.32  E-value: 1.72e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    97 STLIISNSSleEEMAIYAYYYTGIGAGVLIVAYIQVSLWCLAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTD 176
Cdd:cd18572   24 DAVVADGSR--EAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDATKTGELTSRLTS 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   177 DVSKINDGIGDKIGMFFQSITTFLAGFIIGFISGWKLTLVILAVSPLIGLSS---ALWAKVLtsftNKELQ-AYAKAGAV 252
Cdd:cd18572  102 DCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITkvyGRYYRKL----SKEIQdALAEANQV 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   253 AEEVLAAIRTVIAFGGQQKELERYNKNLEEAKNVGIKKAITASISIGIAYLLVYASYALAFWYGTSLVLSNEYSIGEVLT 332
Cdd:cd18572  178 AEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFYGGHLVLSGRMSAGQLVT 257
                        250       260       270
                 ....*....|....*....|....*....|
gi 6755046   333 -VFFSILLGTfSIGHLAPNIEAFANARGAA 361
Cdd:cd18572  258 fMLYQQQLGE-AFQSLGDVFSSLMQAVGAA 286
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
391-605 2.26e-42

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: 154.57  E-value: 2.26e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   391 LEFKNVHFNYPSRSE-VQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTIN----VRYL 465
Cdd:cd03255    1 IELKNLSKTYGGGGEkVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSekelAAFR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   466 REIIGVVSQEPVLFAT-TIAENIRYGredVTMDEIEKAVKEANAYDFI--MKLPHQFDTLVgergAQLSGGQKQRIAIAR 542
Cdd:cd03255   81 RRHIGFVFQSFNLLPDlTALENVELP---LLLAGVPKKERRERAEELLerVGLGDRLNHYP----SELSGGQQQRVAIAR 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6755046   543 ALVRNPKILLLDEATSALDTE-SEAVVQAALDKAREGRTTIVIA-HRLSTVRNADVIAGFDGGVI 605
Cdd:cd03255  154 ALANDPKIILADEPTGNLDSEtGKEVMELLRELNKEAGTTIVVVtHDPELAEYADRIIELRDGKI 218
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
408-1265 2.77e-42

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: 169.71  E-value: 2.77e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     408 ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQdirtinvrylreiIGVVSQEPVLFATTIAENI 487
Cdd:TIGR01271  441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQTSWIMPGTIKDNI 507
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     488 RYGredVTMDEIE--KAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALD--TE 563
Cdd:TIGR01271  508 IFG---LSYDEYRytSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDvvTE 584
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     564 SEaVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREKGIY---------------------- 621
Cdd:TIGR01271  585 KE-IFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFsslllgleafdnfsaerrnsil 663
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     622 ---------------------------------------------------FKLV---MTQTRGNEI-----EPGNNAYG 642
Cdd:TIGR01271  664 tetlrrvsidgdstvfsgpetikqsfkqpppefaekrkqsiilnpiasarkFSFVqmgPQKAQATTIedavrEPSERKFS 743
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     643 SQSDTDASE-------------------------LTSEESKSPLIRRSIYRSVHRK----QDQE---------RRLS--- 681
Cdd:TIGR01271  744 LVPEDEQGEeslprgnqyhhglqhqaqrrqsvlqLMTHSNRGENRREQLQTSFRKKssitQQNElaseldiysRRLSkds 823
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     682 ---MKEAVDED------------VPLVSFW----RILNLNLSewpYLLVGVLCAVIngciqpVFAIVFSRIVGVF----- 737
Cdd:TIGR01271  824 vyeISEEINEEdlkecfaderenVFETTTWntylRYITTNRN---LVFVLIFCLVI------FLAEVAASLLGLWlitdn 894
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     738 -----SRDDDHETKRQNCNLFS----------LFFLVMGLI-SFVTY-FFQGFTFGKAGEILTKRVRYMVFKSMLRQDIS 800
Cdd:TIGR01271  895 psapnYVDQQHANASSPDVQKPviitptsayyIFYIYVGTAdSVLALgFFRGLPLVHTLLTVSKRLHEQMLHSVLQAPMA 974
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     801 WFDDHKnsTGSLTTRLASDASSVKGAMGARLAVVTQ-NVANLGTGVILSLVYGWqltlLLVVIIPLIVLGGIIEMKLL-S 878
Cdd:TIGR01271  975 VLNTMK--AGRILNRFTKDMAIIDDMLPLTLFDFIQlTLIVLGAIFVVSVLQPY----IFIAAIPVAVIFIMLRAYFLrT 1048
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     879 GQALKdkkQLEISGK--IATEAIENFR---TIVSLTREQKFETMYAQSLQvpyrnamkkahvfgitfsfTQAMMYFSYAA 953
Cdd:TIGR01271 1049 SQQLK---QLESEARspIFSHLITSLKglwTIRAFGRQSYFETLFHKALN-------------------LHTANWFLYLS 1106
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     954 CFRFGAYLVAqqlMTFenvMLVFSAVVFGAMAAGN----------------TSSF------APDYAKAKVSASHIIRIIE 1011
Cdd:TIGR01271 1107 TLRWFQMRID---IIF---VFFFIAVTFIAIGTNQdgegevgiiltlamniLSTLqwavnsSIDVDGLMRSVSRVFKFID 1180
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    1012 KTPEiDSYSTEGLKPTLL-----------------EGNVKFNGVQFNYpTRPNIPVLQGLSLEVKKGQTLALVGSSGCGK 1074
Cdd:TIGR01271 1181 LPQE-EPRPSGGGGKYQLstvlvienphaqkcwpsGGQMDVQGLTAKY-TEAGRAVLQDLSFSVEGGQRVGLLGRTGSGK 1258
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    1075 STVVQLLERFYDpMAGSVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAENIaygDNSRAVSHEEIVRAAKEANIHQ 1154
Cdd:TIGR01271 1259 STLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNL---DPYEQWSDEEIWKVAEEVGLKS 1334
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    1155 FIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLST 1234
Cdd:TIGR01271 1335 VIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEA 1414
                         1050      1060      1070
                   ....*....|....*....|....*....|.
gi 6755046    1235 IQNADLIVVIENGKVKEHGTHQQLLAQKGIY 1265
Cdd:TIGR01271 1415 LLECQQFLVIEGSSVKQYDSIQKLLNETSLF 1445
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
1033-1261 3.20e-42

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: 154.66  E-value: 3.20e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1033 VKFNGVQFNYPTRPN-IPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQ---LLERfydPMAGSVFLDGKEIKQLN---VQ 1105
Cdd:cd03258    2 IELKNVSKVFGDTGGkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRcinGLER---PTSGSVLVDGTDLTLLSgkeLR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1106 WLRAHLGIVSQEPILFDC-SIAENIAYGDNSRAVSHEEIVRAAKE----ANIHQFIDSLPdkyntrvgdkgTQLSGGQKQ 1180
Cdd:cd03258   79 KARRRIGMIFQHFNLLSSrTVFENVALPLEIAGVPKAEIEERVLEllelVGLEDKADAYP-----------AQLSGGQKQ 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1181 RIAIARALVRQPHILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQ 1257
Cdd:cd03258  148 RVGIARALANNPKVLLCDEATSALDPETTQSILALLRDinRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEE 227

                 ....
gi 6755046  1258 LLAQ 1261
Cdd:cd03258  228 VFAN 231
ABC_6TM_exporters cd07346
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ...
50-361 3.72e-42

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: 156.56  E-value: 3.72e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    50 MILGTLAAIIHGTLLPLLMLVFGNMTDSFTKAeasilpsitnqsGPNSTLIIsnssleeemaiYAYYYTGIGAGVLIVAY 129
Cdd:cd07346    1 LLLALLLLLLATALGLALPLLTKLLIDDVIPA------------GDLSLLLW-----------IALLLLLLALLRALLSY 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   130 IQVSLWCLAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDKIGMFFQSITTFLAGFIIGFIS 209
Cdd:cd07346   58 LRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYL 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   210 GWKLTLVILAVSPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQKELERYNKNLEEAKNVGIK 289
Cdd:cd07346  138 NWKLTLVALLLLPLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLR 217
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6755046   290 KAITASISIGIAYLLVYASYALAFWYGTSLVLSNEYSIGEvLTVFFSiLLGTFS--IGHLAPNIEAFANARGAA 361
Cdd:cd07346  218 AARLSALFSPLIGLLTALGTALVLLYGGYLVLQGSLTIGE-LVAFLA-YLGMLFgpIQRLANLYNQLQQALASL 289
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
391-608 5.30e-42

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 153.66  E-value: 5.30e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   391 LEFKNVHFNYPS-RSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTIN----VRYL 465
Cdd:COG1136    5 LELRNLTKSYGTgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSerelARLR 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   466 REIIGVVSQEPVLFAT-TIAENI----RYGREDVtmDEIEKAVKEANAY----DFIMKLPHQfdtlvgergaqLSGGQKQ 536
Cdd:COG1136   85 RRHIGFVFQFFNLLPElTALENValplLLAGVSR--KERRERARELLERvglgDRLDHRPSQ-----------LSGGQQQ 151
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6755046   537 RIAIARALVRNPKILLLDEATSALDTESEAVVQAALDK-AREGRTTIVIA-HRLSTVRNADVIAGFDGGVIVEQ 608
Cdd:COG1136  152 RVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRElNRELGTTIVMVtHDPELAARADRVIRLRDGRIVSD 225
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
391-616 5.31e-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: 5.31e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   391 LEFKNVHFNYPSRSEVqiLKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIG 470
Cdd:cd03295    1 IEFENVTKRYGGGKKA--VNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   471 VVSQEPVLFA-TTIAENI-------RYGREdvtmdEIEKAVKEANAydfIMKLPHQfdTLVGERGAQLSGGQKQRIAIAR 542
Cdd:cd03295   79 YVIQQIGLFPhMTVEENIalvpkllKWPKE-----KIRERADELLA---LVGLDPA--EFADRYPHELSGGQQQRVGVAR 148
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6755046   543 ALVRNPKILLLDEATSALDTESEAVVQAALDKARE--GRTTIVIAHRL-STVRNADVIAGFDGGVIVEQGNHDELMR 616
Cdd:cd03295  149 ALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILR 225
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
391-586 6.24e-42

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


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 154.86  E-value: 6.24e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   391 LEFKNVHFNYPSRS-EVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRylreiI 469
Cdd:COG1116    8 LELRGVSKRFPTGGgGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD-----R 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   470 GVVSQEPVLFA-TTIAENIRYGREDVTMDEiEKAVKEANAY-------DFIMKLPHQfdtlvgergaqLSGGQKQRIAIA 541
Cdd:COG1116   83 GVVFQEPALLPwLTVLDNVALGLELRGVPK-AERRERARELlelvglaGFEDAYPHQ-----------LSGGMRQRVAIA 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 6755046   542 RALVRNPKILLLDEATSALDTESEAVVQAALDK--AREGRTTIVIAH 586
Cdd:COG1116  151 RALANDPEVLLMDEPFGALDALTRERLQDELLRlwQETGKTVLFVTH 197
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
391-617 7.22e-42

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: 156.37  E-value: 7.22e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   391 LEFKNVHFNYPSRS-EVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPL---EGVVSIDGQDIRTINVRYLR 466
Cdd:COG0444    2 LEVRNLKVYFPTRRgVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKLSEKELR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   467 EI----IGVVSQEPvlFA---------TTIAENIRYgREDVTMDEIEKAVKEA-------NAYDFIMKLPHQFdtlvger 526
Cdd:COG0444   82 KIrgreIQMIFQDP--MTslnpvmtvgDQIAEPLRI-HGGLSKAEARERAIELlervglpDPERRLDRYPHEL------- 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   527 gaqlSGGQKQRIAIARALVRNPKILLLDEATSALDteseAVVQAA-LD-----KAREGRTTIVIAHRLSTVRN-ADVIAG 599
Cdd:COG0444  152 ----SGGMRQRVMIARALALEPKLLIADEPTTALD----VTIQAQiLNllkdlQRELGLAILFITHDLGVVAEiADRVAV 223
                        250
                 ....*....|....*...
gi 6755046   600 FDGGVIVEQGNHDELMRE 617
Cdd:COG0444  224 MYAGRIVEEGPVEELFEN 241
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
391-617 8.55e-42

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: 154.05  E-value: 8.55e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   391 LEFKNVHFNYPSRsevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIG 470
Cdd:COG1120    2 LEAENLSVGYGGR---PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   471 VVSQEPVL-FATTIAENIRYGR------------EDvtMDEIEKAVKEANAYDFIMKLphqFDTlvgergaqLSGGQKQR 537
Cdd:COG1120   79 YVPQEPPApFGLTVRELVALGRyphlglfgrpsaED--REAVEEALERTGLEHLADRP---VDE--------LSGGERQR 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   538 IAIARALVRNPKILLLDEATSALDTESEAVVQAALDK--AREGRTTIVIAHRLS-TVRNADVIAGFDGGVIVEQGNHDEL 614
Cdd:COG1120  146 VLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRlaRERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEV 225

                 ...
gi 6755046   615 MRE 617
Cdd:COG1120  226 LTP 228
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
391-586 1.21e-41

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: 152.63  E-value: 1.21e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   391 LEFKNVHFNYPSRS-EVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRylreiI 469
Cdd:cd03293    1 LEVRNVSKTYGGGGgAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD-----R 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   470 GVVSQEPVLFA-TTIAENIRYGRE--DVTMDEIEKAVKEANA----YDFIMKLPHQfdtlvgergaqLSGGQKQRIAIAR 542
Cdd:cd03293   76 GYVFQQDALLPwLTVLDNVALGLElqGVPKAEARERAEELLElvglSGFENAYPHQ-----------LSGGMRQRVALAR 144
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 6755046   543 ALVRNPKILLLDEATSALDTESEAVVQAALDK--AREGRTTIVIAH 586
Cdd:cd03293  145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDiwRETGKTVLLVTH 190
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
391-616 1.33e-41

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: 153.04  E-value: 1.33e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   391 LEFKNVHFNYPSRsevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREI-- 468
Cdd:cd03261    1 IELRGLTKSFGGR---TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLrr 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   469 -IGVVSQEPVLF-ATTIAENIRYG-REDVTMDE--IEKAVKeanaydfiMKLphqfdTLVGERG------AQLSGGQKQR 537
Cdd:cd03261   78 rMGMLFQSGALFdSLTVFENVAFPlREHTRLSEeeIREIVL--------EKL-----EAVGLRGaedlypAELSGGMKKR 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   538 IAIARALVRNPKILLLDEATSALD-TESEAVVQAALD-KAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDEL 614
Cdd:cd03261  145 VALARALALDPELLLYDEPTAGLDpIASGVIDDLIRSlKKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEEL 224

                 ..
gi 6755046   615 MR 616
Cdd:cd03261  225 RA 226
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
1033-1251 1.79e-41

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: 151.86  E-value: 1.79e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1033 VKFNGVQFNYPT-RPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNvqwlrAHL 1111
Cdd:cd03293    1 LEVRNVSKTYGGgGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG-----PDR 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1112 GIVSQEPILFD-CSIAENIAYGDNSRAVSHEEIVRAAKEAnIHQ-----FIDSLPDkyntrvgdkgtQLSGGQKQRIAIA 1185
Cdd:cd03293   76 GYVFQQDALLPwLTVLDNVALGLELQGVPKAEARERAEEL-LELvglsgFENAYPH-----------QLSGGMRQRVALA 143
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6755046  1186 RALVRQPHILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVIEN--GKVKE 1251
Cdd:cd03293  144 RALAVDPDVLLLDEPFSALDALTREQLQEELLDiwRETGKTVLLVTHDIDeAVFLADRVVVLSArpGRIVA 214
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
1049-1261 3.46e-41

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


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 151.69  E-value: 3.46e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1049 PVLQGLSLEVKKGQTLALVGSSGCGKSTV---VQLLERfydPMAGSVFLDGKEI--KQLNVQWLRAHLGIVSQEPILF-D 1122
Cdd:COG1126   15 EVLKGISLDVEKGEVVVIIGPSGSGKSTLlrcINLLEE---PDSGTITVDGEDLtdSKKDINKLRRKVGMVFQQFNLFpH 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1123 CSIAENIAYGD-NSRAVSHEEIVRAAKEAnihqfidsLpdkynTRVG--DKG----TQLSGGQKQRIAIARALVRQPHIL 1195
Cdd:COG1126   92 LTVLENVTLAPiKVKKMSKAEAEERAMEL--------L-----ERVGlaDKAdaypAQLSGGQQQRVAIARALAMEPKVM 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6755046  1196 LLDEATSALDTEsekVVQEALD--K--AREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLLAQ 1261
Cdd:COG1126  159 LFDEPTSALDPE---LVGEVLDvmRdlAKEGMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGPPEEFFEN 226
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
1047-1261 5.18e-41

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 151.37  E-value: 5.18e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1047 NIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWlRAHLGIVSQEPILF-DCSI 1125
Cdd:COG1131   12 DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEV-RRRIGYVPQEPALYpDLTV 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1126 AENIAYGDNSRAVSHEEIVRAAKEAnIHQFidSLPDKYNTRVGdkgtQLSGGQKQRIAIARALVRQPHILLLDEATSALD 1205
Cdd:COG1131   91 RENLRFFARLYGLPRKEARERIDEL-LELF--GLTDAADRKVG----TLSGGMKQRLGLALALLHDPELLILDEPTSGLD 163
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 6755046  1206 TESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLLAQ 1261
Cdd:COG1131  164 PEARRELWELLRElAAEGKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELKAR 221
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
1033-1254 5.24e-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: 155.26  E-value: 5.24e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1033 VKFNGVQFNYPTRPnipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQwlRAHLG 1112
Cdd:COG3842    6 LELENVSKRYGDVT---ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE--KRNVG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1113 IVSQEPILF-DCSIAENIAYGDNSRAVSHEEIVRAAKEA----NIHQFIDSLPDkyntrvgdkgtQLSGGQKQRIAIARA 1187
Cdd:COG3842   81 MVFQDYALFpHLTVAENVAFGLRMRGVPKAEIRARVAELlelvGLEGLADRYPH-----------QLSGGQQQRVALARA 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6755046  1188 LVRQPHILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS---TIqnADLIVVIENGKVKEHGT 1254
Cdd:COG3842  150 LAPEPRVLLLDEPLSALDAKLREEMREELRRlqRELGITFIYVTHDQEealAL--ADRIAVMNDGRIEQVGT 219
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
1033-1261 8.54e-41

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: 158.53  E-value: 8.54e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1033 VKFNGVQFNYPTRPNiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDP---MAGSVFLDGKEIKQLNVQWLRA 1109
Cdd:COG1123    5 LEVRDLSVRYPGGDV-PAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLDGRDLLELSEALRGR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1110 HLGIVSQEPI--LFDCSIAENIAYGDNSRAVSHEEIVRAAKEA----NIHQFIDSLPDkyntrvgdkgtQLSGGQKQRIA 1183
Cdd:COG1123   84 RIGMVFQDPMtqLNPVTVGDQIAEALENLGLSRAEARARVLELleavGLERRLDRYPH-----------QLSGGQRQRVA 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1184 IARALVRQPHILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTI-QNADLIVVIENGKVKEHGTHQQLLA 1260
Cdd:COG1123  153 IAMALALDPDLLIADEPTTALDVTTQAEILDLLRElqRERGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILA 232

                 .
gi 6755046  1261 Q 1261
Cdd:COG1123  233 A 233
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
1042-1260 1.04e-40

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: 150.72  E-value: 1.04e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1042 YPTRP-NIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGIVSQEPIL 1120
Cdd:COG1124   11 YGQGGrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVFQDPYA 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1121 -------FDCSIAE--NIAYGDNSRavshEEIVRAAKEANIH-QFIDSLPDkyntrvgdkgtQLSGGQKQRIAIARALVR 1190
Cdd:COG1124   91 slhprhtVDRILAEplRIHGLPDRE----ERIAELLEQVGLPpSFLDRYPH-----------QLSGGQRQRVAIARALIL 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6755046  1191 QPHILLLDEATSALDTesekVVQ-EALD-----KAREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLLA 1260
Cdd:COG1124  156 EPELLLLDEPTSALDV----SVQaEILNllkdlREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLA 228
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
115-624 1.09e-40

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: 164.73  E-value: 1.09e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     115 YYYTGIGAGVLIVAY-IQVSLWCLAAGRQIHkirQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDKIGMFF 193
Cdd:TIGR00957 1011 YGALGILQGFAVFGYsMAVSIGGIQASRVLH---QDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFM 1087
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     194 QSITTFLAGFIIGFISGWKLTLVILAVSPLIGLSSALWakVLTSFTNKELQAYAKAGAVAE--EVLAAIRTVIAFGGQQK 271
Cdd:TIGR00957 1088 GSLFNVIGALIVILLATPIAAVIIPPLGLLYFFVQRFY--VASSRQLKRLESVSRSPVYSHfnETLLGVSVIRAFEEQER 1165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     272 ELERYNKNLEEAKnvgikKAITASI------SIGIAYL-----LVYASYALAFWYGTS--LV-LSNEYSIGevLTVFFSI 337
Cdd:TIGR00957 1166 FIHQSDLKVDENQ-----KAYYPSIvanrwlAVRLECVgncivLFAALFAVISRHSLSagLVgLSVSYSLQ--VTFYLNW 1238
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     338 LLGTFSigHLAPNIeafanargAAFEIFKIIDNEPSIDSFSTKGYKPDSI---MGNLEFKNVHFNYpsRSEVQ-ILKGLN 413
Cdd:TIGR00957 1239 LVRMSS--EMETNI--------VAVERLKEYSETEKEAPWQIQETAPPSGwppRGRVEFRNYCLRY--REDLDlVLRHIN 1306
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     414 LKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENI----RY 489
Cdd:TIGR00957 1307 VTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLdpfsQY 1386
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     490 GREDVTMdeiekAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQ 569
Cdd:TIGR00957 1387 SDEEVWW-----ALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQ 1461
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 6755046     570 AALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREKGIYFKL 624
Cdd:TIGR00957 1462 STIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSM 1516
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
391-605 1.73e-40

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: 148.83  E-value: 1.73e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   391 LEFKNVHFNYpsrSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDI--RTINVRYLREI 468
Cdd:cd03262    1 IEIKNLHKSF---GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQK 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   469 IGVVSQEPVLFA-TTIAENIRYGRedVTMDEIEKAVKEANAYDFIMK--LPHQFDtlvgERGAQLSGGQKQRIAIARALV 545
Cdd:cd03262   78 VGMVFQQFNLFPhLTVLENITLAP--IKVKGMSKAEAEERALELLEKvgLADKAD----AYPAQLSGGQQQRVAIARALA 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6755046   546 RNPKILLLDEATSALDTE-SEAVVQAALDKAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVI 605
Cdd:cd03262  152 MNPKVMLFDEPTSALDPElVGEVLDVMKDLAEEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
391-603 2.00e-40

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: 147.33  E-value: 2.00e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   391 LEFKNVHFNYPsrsEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRT--INVRYLREI 468
Cdd:cd03229    1 LELKNVSKRYG---QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDleDELPPLRRR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   469 IGVVSQEPVLFAT-TIAENIRYGredvtmdeiekavkeanaydfimklphqfdtlvgergaqLSGGQKQRIAIARALVRN 547
Cdd:cd03229   78 IGMVFQDFALFPHlTVLENIALG---------------------------------------LSGGQQQRVALARALAMD 118
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 6755046   548 PKILLLDEATSALDTESEAVVQAALD--KAREGRTTIVIAHRLSTVRN-ADVIAGFDGG 603
Cdd:cd03229  119 PDVLLLDEPTSALDPITRREVRALLKslQAQLGITVVLVTHDLDEAARlADRVVVLRDG 177
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
1033-1259 3.57e-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: 149.42  E-value: 3.57e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1033 VKFNGVQFNYPTRPnipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLG 1112
Cdd:COG1120    2 LEAENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1113 IVSQEPIL-FDCSIAENIAYG-----DNSRAVSHE--EIVRAA-KEANIHQFIDslpdkynTRVgdkgTQLSGGQKQRIA 1183
Cdd:COG1120   79 YVPQEPPApFGLTVRELVALGryphlGLFGRPSAEdrEAVEEAlERTGLEHLAD-------RPV----DELSGGERQRVL 147
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6755046  1184 IARALVRQPHILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVIENGKVKEHGTHQQLL 1259
Cdd:COG1120  148 IARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRlaRERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEVL 226
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
1033-1251 3.60e-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: 149.47  E-value: 3.60e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1033 VKFNGVQFNYPTRPN-IPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLnvqwlRAHL 1111
Cdd:COG1116    8 LELRGVSKRFPTGGGgVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGP-----GPDR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1112 GIVSQEPILFD-CSIAENIAYGDNSRAVSHEEIVRAAKEA----NIHQFIDSLPDkyntrvgdkgtQLSGGQKQRIAIAR 1186
Cdd:COG1116   83 GVVFQEPALLPwLTVLDNVALGLELRGVPKAERRERARELlelvGLAGFEDAYPH-----------QLSGGMRQRVAIAR 151
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6755046  1187 ALVRQPHILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAH------RLstiqnADLIVVIEN--GKVKE 1251
Cdd:COG1116  152 ALANDPEVLLMDEPFGALDALTRERLQDELLRlwQETGKTVLFVTHdvdeavFL-----ADRVVVLSArpGRIVE 221
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
392-603 4.67e-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: 4.67e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   392 EFKNVHFNYPSRsevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIGV 471
Cdd:cd00267    1 EIENLSFRYGGR---TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   472 VSQepvlfattiaenirygredvtmdeiekavkeanaydfimklphqfdtlvgergaqLSGGQKQRIAIARALVRNPKIL 551
Cdd:cd00267   78 VPQ-------------------------------------------------------LSGGQRQRVALARALLLNPDLL 102
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 6755046   552 LLDEATSALDTESEAVVQAALDK-AREGRTTIVIAHRLSTVRNA-DVIAGFDGG 603
Cdd:cd00267  103 LLDEPTSGLDPASRERLLELLRElAEEGRTVIIVTHDPELAELAaDRVIVLKDG 156
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
1033-1248 6.16e-40

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: 146.85  E-value: 6.16e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1033 VKFNGVQFNYPTRPNI--PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL--ErfYDPMAGSVFLDGKeikqlnvqwlr 1108
Cdd:cd03250    1 ISVEDASFTWDSGEQEtsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALlgE--LEKLSGSVSVPGS----------- 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1109 ahLGIVSQEPILFDCSIAENIAYG---DNSRavsHEEIVRAAKeanIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIA 1185
Cdd:cd03250   68 --IAYVSQEPWIQNGTIRENILFGkpfDEER---YEKVIKACA---LEPDLEILPDGDLTEIGEKGINLSGGQKQRISLA 139
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6755046  1186 RALVRQPHILLLDEATSALDTES-----EKVVQEALdkaREGRTCIVIAHRLSTIQNADLIVVIENGK 1248
Cdd:cd03250  140 RAVYSDADIYLLDDPLSAVDAHVgrhifENCILGLL---LNNKTRILVTHQLQLLPHADQIVVLDNGR 204
ECF_ATPase_1 TIGR04520
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
1033-1262 8.66e-40

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: 148.73  E-value: 8.66e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    1033 VKFNGVQFNYPtRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIK-QLNVQWLRAHL 1111
Cdd:TIGR04520    1 IEVENVSFSYP-ESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLdEENLWEIRKKV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    1112 GIVSQEPilfD----CSIAEN-IAYGDNSRAVSHEEIVR----AAKEANIHQFIDSLPdkyntrvgdkgTQLSGGQKQRI 1182
Cdd:TIGR04520   80 GMVFQNP---DnqfvGATVEDdVAFGLENLGVPREEMRKrvdeALKLVGMEDFRDREP-----------HLLSGGQKQRV 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    1183 AIARALVRQPHILLLDEATSALDTESEKVVQEALDKAR--EGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLA 1260
Cdd:TIGR04520  146 AIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNkeEGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPREIFS 225

                   ..
gi 6755046    1261 QK 1262
Cdd:TIGR04520  226 QV 227
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
391-614 9.69e-40

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


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 148.26  E-value: 9.69e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   391 LEFKNVHFNYpsrSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYD--P---LEGVVSIDGQDI--RTINVR 463
Cdd:COG1117   12 IEVRNLNVYY---GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPgarVEGEILLDGEDIydPDVDVV 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   464 YLREIIGVVSQEPVLFATTIAENIRYG------REDVTMDEI-EKAVKEANAYDFImKlphqfDTLvGERGAQLSGGQKQ 536
Cdd:COG1117   89 ELRRRVGMVFQKPNPFPKSIYDNVAYGlrlhgiKSKSELDEIvEESLRKAALWDEV-K-----DRL-KKSALGLSGGQQQ 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   537 RIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREgRTTIVI-------AHRLStvrnaDVIAGFDGGVIVEQG 609
Cdd:COG1117  162 RLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKK-DYTIVIvthnmqqAARVS-----DYTAFFYLGELVEFG 235

                 ....*
gi 6755046   610 NHDEL 614
Cdd:COG1117  236 PTEQI 240
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
1033-1249 1.08e-39

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: 146.87  E-value: 1.08e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1033 VKFNGVQFNYPTRPN-IPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWL---- 1107
Cdd:cd03255    1 IELKNLSKTYGGGGEkVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1108 RAHLGIVSQE----PILfdcSIAENIAYGDNSRAVSHEEIVRAAKEAnihqfIDS--LPDKYNTRVGdkgtQLSGGQKQR 1181
Cdd:cd03255   81 RRHIGFVFQSfnllPDL---TALENVELPLLLAGVPKKERRERAEEL-----LERvgLGDRLNHYPS----ELSGGQQQR 148
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1182 IAIARALVRQPHILLLDEATSALDTESEKVVQEAL-DKAREGRTCIVIA-HRLSTIQNADLIVVIENGKV 1249
Cdd:cd03255  149 VAIARALANDPKIILADEPTGNLDSETGKEVMELLrELNKEAGTTIVVVtHDPELAEYADRIIELRDGKI 218
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
1033-1254 1.78e-39

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 150.23  E-value: 1.78e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1033 VKFNGVQFNYPTRPN-IPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQ---LLERfydPMAGSVFLDGKEIKQLNVQWLR 1108
Cdd:COG1135    2 IELENLSKTFPTKGGpVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRcinLLER---PTSGSVLVDGVDLTALSERELR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1109 A---HLGIVSQEPILFD-CSIAENIAY-----GdnsraVSHEEIvrAAKeanihqfIDSLPDkyntRVG--DKG----TQ 1173
Cdd:COG1135   79 AarrKIGMIFQHFNLLSsRTVAENVALpleiaG-----VPKAEI--RKR-------VAELLE----LVGlsDKAdaypSQ 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1174 LSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVIENGKVK 1250
Cdd:COG1135  141 LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRelGLTIVLITHEMDVVRRiCDRVAVLENGRIV 220

                 ....
gi 6755046  1251 EHGT 1254
Cdd:COG1135  221 EQGP 224
PLN03232 PLN03232
ABC transporter C family member; Provisional
61-641 2.19e-39

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 160.14  E-value: 2.19e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     61 GTLLPLLMLVFGNMTDSFTKAEASILPSITNQSGPNSTliisnssleeEMAIYAYYYTGIGAGVLIVAYIQvSLW----C 136
Cdd:PLN03232  910 GLWVVMILLVCYLTTEVLRVSSSTWLSIWTDQSTPKSY----------SPGFYIVVYALLGFGQVAVTFTN-SFWlissS 978
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    137 LAAGRQIHkirQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDKIGMFFQSITTFLAGF-IIGFISgwklTL 215
Cdd:PLN03232  979 LHAAKRLH---DAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFMNQLWQLLSTFaLIGTVS----TI 1051
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    216 VILAVSPLIGL---------SSALWAKVLTSFTNKELqaYAKAGAvAEEVLAAIRTVIAFGGQQKELERYNKNleeakNV 286
Cdd:PLN03232 1052 SLWAIMPLLILfyaaylyyqSTSREVRRLDSVTRSPI--YAQFGE-ALNGLSSIRAYKAYDRMAKINGKSMDN-----NI 1123
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    287 GIKKAITAS--------ISIGIAYLLVYASYALaFWYGTSlvlSNEYSIGEVLTVFFS-------ILLGTFSIGHLAPN- 350
Cdd:PLN03232 1124 RFTLANTSSnrwltirlETLGGVMIWLTATFAV-LRNGNA---ENQAGFASTMGLLLSytlnittLLSGVLRQASKAENs 1199
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    351 ---IEAFANARGAAFEIFKIIDNEPSIDSFSTKGykpdsimgNLEFKNVHFNYpsRSEVQ-ILKGLNLKVKSGQTVALVG 426
Cdd:PLN03232 1200 lnsVERVGNYIDLPSEATAIIENNRPVSGWPSRG--------SIKFEDVHLRY--RPGLPpVLHGLSFFVSPSEKVGVVG 1269
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    427 NSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENIRYGREDVTMDeIEKAVKEA 506
Cdd:PLN03232 1270 RTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDAD-LWEALERA 1348
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    507 NAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAH 586
Cdd:PLN03232 1349 HIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAH 1428
                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 6755046    587 RLSTVRNADVIAGFDGGVIVEQGNHDELM-REKGIYFKlvMTQTRGneiePGNNAY 641
Cdd:PLN03232 1429 RLNTIIDCDKILVLSSGQVLEYDSPQELLsRDTSAFFR--MVHSTG----PANAQY 1478
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
388-609 6.19e-39

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 149.09  E-value: 6.19e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   388 MGNLEFKNVHFNYpsrSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVrYLRE 467
Cdd:COG3842    3 MPALELENVSKRY---GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPP-EKRN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   468 IiGVVSQEPVLFA-TTIAENIRYG--REDVTMDEIEKAVKEANAydfIMKLPHQFDTLVgergAQLSGGQKQRIAIARAL 544
Cdd:COG3842   79 V-GMVFQDYALFPhLTVAENVAFGlrMRGVPKAEIRARVAELLE---LVGLEGLADRYP----HQLSGGQQQRVALARAL 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   545 VRNPKILLLDEATSALDTESEAVVQAALDK--AREGRTTIVIAHRLS---TVrnADVIAGFDGGVIVEQG 609
Cdd:COG3842  151 APEPRVLLLDEPLSALDAKLREEMREELRRlqRELGITFIYVTHDQEealAL--ADRIAVMNDGRIEQVG 218
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
1033-1260 7.16e-39

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: 145.14  E-value: 7.16e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1033 VKFNGVQFNYPTRPniPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLG 1112
Cdd:cd03295    1 IEFENVTKRYGGGK--KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1113 IVSQEPILF-DCSIAENIAYGDNSRAVSHEEIVRAAKEanIHQFIDSLPDKYNTRVGDkgtQLSGGQKQRIAIARALVRQ 1191
Cdd:cd03295   79 YVIQQIGLFpHMTVEENIALVPKLLKWPKEKIRERADE--LLALVGLDPAEFADRYPH---ELSGGQQQRVGVARALAAD 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6755046  1192 PHILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRL-STIQNADLIVVIENGKVKEHGTHQQLLA 1260
Cdd:cd03295  154 PPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILR 225
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
1033-1264 9.28e-39

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 145.90  E-value: 9.28e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1033 VKFNGVQFNYPTRPNiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLG 1112
Cdd:PRK13632    8 IKVENVSFSYPNSEN-NALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1113 IVSQEPilfD-----CSIAENIAYGDNSRAVSHEE----IVRAAKEANIHQFIDSLPDKyntrvgdkgtqLSGGQKQRIA 1183
Cdd:PRK13632   87 IIFQNP---DnqfigATVEDDIAFGLENKKVPPKKmkdiIDDLAKKVGMEDYLDKEPQN-----------LSGGQKQRVA 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1184 IARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGR--TCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQ 1261
Cdd:PRK13632  153 IASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNN 232

                  ...
gi 6755046   1262 KGI 1264
Cdd:PRK13632  233 KEI 235
ABC_6TM_ABCB10_like cd18573
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ...
102-334 9.67e-39

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: 146.51  E-value: 9.67e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   102 SNSSLEEEMAIYAYYYTGIGAGVLIVA----YIQVSLWCLAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDD 177
Cdd:cd18573   28 KESGDIEIFGLSLKTFALALLGVFVVGaaanFGRVYLLRIAGERIVARLRKRLFKSILRQDAAFFDKNKTGELVSRLSSD 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   178 VSKINDGIGDKIGMFFQSITTFLAGFIIGFISGWKLTLVILAVSPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVL 257
Cdd:cd18573  108 TSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRYVRKLSKQVQDALADATKVAEERL 187
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6755046   258 AAIRTVIAFGGQQKELERYNKNLEEAKNVGIKKAITASISIGIAYLLVYASYALAFWYGTSLVLSNEYSIGEvLTVF 334
Cdd:cd18573  188 SNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLLSVLYYGGSLVASGELTVGD-LTSF 263
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
392-620 1.02e-38

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 145.90  E-value: 1.02e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    392 EFKNVHFNYPSrSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIGV 471
Cdd:PRK13632    9 KVENVSFSYPN-SENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    472 VSQEP---VLFATT---IA---ENIRYGREDVTmDEIEKAVKEANAYDFIMKLPHqfdtlvgergaQLSGGQKQRIAIAR 542
Cdd:PRK13632   88 IFQNPdnqFIGATVeddIAfglENKKVPPKKMK-DIIDDLAKKVGMEDYLDKEPQ-----------NLSGGQKQRVAIAS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    543 ALVRNPKILLLDEATSALDTESEAVVQAALDKAREGR--TTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREKGI 620
Cdd:PRK13632  156 VLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNKEI 235
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
391-619 1.83e-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: 144.23  E-value: 1.83e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   391 LEFKNVHFNYpsrSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIiG 470
Cdd:COG4555    2 IEVENLSKKY---GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQI-G 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   471 VVSQEPVLFAT-TIAENIRYGRE--DVTMDEIEKAVKEanaYDFIMKLPHQFDTLVGErgaqLSGGQKQRIAIARALVRN 547
Cdd:COG4555   78 VLPDERGLYDRlTVRENIRYFAElyGLFDEELKKRIEE---LIELLGLEEFLDRRVGE----LSTGMKKKVALARALVHD 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6755046   548 PKILLLDEATSALDTES-EAVVQAALDKAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDELMREKG 619
Cdd:COG4555  151 PKVLLLDEPTNGLDVMArRLLREILRALKKEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
1044-1248 1.99e-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: 141.56  E-value: 1.99e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1044 TRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLN--VQWLRAHLGIVSQEPILF 1121
Cdd:cd03229    9 RYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRRIGMVFQDFALF 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1122 -DCSIAENIAYGdnsravsheeivraakeanihqfidslpdkyntrvgdkgtqLSGGQKQRIAIARALVRQPHILLLDEA 1200
Cdd:cd03229   89 pHLTVLENIALG-----------------------------------------LSGGQQQRVALARALAMDPDVLLLDEP 127
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 6755046  1201 TSALDTESEKVVQEALD--KAREGRTCIVIAHRLSTIQN-ADLIVVIENGK 1248
Cdd:cd03229  128 TSALDPITRREVRALLKslQAQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
1034-1248 2.00e-38

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: 140.84  E-value: 2.00e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1034 KFNGVQFNYPTRPnipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGI 1113
Cdd:cd00267    1 EIENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1114 VSQepilfdcsiaeniaygdnsravsheeivraakeanihqfidslpdkyntrvgdkgtqLSGGQKQRIAIARALVRQPH 1193
Cdd:cd00267   78 VPQ---------------------------------------------------------LSGGQRQRVALARALLLNPD 100
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 6755046  1194 ILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQNA-DLIVVIENGK 1248
Cdd:cd00267  101 LLLLDEPTSGLDPASRERLLELLRElAEEGRTVIIVTHDPELAELAaDRVIVLKDGK 157
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
1050-1258 2.37e-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: 2.37e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD--P---MAGSVFLDGKEI--KQLNVQWLRAHLGIVSQEPILFD 1122
Cdd:COG1117   26 ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPgarVEGEILLDGEDIydPDVDVVELRRRVGMVFQKPNPFP 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1123 CSIAENIAYG-----DNSRAVsHEEIVRAA-KEANihqfidsLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILL 1196
Cdd:COG1117  106 KSIYDNVAYGlrlhgIKSKSE-LDEIVEESlRKAA-------LWDEVKDRLKKSALGLSGGQQQRLCIARALAVEPEVLL 177
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6755046  1197 LDEATSALDTESEKVVQEALDKAREgRTCIVI-------AHRLStiqnaDLIVVIENGKVKEHGTHQQL 1258
Cdd:COG1117  178 MDEPTSALDPISTAKIEELILELKK-DYTIVIvthnmqqAARVS-----DYTAFFYLGELVEFGPTEQI 240
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
1049-1260 2.91e-38

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: 143.58  E-value: 2.91e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1049 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNV---QWLRAHLGIVSQEPILFDC-S 1124
Cdd:COG1127   19 VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEkelYELRRRIGMLFQGGALFDSlT 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1125 IAENIAYG-DNSRAVSHEEIVRAAKEA----NIHQFIDSLPDkyntrvgdkgtQLSGGQKQRIAIARALVRQPHILLLDE 1199
Cdd:COG1127   99 VFENVAFPlREHTDLSEAEIRELVLEKlelvGLPGAADKMPS-----------ELSGGMRKRVALARALALDPEILLYDE 167
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6755046  1200 ATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLLA 1260
Cdd:COG1127  168 PTAGLDPITSAVIDELIRELRDelGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLA 231
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
1036-1261 4.15e-38

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 144.39  E-value: 4.15e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1036 NGVQFNYPTRPNiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGIVS 1115
Cdd:PRK13635    9 EHISFRYPDAAT-YALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGMVF 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1116 QEPilfD-----CSIAENIAYGDNSRAVSHEEIVR----AAKEANIHQFIDSLPdkyntrvgdkgTQLSGGQKQRIAIAR 1186
Cdd:PRK13635   88 QNP---DnqfvgATVQDDVAFGLENIGVPREEMVErvdqALRQVGMEDFLNREP-----------HRLSGGQKQRVAIAG 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1187 ALVRQPHILLLDEATSALDTESEkvvQEALD-----KAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQ 1261
Cdd:PRK13635  154 VLALQPDIIILDEATSMLDPRGR---REVLEtvrqlKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKS 230
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
388-561 1.32e-37

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


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 145.22  E-value: 1.32e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   388 MGNLEFKNVHFNYpsrSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYlRE 467
Cdd:COG3839    1 MASLELENVSKSY---GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD-RN 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   468 IiGVVSQEPVLF-ATTIAENIRYG--REDVTMDEIEKAVKEANAydfIMKLPHQFDTLVgergAQLSGGQKQRIAIARAL 544
Cdd:COG3839   77 I-AMVFQSYALYpHMTVYENIAFPlkLRKVPKAEIDRRVREAAE---LLGLEDLLDRKP----KQLSGGQRQRVALGRAL 148
                        170
                 ....*....|....*..
gi 6755046   545 VRNPKILLLDEATSALD 561
Cdd:COG3839  149 VREPKVFLLDEPLSNLD 165
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
1033-1260 1.40e-37

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: 141.49  E-value: 1.40e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1033 VKFNGVQFNYPTRPnipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNV---QWLRA 1109
Cdd:cd03261    1 IELRGLTKSFGGRT---VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEaelYRLRR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1110 HLGIVSQEPILFDC-SIAENIAYGDNS-RAVSHEEIVRAAKE----ANIHQFIDSLPDkyntrvgdkgtQLSGGQKQRIA 1183
Cdd:cd03261   78 RMGMLFQSGALFDSlTVFENVAFPLREhTRLSEEEIREIVLEkleaVGLRGAEDLYPA-----------ELSGGMKKRVA 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1184 IARALVRQPHILLLDEATSALD-TESEKVVQEALD-KAREGRTCIVIAHRLSTI-QNADLIVVIENGKVKEHGTHQQLLA 1260
Cdd:cd03261  147 LARALALDPELLLYDEPTAGLDpIASGVIDDLIRSlKKELGLTSIMVTHDLDTAfAIADRIAVLYDGKIVAEGTPEELRA 226
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
1034-1263 2.11e-37

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: 141.15  E-value: 2.11e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1034 KFNGVQFNYPtrpNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNvQWLRAHLGI 1113
Cdd:COG4555    3 EVENLSKKYG---KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEP-REARRQIGV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1114 VSQEPILFD-CSIAENIAYGDNSRAVSHEEIVRAAKEAnIHQFIdsLPDKYNTRVGDkgtqLSGGQKQRIAIARALVRQP 1192
Cdd:COG4555   79 LPDERGLYDrLTVRENIRYFAELYGLFDEELKKRIEEL-IELLG--LEEFLDRRVGE----LSTGMKKKVALARALVHDP 151
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6755046  1193 HILLLDEATSALDTESEKVVQEALDKAREGRTCIVIA-HRLSTIQN-ADLIVVIENGKVKEHGTHQQLLAQKG 1263
Cdd:COG4555  152 KVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSsHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
ABCC_SUR2 cd03288
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...
1049-1271 2.22e-37

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: 141.58  E-value: 2.22e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1049 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAEN 1128
Cdd:cd03288   35 PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFN 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1129 IaygDNSRAVSHEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTES 1208
Cdd:cd03288  115 L---DPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMAT 191
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6755046  1209 EKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQK-GIYFSMVQA 1271
Cdd:cd03288  192 ENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEdGVFASLVRT 255
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
391-607 2.35e-37

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 140.19  E-value: 2.35e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   391 LEFKNVHFNYPSrsEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTIN---VRYLRE 467
Cdd:COG2884    2 IRFENVSKRYPG--GREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrreIPYLRR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   468 IIGVVSQE-PVLFATTIAENIRY-----GREDvtmDEIEKAVKEA----NAYDFIMKLPHQfdtlvgergaqLSGGQKQR 537
Cdd:COG2884   80 RIGVVFQDfRLLPDRTVYENVALplrvtGKSR---KEIRRRVREVldlvGLSDKAKALPHE-----------LSGGEQQR 145
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6755046   538 IAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIA-HRLSTVRNAD--VIAgFDGGVIVE 607
Cdd:COG2884  146 VAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIAtHDLELVDRMPkrVLE-LEDGRLVR 217
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
1055-1261 6.21e-37

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: 140.47  E-value: 6.21e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1055 SLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRA----HLGIVSQEPILF-DCSIAENI 1129
Cdd:cd03294   44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkKISMVFQSFALLpHRTVLENV 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1130 AYGDNSRAVSHEEIVRAAKEA----NIHQFIDSLPDkyntrvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEATSALD 1205
Cdd:cd03294  124 AFGLEVQGVPRAEREERAAEAlelvGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 6755046  1206 TESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVIENGKVKEHGTHQQLLAQ 1261
Cdd:cd03294  193 PLIRREMQDELLRlqAELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILTN 251
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
406-617 1.55e-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: 1.55e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   406 VQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREI---IGVVSQEPvlFA-- 480
Cdd:COG4608   31 VKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLrrrMQMVFQDP--YAsl 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   481 -------TTIAENIRYgREDVTMDEIEKAVKEA------NAyDFIMKLPHQFdtlvgergaqlSGGQKQRIAIARALVRN 547
Cdd:COG4608  109 nprmtvgDIIAEPLRI-HGLASKAERRERVAELlelvglRP-EHADRYPHEF-----------SGGQRQRIGIARALALN 175
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6755046   548 PKILLLDEATSALDteseaV-VQAA-----LD-KAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDELMRE 617
Cdd:COG4608  176 PKLIVCDEPVSALD-----VsIQAQvlnllEDlQDELGLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDELYAR 248
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
391-617 2.90e-36

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 137.91  E-value: 2.90e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   391 LEFKNVHFNYPSRsevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRylreiIG 470
Cdd:COG1121    7 IELENLTVSYGGR---PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRR-----IG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   471 VVSQEPVL---FATTIAENI------------RYGREDVtmDEIEKAVKEANAYDFImklphqfDTLVGErgaqLSGGQK 535
Cdd:COG1121   79 YVPQRAEVdwdFPITVRDVVlmgrygrrglfrRPSRADR--EAVDEALERVGLEDLA-------DRPIGE----LSGGQQ 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   536 QRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDK-AREGRTTIVIAHRLSTVR-NADVIAGFDGGVIVEqGNHDE 613
Cdd:COG1121  146 QRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVReYFDRVLLLNRGLVAH-GPPEE 224

                 ....
gi 6755046   614 LMRE 617
Cdd:COG1121  225 VLTP 228
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
392-609 3.60e-36

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 140.71  E-value: 3.60e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    392 EFKNVHFNYPSRS-EVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREI-- 468
Cdd:PRK11153    3 ELKNISKVFPQGGrTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKArr 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    469 -IGVVSQEPVLFAT-TIAENIRYGRE--DVTMDEIEKAVKE----------ANAYdfimklPhqfdtlvgergAQLSGGQ 534
Cdd:PRK11153   83 qIGMIFQHFNLLSSrTVFDNVALPLElaGTPKAEIKARVTEllelvglsdkADRY------P-----------AQLSGGQ 145
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6755046    535 KQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKA-REGRTTIV-IAHRLSTVRN-ADVIAGFDGGVIVEQG 609
Cdd:PRK11153  146 KQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDInRELGLTIVlITHEMDVVKRiCDRVAVIDAGRLVEQG 223
PLN03130 PLN03130
ABC transporter C family member; Provisional
113-664 6.87e-36

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 149.12  E-value: 6.87e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    113 YAYYYTGIGAGVLIVAYIQvSLW----CLAAGRQIHkirQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDK 188
Cdd:PLN03130  955 YNLIYALLSFGQVLVTLLN-SYWlimsSLYAAKRLH---DAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVAVF 1030
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    189 IGMFFQSITTFLAGFI-IGFISgwklTLVILAVSPLIGL---------SSALWAKVLTSFTNKELqaYAKAGAvAEEVLA 258
Cdd:PLN03130 1031 VNMFLGQIFQLLSTFVlIGIVS----TISLWAIMPLLVLfygaylyyqSTAREVKRLDSITRSPV--YAQFGE-ALNGLS 1103
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    259 AIRTVIAF-------GGQQKELERYN-KNLEEAKNVGIKKAITASISIGI-AYLLVY----ASYALAFWYGTSLVLSNEY 325
Cdd:PLN03130 1104 TIRAYKAYdrmaeinGRSMDNNIRFTlVNMSSNRWLAIRLETLGGLMIWLtASFAVMqngrAENQAAFASTMGLLLSYAL 1183
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    326 SIGEVLTvffsillGTFSIGHLAPN----IEAFANARGAAFEIFKII-DNEPSidsfstKGYkPDSimGNLEFKNVHFNY 400
Cdd:PLN03130 1184 NITSLLT-------AVLRLASLAENslnaVERVGTYIDLPSEAPLVIeNNRPP------PGW-PSS--GSIKFEDVVLRY 1247
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    401 psRSEVQ-ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIGVVSQEPVLF 479
Cdd:PLN03130 1248 --RPELPpVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLF 1325
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    480 ATTIAENIRYGREDVTMDEIEkAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSA 559
Cdd:PLN03130 1326 SGTVRFNLDPFNEHNDADLWE-SLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAA 1404
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    560 LDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREKGIYFKlVMTQTRGneiePGNN 639
Cdd:PLN03130 1405 VDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFS-KMVQSTG----AANA 1479
                         570       580
                  ....*....|....*....|....*...
gi 6755046    640 AYgSQS---DTDASELTSEESKSPLIRR 664
Cdd:PLN03130 1480 QY-LRSlvfGGDEDRLAREESKALDGQR 1506
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
1033-1253 7.98e-36

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 135.95  E-value: 7.98e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1033 VKFNGVQFNYPtrPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLN---VQWLRA 1109
Cdd:COG2884    2 IRFENVSKRYP--GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrreIPYLRR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1110 HLGIVSQE-PILFDCSIAENIAY-----GdnsraVSHEEIVRAAKEA----NIHQFIDSLPDkyntrvgdkgtQLSGGQK 1179
Cdd:COG2884   80 RIGVVFQDfRLLPDRTVYENVALplrvtG-----KSRKEIRRRVREVldlvGLSDKAKALPH-----------ELSGGEQ 143
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6755046  1180 QRIAIARALVRQPHILLLDEATSALDTE-SEKVVqEALDKAREGRTCIVIA-HRLSTIQNADL-IVVIENGKVKEHG 1253
Cdd:COG2884  144 QRVAIARALVNRPELLLADEPTGNLDPEtSWEIM-ELLEEINRRGTTVLIAtHDLELVDRMPKrVLELEDGRLVRDE 219
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
391-605 9.78e-36

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: 133.68  E-value: 9.78e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   391 LEFKNVHFNYPSRsevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTiNVRYLREIIG 470
Cdd:cd03230    1 IEVRNLSKRYGKK---TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   471 VVSQEPVLFAT-TIAENIRYgredvtmdeiekavkeanaydfimklphqfdtlvgergaqlSGGQKQRIAIARALVRNPK 549
Cdd:cd03230   77 YLPEEPSLYENlTVRENLKL-----------------------------------------SGGMKQRLALAQALLHDPE 115
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 6755046   550 ILLLDEATSALDTESEAVVQAALDK-AREGRTTIVIAHRLSTVRN-ADVIAGFDGGVI 605
Cdd:cd03230  116 LLILDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
391-597 1.90e-35

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: 134.13  E-value: 1.90e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   391 LEFKNVHFNYPSRSEVQ--ILKGLNLKVKSGQTVALVGNSGCGKSTTVQ-LMQRLyDPLEGVVSIDGQdirtinvrylre 467
Cdd:cd03250    1 ISVEDASFTWDSGEQETsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSaLLGEL-EKLSGSVSVPGS------------ 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   468 iIGVVSQEPVLFATTIAENIRYGREdvtMDEIE-KAVKEANA--YDFIMkLPHQFDTLVGERGAQLSGGQKQRIAIARAL 544
Cdd:cd03250   68 -IAYVSQEPWIQNGTIRENILFGKP---FDEERyEKVIKACAlePDLEI-LPDGDLTEIGEKGINLSGGQKQRISLARAV 142
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 6755046   545 VRNPKILLLDEATSALDTESEA-----VVQAALdkaREGRTTIVIAHRLSTVRNADVI 597
Cdd:cd03250  143 YSDADIYLLDDPLSAVDAHVGRhifenCILGLL---LNNKTRILVTHQLQLLPHADQI 197
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
1050-1259 4.33e-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: 134.00  E-value: 4.33e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQwlRAHLGIVSQEPILF-DCSIAEN 1128
Cdd:cd03299   14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFpHMTVYKN 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1129 IAYGDNSRAVSHEEIVRAAKEANIHQFIDSLPDKYNTRvgdkgtqLSGGQKQRIAIARALVRQPHILLLDEATSALDTES 1208
Cdd:cd03299   92 IAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPET-------LSGGEQQRVAIARALVVNPKILLLDEPFSALDVRT 164
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 6755046  1209 EKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLL 1259
Cdd:cd03299  165 KEKLREELKKIRKefGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVF 218
ABC_6TM_TAP_ABCB8_10_like cd18557
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ...
709-1004 4.72e-35

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: 135.77  E-value: 4.72e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   709 LLVGVLCAVIngciQPVFaivFSRIVGVFSRDDDHETKRQNCNLFSLFFLVMGLISFVTYFFqgftFGKAGEILTKRVRY 788
Cdd:cd18557    5 LLISSAAQLL----LPYL---IGRLIDTIIKGGDLDVLNELALILLAIYLLQSVFTFVRYYL----FNIAGERIVARLRR 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   789 MVFKSMLRQDISWFDDHKnsTGSLTTRLASDASSVKGAMGARLAVVTQNVANLGTGVILSLVYGWQLTLLLVVIIPLIVL 868
Cdd:cd18557   74 DLFSSLLRQEIAFFDKHK--TGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLI 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   869 GGII---EMKLLSGQALkdkKQLEISGKIATEAIENFRTIVSLTREQKFETMYAQSLQVPYRNAMKKAHVFGITFSFTQA 945
Cdd:cd18557  152 ASKIygrYIRKLSKEVQ---DALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSL 228
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6755046   946 MMYFSYAACFRFGAYLVAQ------QLMTFenvmLVFSAVVfgAMAAGNTSSFAPDYAKAkVSAS 1004
Cdd:cd18557  229 LIYLSLLLVLWYGGYLVLSgqltvgELTSF----ILYTIMV--ASSVGGLSSLLADIMKA-LGAS 286
PhnC COG3638
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ...
1033-1249 5.41e-35

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


Pssm-ID: 442855 [Multi-domain]  Cd Length: 249  Bit Score: 134.41  E-value: 5.41e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1033 VKFNGVQFNYPTRPniPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLN---VQWLRA 1109
Cdd:COG3638    3 LELRNLSKRYPGGT--PALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRgraLRRLRR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1110 HLGIVSQEPILFD-CSIAENI---AYGDNS------RAVSHEEIVRAakeaniHQFIDS--LPDKYNTRVGdkgtQLSGG 1177
Cdd:COG3638   81 RIGMIFQQFNLVPrLSVLTNVlagRLGRTStwrsllGLFPPEDRERA------LEALERvgLADKAYQRAD----QLSGG 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6755046  1178 QKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEAL-DKARE-GRTCIVIAHRLSTIQN-ADLIVVIENGKV 1249
Cdd:COG3638  151 QQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLrRIAREdGITVVVNLHQVDLARRyADRIIGLRDGRV 225
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
1036-1261 6.28e-35

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


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 137.20  E-value: 6.28e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1036 NGVQFNYPTRPnipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQL---LERfydPMAGSVFLDGKEIK-QLNVQwlRAHL 1111
Cdd:COG1118    6 RNISKRFGSFT---LLDDVSLEIASGELVALLGPSGSGKTTLLRIiagLET---PDSGRIVLNGRDLFtNLPPR--ERRV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1112 GIVSQEPILF-DCSIAENIAYGDNSRAVSHEEIVRAAKE----ANIHQFIDSLPdkyntrvgdkgTQLSGGQKQRIAIAR 1186
Cdd:COG1118   78 GFVFQHYALFpHMTVAENIAFGLRVRPPSKAEIRARVEEllelVQLEGLADRYP-----------SQLSGGQRQRVALAR 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1187 ALVRQPHILLLDEATSALDT----ESEKVVQEALDkaREGRTCIVIAH------RLstiqnADLIVVIENGKVKEHGTHQ 1256
Cdd:COG1118  147 ALAVEPEVLLLDEPFGALDAkvrkELRRWLRRLHD--ELGGTTVFVTHdqeealEL-----ADRVVVMNQGRIEQVGTPD 219

                 ....*
gi 6755046  1257 QLLAQ 1261
Cdd:COG1118  220 EVYDR 224
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
391-614 8.48e-35

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: 133.46  E-value: 8.48e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   391 LEFKNVHFNYPSrsEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREI-- 468
Cdd:cd03256    1 IEVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLrr 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   469 -IGVVSQEPVLFA-TTIAENIRYGREDVT---------MDEIEKAvkeaNAYDFIMKLphQFDTLVGERGAQLSGGQKQR 537
Cdd:cd03256   79 qIGMIFQQFNLIErLSVLENVLSGRLGRRstwrslfglFPKEEKQ----RALAALERV--GLLDKAYQRADQLSGGQQQR 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   538 IAIARALVRNPKILLLDEATSALDTE-SEAVVQAALDKARE-GRTTIVIAHRLSTVR-NADVIAGFDGGVIVEQGNHDEL 614
Cdd:cd03256  153 VAIARALMQQPKLILADEPVASLDPAsSRQVMDLLKRINREeGITVIVSLHQVDLAReYADRIVGLKDGRIVFDGPPAEL 232
PhnC COG3638
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ...
391-606 1.19e-34

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


Pssm-ID: 442855 [Multi-domain]  Cd Length: 249  Bit Score: 133.26  E-value: 1.19e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   391 LEFKNVHFNYPSRseVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREI-- 468
Cdd:COG3638    3 LELRNLSKRYPGG--TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLrr 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   469 -IGVVSQEPVLFA-TTIAENI-----------RYGREDVTMDEIEKAvkeanaydfimklphqFDTL--VG------ERG 527
Cdd:COG3638   81 rIGMIFQQFNLVPrLSVLTNVlagrlgrtstwRSLLGLFPPEDRERA----------------LEALerVGladkayQRA 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   528 AQLSGGQKQRIAIARALVRNPKILLLDEATSALDTE-SEAVVQAALDKARE-GRTTIVIAHRLSTVRN-ADVIAGFDGGV 604
Cdd:COG3638  145 DQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKtARQVMDLLRRIAREdGITVVVNLHQVDLARRyADRIIGLRDGR 224

                 ..
gi 6755046   605 IV 606
Cdd:COG3638  225 VV 226
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
413-617 1.29e-34

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: 133.92  E-value: 1.29e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   413 NLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREI----IGVVSQEPVLFA-TTIAENI 487
Cdd:cd03294   44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELrrkkISMVFQSFALLPhRTVLENV 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   488 RYGREDVTMDEIEKAVKEANAY------DFIMKLPHqfdtlvgergaQLSGGQKQRIAIARALVRNPKILLLDEATSALD 561
Cdd:cd03294  124 AFGLEVQGVPRAEREERAAEALelvgleGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 6755046   562 TESEAVVQAALDK--AREGRTTIVIAHRLS-TVRNADVIAGFDGGVIVEQGNHDELMRE 617
Cdd:cd03294  193 PLIRREMQDELLRlqAELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILTN 251
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
1050-1249 1.40e-34

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: 131.88  E-value: 1.40e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQW--LRAHLGIVSQEPILF-DCSIA 1126
Cdd:cd03262   15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNIneLRQKVGMVFQQFNLFpHLTVL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1127 ENIAYGD-NSRAVSHEEIVRAAKEA----NIHQFIDSLPDkyntrvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEAT 1201
Cdd:cd03262   95 ENITLAPiKVKGMSKAEAEERALELlekvGLADKADAYPA-----------QLSGGQQQRVAIARALAMNPKVMLFDEPT 163
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 6755046  1202 SALDTEsekVVQEALDK----AREGRTCIVIAHRLSTIQN-ADLIVVIENGKV 1249
Cdd:cd03262  164 SALDPE---LVGEVLDVmkdlAEEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
ABCC_SUR2 cd03288
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...
408-627 1.75e-34

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: 133.11  E-value: 1.75e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   408 ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENI 487
Cdd:cd03288   36 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   488 RYGREdVTMDEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAV 567
Cdd:cd03288  116 DPECK-CTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENI 194
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6755046   568 VQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELM-REKGIYFKLVMT 627
Cdd:cd03288  195 LQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLaQEDGVFASLVRT 255
ABC_6TM_bac_exporter_ABCB8_10_like cd18576
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ...
122-361 2.75e-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: 2.75e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   122 AGVLIV----AYIQVSLWCLAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDKIGMFFQSIT 197
Cdd:cd18576   43 LGLFLLqavfSFFRIYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQIL 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   198 TFLAGFIIGFISGWKLTLVILAVSPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQKELERYN 277
Cdd:cd18576  123 TLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFGRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYR 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   278 KNLEEAKNVGIKKAITASISIGIAYLLVYASYALAFWYGTSLVLSNEYSIGEVLT-VFFSILLGTfSIGHLAPNIEAFAN 356
Cdd:cd18576  203 KALERVVKLALKRARIRALFSSFIIFLLFGAIVAVLWYGGRLVLAGELTAGDLVAfLLYTLFIAG-SIGSLADLYGQLQK 281

                 ....*
gi 6755046   357 ARGAA 361
Cdd:cd18576  282 ALGAS 286
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
1033-1261 3.60e-34

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 131.75  E-value: 3.60e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1033 VKFNGVQFNYPTRPnipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLnvqwlRAHLG 1112
Cdd:COG1121    7 IELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-----RRRIG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1113 IVSQE-------PIlfdcSIAENIAYG--------DNSRAVSHEEIVRAAKEANIHQFIDslpdkynTRVGdkgtQLSGG 1177
Cdd:COG1121   79 YVPQRaevdwdfPI----TVRDVVLMGrygrrglfRRPSRADREAVDEALERVGLEDLAD-------RPIG----ELSGG 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1178 QKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTI-QNADLIVVIeNGKVKEHGTH 1255
Cdd:COG1121  144 QQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVrEYFDRVLLL-NRGLVAHGPP 222

                 ....*.
gi 6755046  1256 QQLLAQ 1261
Cdd:COG1121  223 EEVLTP 228
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
1049-1258 4.68e-34

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: 131.21  E-value: 4.68e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1049 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIkqLNVQWLRAHLGIVSQEPILF-DCSIAE 1127
Cdd:cd03300   14 VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--TNLPPHKRPVNTVFQNYALFpHLTVFE 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1128 NIAYGDNSRAVSHEEIVRAAKEAnIHQF-IDSLPDKYNTrvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEATSALDT 1206
Cdd:cd03300   92 NIAFGLRLKKLPKAEIKERVAEA-LDLVqLEGYANRKPS-------QLSGGQQQRVAIARALVNEPKVLLLDEPLGALDL 163
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 6755046  1207 ESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVIENGKVKEHGTHQQL 1258
Cdd:cd03300  164 KLRKDMQLELKRlqKELGITFVFVTHDQEeALTMSDRIAVMNKGKIQQIGTPEEI 218
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
391-615 5.19e-34

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 131.37  E-value: 5.19e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    391 LEFKNV--HFnypsrSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIR--TINVRYLR 466
Cdd:PRK09493    2 IEFKNVskHF-----GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIR 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    467 EIIGVVSQEPVLFATTIA-ENIRYGREDVTmdEIEKAVKEANAYDFIMKlphqfdtlVG--ERG----AQLSGGQKQRIA 539
Cdd:PRK09493   77 QEAGMVFQQFYLFPHLTAlENVMFGPLRVR--GASKEEAEKQARELLAK--------VGlaERAhhypSELSGGQQQRVA 146
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6755046    540 IARALVRNPKILLLDEATSALDTE-SEAVVQAALDKAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDELM 615
Cdd:PRK09493  147 IARALAVKPKLMLFDEPTSALDPElRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLI 224
ABC_6TM_exporters cd07346
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ...
709-1006 9.41e-34

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: 132.29  E-value: 9.41e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   709 LLVGVLCAVINGCIQPVFAIVFSRIVGVFSRDDDHETkrqnCNLFSLFFLVMGLISFVTYFFQGFTFGKAGEILTKRVRY 788
Cdd:cd07346    1 LLLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSL----LLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRR 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   789 MVFKSMLRQDISWFDdhKNSTGSLTTRLASDASSVKGAMGARLAVVTQNVANLGTGVILSLVYGWQLTLLLVVIIPLIVL 868
Cdd:cd07346   77 DLFRHLQRLSLSFFD--RNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   869 GGIIEMKLLSGQALKDKKQLEISGKIATEAIENFRTIVSLTREQKFETMYAQSLQVPYRNAMKKAHVFGITFSFTQAMMY 948
Cdd:cd07346  155 ILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTA 234
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 6755046   949 FSYAACFRFGAYLVAQQLMTFENVMLVFSAVVFGAMAAGNTSSFAPDYAKAKVSASHI 1006
Cdd:cd07346  235 LGTALVLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
cbiO PRK13650
energy-coupling factor transporter ATPase;
1033-1261 1.11e-33

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 131.39  E-value: 1.11e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1033 VKFNGVQFNYPTRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLG 1112
Cdd:PRK13650    5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1113 IVSQEP--ILFDCSIAENIAYGDNSRAVSHEEIVRAAKEA----NIHQFIDSLPdkyntrvgdkgTQLSGGQKQRIAIAR 1186
Cdd:PRK13650   85 MVFQNPdnQFVGATVEDDVAFGLENKGIPHEEMKERVNEAlelvGMQDFKEREP-----------ARLSGGQKQRVAIAG 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6755046   1187 ALVRQPHILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQ 1261
Cdd:PRK13650  154 AVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSR 230
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
1033-1249 1.44e-33

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: 127.51  E-value: 1.44e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1033 VKFNGVQFNYPTRPnipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQwLRAHLG 1112
Cdd:cd03230    1 IEVRNLSKRYGKKT---ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEE-VKRRIG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1113 IVSQEPILF-DCSIAENIaygdnsravsheeivraakeanihqfidslpdkyntrvgdkgtQLSGGQKQRIAIARALVRQ 1191
Cdd:cd03230   77 YLPEEPSLYeNLTVRENL-------------------------------------------KLSGGMKQRLALAQALLHD 113
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1192 PHILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVIENGKV 1249
Cdd:cd03230  114 PELLILDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
391-585 1.92e-33

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: 128.68  E-value: 1.92e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   391 LEFKNVHFNYPSrsEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDI---RTINVRYLRE 467
Cdd:cd03292    1 IEFINVTKTYPN--GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsdlRGRAIPYLRR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   468 IIGVVSQEPVLFAT-TIAENIRYGRE--DVTMDEIEKAVKEANAydfIMKLPHQFDTLvgerGAQLSGGQKQRIAIARAL 544
Cdd:cd03292   79 KIGVVFQDFRLLPDrNVYENVAFALEvtGVPPREIRKRVPAALE---LVGLSHKHRAL----PAELSGGEQQRVAIARAI 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 6755046   545 VRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIA 585
Cdd:cd03292  152 VNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVA 192
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
392-605 1.98e-33

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: 128.42  E-value: 1.98e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   392 EFKNVHFNYPSRsevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQdirtiNVRYLREIIGV 471
Cdd:cd03235    1 EVEDLTVSYGGH---PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK-----PLEKERKRIGY 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   472 VSQEPVL---FATTIAENI------------RYGREDvtMDEIEKAVKEANAYDFIMKlphQFDtlvgergaQLSGGQKQ 536
Cdd:cd03235   73 VPQRRSIdrdFPISVRDVVlmglyghkglfrRLSKAD--KAKVDEALERVGLSELADR---QIG--------ELSGGQQQ 139
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6755046   537 RIAIARALVRNPKILLLDEATSALDTESEAVVQAALDK-AREGRTTIVIAHRLSTV-RNADVIAGFDGGVI 605
Cdd:cd03235  140 RVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVlEYFDRVLLLNRTVV 210
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
1049-1254 2.83e-33

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 133.15  E-value: 2.83e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1049 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQwlRAHLGIVSQEPILF-DCSIAE 1127
Cdd:PRK09452   28 EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVNTVFQSYALFpHMTVFE 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1128 NIAYGDNSRAVSHEEIVRAAKEA----NIHQFIDSLPdkyntrvgdkgTQLSGGQKQRIAIARALVRQPHILLLDEATSA 1203
Cdd:PRK09452  106 NVAFGLRMQKTPAAEITPRVMEAlrmvQLEEFAQRKP-----------HQLSGGQQQRVAIARAVVNKPKVLLLDESLSA 174
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 6755046   1204 LDTESEKVVQEALdKA--RE-GRTCIVIAH-RLSTIQNADLIVVIENGKVKEHGT 1254
Cdd:PRK09452  175 LDYKLRKQMQNEL-KAlqRKlGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGT 228
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
1034-1249 2.94e-33

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: 129.22  E-value: 2.94e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1034 KFNGVQFNYPTrpNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWL---RAH 1110
Cdd:cd03256    2 EVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALrqlRRQ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1111 LGIVSQEPILFD-CSIAENI---AYGDNS------RAVSHEEIVRAAkeANIHQFidSLPDKYNTRVGdkgtQLSGGQKQ 1180
Cdd:cd03256   80 IGMIFQQFNLIErLSVLENVlsgRLGRRStwrslfGLFPKEEKQRAL--AALERV--GLLDKAYQRAD----QLSGGQQQ 151
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6755046  1181 RIAIARALVRQPHILLLDEATSALDTESEKVVQEAL-DKARE-GRTCIVIAHRLSTI-QNADLIVVIENGKV 1249
Cdd:cd03256  152 RVAIARALMQQPKLILADEPVASLDPASSRQVMDLLkRINREeGITVIVSLHQVDLArEYADRIVGLKDGRI 223
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
391-616 4.35e-33

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: 135.97  E-value: 4.35e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   391 LEFKNVHFNYPSR--------SEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLyDPLEGVVSIDGQDIRTIN- 461
Cdd:COG4172  276 LEARDLKVWFPIKrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLSr 354
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   462 --VRYLREIIGVVSQEPvlFAT-----TIAENIRYG----REDVTMDEIEKAVKEA-----------NAYdfimklPHQF 519
Cdd:COG4172  355 raLRPLRRRMQVVFQDP--FGSlsprmTVGQIIAEGlrvhGPGLSAAERRARVAEAleevgldpaarHRY------PHEF 426
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   520 dtlvgergaqlSGGQKQRIAIARALVRNPKILLLDEATSALDteseAVVQAA-LD-----KAREGRTTIVIAHRLSTVRN 593
Cdd:COG4172  427 -----------SGGQRQRIAIARALILEPKLLVLDEPTSALD----VSVQAQiLDllrdlQREHGLAYLFISHDLAVVRA 491
                        250       260
                 ....*....|....*....|....
gi 6755046   594 -ADVIAGFDGGVIVEQGNHDELMR 616
Cdd:COG4172  492 lAHRVMVMKDGKVVEQGPTEQVFD 515
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
1042-1261 4.89e-33

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: 130.94  E-value: 4.89e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1042 YPTRPN-IPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMA---GSVFLDGKEIKQLNVQWLRA----HLGI 1113
Cdd:COG0444   11 FPTRRGvVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGitsGEILFDGEDLLKLSEKELRKirgrEIQM 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1114 VSQEP---------ILFdcSIAENI-AYGDNSRAVSHEEIVRAAKEANIH---QFIDSLPdkyntrvgdkgTQLSGGQKQ 1180
Cdd:COG0444   91 IFQDPmtslnpvmtVGD--QIAEPLrIHGGLSKAEARERAIELLERVGLPdpeRRLDRYP-----------HELSGGMRQ 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1181 RIAIARALVRQPHILLLDEATSALDTesekVVQ-EALD-----KAREGRTCIVIAHRLSTI-QNADLIVVIENGKVKEHG 1253
Cdd:COG0444  158 RVMIARALALEPKLLIADEPTTALDV----TIQaQILNllkdlQRELGLAILFITHDLGVVaEIADRVAVMYAGRIVEEG 233

                 ....*...
gi 6755046  1254 THQQLLAQ 1261
Cdd:COG0444  234 PVEELFEN 241
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
392-609 5.13e-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: 5.13e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   392 EFKNVHFNYPSRsevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIGV 471
Cdd:cd03214    1 EVENLSVGYGGR---TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   472 VSQepvlfattiaenirygredvtmdeiekAVKEANAYDFIMKlphQFDTlvgergaqLSGGQKQRIAIARALVRNPKIL 551
Cdd:cd03214   78 VPQ---------------------------ALELLGLAHLADR---PFNE--------LSGGERQRVLLARALAQEPPIL 119
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6755046   552 LLDEATSALDTESE-AVVQAALDKARE-GRTTIVIAHRLS-TVRNADVIAGFDGGVIVEQG 609
Cdd:cd03214  120 LLDEPTSHLDIAHQiELLELLRRLARErGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
1033-1254 5.44e-33

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


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 131.73  E-value: 5.44e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1033 VKFNGVQFNYPtrpNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQwlRAHLG 1112
Cdd:COG3839    4 LELENVSKSYG---GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPK--DRNIA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1113 IVSQEPILFD-CSIAENIAYGDNSRAVSHEEIVRAAKEA----NIHQFIDSLPDkyntrvgdkgtQLSGGQKQRIAIARA 1187
Cdd:COG3839   79 MVFQSYALYPhMTVYENIAFPLKLRKVPKAEIDRRVREAaellGLEDLLDRKPK-----------QLSGGQRQRVALGRA 147
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6755046  1188 LVRQPHILLLDEATSALD------TESE-KVVQEALdkareGRTCIVIAHRLS---TIqnADLIVVIENGKVKEHGT 1254
Cdd:COG3839  148 LVREPKVFLLDEPLSNLDaklrveMRAEiKRLHRRL-----GTTTIYVTHDQVeamTL--ADRIAVMNDGRIQQVGT 217
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
391-597 7.72e-33

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: 126.82  E-value: 7.72e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   391 LEFKNVHFnypSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYlREIIG 470
Cdd:COG4133    3 LEAENLSC---RRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDY-RRRLA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   471 VVSQEPVLFAT-TIAENIR-----YGReDVTMDEIEKAVKEanaydfiMKLPHQFDTLVGergaQLSGGQKQRIAIARAL 544
Cdd:COG4133   79 YLGHADGLKPElTVRENLRfwaalYGL-RADREAIDEALEA-------VGLAGLADLPVR----QLSAGQKRRVALARLL 146
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 6755046   545 VRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIA-HRLSTVRNADVI 597
Cdd:COG4133  147 LSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTtHQPLELAAARVL 200
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
1048-1260 2.03e-32

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: 126.01  E-value: 2.03e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1048 IPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQwLRAHLGI--VSQEPILF-DCS 1124
Cdd:cd03224   13 SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPH-ERARAGIgyVPEGRRIFpELT 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1125 IAENIAYGDNSRAvsheeivRAAKEANIHQFIDSLPDKYnTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSAL 1204
Cdd:cd03224   92 VEENLLLGAYARR-------RAKRKARLERVYELFPRLK-ERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGL 163
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6755046  1205 dteSEKVVQE---ALDKAREGRTCIVIAHrlstiQNADLI-------VVIENGKVKEHGTHQQLLA 1260
Cdd:cd03224  164 ---APKIVEEifeAIRELRDEGVTILLVE-----QNARFAleiadraYVLERGRVVLEGTAAELLA 221
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
391-616 2.15e-32

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


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 129.88  E-value: 2.15e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   391 LEFKNVHFNYPSRsevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRT-INVRYLReiI 469
Cdd:COG1118    3 IEVRNISKRFGSF---TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTnLPPRERR--V 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   470 GVVSQEPVLFA-TTIAENIRYG--REDVTMDEIEKAVKE----------ANAYdfimklPHQfdtlvgergaqLSGGQKQ 536
Cdd:COG1118   78 GFVFQHYALFPhMTVAENIAFGlrVRPPSKAEIRARVEEllelvqleglADRY------PSQ-----------LSGGQRQ 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   537 RIAIARALVRNPKILLLDEATSALDT----ESEAVVQAALDkaREGRTTIVIAH-RLSTVRNADVIAGFDGGVIVEQGNH 611
Cdd:COG1118  141 RVALARALAVEPEVLLLDEPFGALDAkvrkELRRWLRRLHD--ELGGTTVFVTHdQEEALELADRVVVMNQGRIEQVGTP 218

                 ....*
gi 6755046   612 DELMR 616
Cdd:COG1118  219 DEVYD 223
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
394-586 2.17e-32

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: 125.45  E-value: 2.17e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   394 KNVHFNYPSRSEvqILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIrtiNVRYLREIIGVVS 473
Cdd:cd03226    3 ENISFSYKKGTE--ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI---KAKERRKSIGYVM 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   474 QEP--VLFATTIAENIRYGREDVTMD--EIEKAVKEANAYDFIMKLPHQfdtlvgergaqLSGGQKQRIAIARALVRNPK 549
Cdd:cd03226   78 QDVdyQLFTDSVREELLLGLKELDAGneQAETVLKDLDLYALKERHPLS-----------LSGGQKQRLAIAAALLSGKD 146
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 6755046   550 ILLLDEATSALDTES-EAVVQAALDKAREGRTTIVIAH 586
Cdd:cd03226  147 LLIFDEPTSGLDYKNmERVGELIRELAAQGKAVIVITH 184
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
391-616 2.18e-32

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 127.82  E-value: 2.18e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    391 LEFKNVHFNYPSRSEvQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIG 470
Cdd:PRK13635    6 IRVEHISFRYPDAAT-YALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    471 VVSQEP--VLFATTIAENIRYGRED--VTMDE----IEKAVKEANAYDFIMKLPHQfdtlvgergaqLSGGQKQRIAIAR 542
Cdd:PRK13635   85 MVFQNPdnQFVGATVQDDVAFGLENigVPREEmverVDQALRQVGMEDFLNREPHR-----------LSGGQKQRVAIAG 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6755046    543 ALVRNPKILLLDEATSALDTESEAVVQAALD--KAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMR 616
Cdd:PRK13635  154 VLALQPDIIILDEATSMLDPRGRREVLETVRqlKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFK 229
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
391-618 3.27e-32

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 127.12  E-value: 3.27e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    391 LEFKNVHFNYPSRSEVqiLKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYL--REI 468
Cdd:PRK13639    2 LETRDLKYSYPDGTEA--LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLevRKT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    469 IGVVSQEP--VLFATTIAENIRYGREDV--TMDEIEKAVKEA----NAYDFIMKLPHqfdtlvgergaQLSGGQKQRIAI 540
Cdd:PRK13639   80 VGIVFQNPddQLFAPTVEEDVAFGPLNLglSKEEVEKRVKEAlkavGMEGFENKPPH-----------HLSGGQKKRVAI 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    541 ARALVRNPKILLLDEATSALDTE-SEAVVQAALDKAREGRTTIVIAHRLSTV-RNADVIAGFDGGVIVEQGNHDELMREK 618
Cdd:PRK13639  149 AGILAMKPEIIVLDEPTSGLDPMgASQIMKLLYDLNKEGITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEVFSDI 228
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
1055-1261 3.76e-32

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 125.64  E-value: 3.76e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1055 SLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQwLRAhLGIVSQEPILFD-CSIAENIAYGD 1133
Cdd:COG3840   19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPA-ERP-VSMLFQENNLFPhLTVAQNIGLGL 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1134 NSR----AVSHEEIVRAAKEANIHQFIDSLPDkyntrvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEATSALD---- 1205
Cdd:COG3840   97 RPGlkltAEQRAQVEQALERVGLAGLLDRLPG-----------QLSGGQRQRVALARCLVRKRPILLLDEPFSALDpalr 165
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 6755046  1206 TESEKVVQEALDkaREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLLAQ 1261
Cdd:COG3840  166 QEMLDLVDELCR--ERGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDG 220
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
1045-1250 4.93e-32

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: 124.29  E-value: 4.93e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1045 RPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQlnvQWLRAHLGIVSQEP--ILFD 1122
Cdd:cd03226   10 KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA---KERRKSIGYVMQDVdyQLFT 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1123 CSIAENIAYGDNSRAVSHEEIVRAAKEANIHQFIDSLPdkyntrvgdkgTQLSGGQKQRIAIARALVRQPHILLLDEATS 1202
Cdd:cd03226   87 DSVREELLLGLKELDAGNEQAETVLKDLDLYALKERHP-----------LSLSGGQKQRLAIAAALLSGKDLLIFDEPTS 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 6755046  1203 ALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVIENGKVK 1250
Cdd:cd03226  156 GLDYKNMERVGELIRElAAQGKAVIVITHDYEFLAKvCDRVLLLANGAIV 205
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
391-614 1.28e-31

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 124.89  E-value: 1.28e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    391 LEFKNVHFNYpsrSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYD-----PLEGVVSIDGQDI---RTINV 462
Cdd:PRK14239    6 LQVSDLSVYY---NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIyspRTDTV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    463 RyLREIIGVVSQEPVLFATTIAENIRYG------REDVTMDE-IEKAVKEANAYDFIMKLPHqfDTLVGergaqLSGGQK 535
Cdd:PRK14239   83 D-LRKEIGMVFQQPNPFPMSIYENVVYGlrlkgiKDKQVLDEaVEKSLKGASIWDEVKDRLH--DSALG-----LSGGQQ 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    536 QRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTV-RNADVIAGFDGGVIVEQGNHDEL 614
Cdd:PRK14239  155 QRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQAsRISDRTGFFLDGDLIEYNDTKQM 234
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
1026-1261 1.38e-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: 131.35  E-value: 1.38e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1026 PTLLEGNvkfnGVQFNYPTRPNI--------PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFyDPMAGSVFLDGK 1097
Cdd:COG4172  273 PPLLEAR----DLKVWFPIKRGLfrrtvghvKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQ 347
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1098 EIKQLN---VQWLRAHLGIVSQEPilFDC-----SIAENIAYGdnsRAVSHEEIVRAAKEANIhqfIDSLpdkynTRVG- 1168
Cdd:COG4172  348 DLDGLSrraLRPLRRRMQVVFQDP--FGSlsprmTVGQIIAEG---LRVHGPGLSAAERRARV---AEAL-----EEVGl 414
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1169 DKGT------QLSGGQKQRIAIARALVRQPHILLLDEATSALDteseKVVQ-EALD-----KAREGRTCIVIAHRLSTIQ 1236
Cdd:COG4172  415 DPAArhryphEFSGGQRQRIAIARALILEPKLLVLDEPTSALD----VSVQaQILDllrdlQREHGLAYLFISHDLAVVR 490
                        250       260
                 ....*....|....*....|....*.
gi 6755046  1237 N-ADLIVVIENGKVKEHGTHQQLLAQ 1261
Cdd:COG4172  491 AlAHRVMVMKDGKVVEQGPTEQVFDA 516
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
1044-1243 1.43e-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: 122.97  E-value: 1.43e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1044 TRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWlRAHLGIVSQEPILF-D 1122
Cdd:COG4133   11 RRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDY-RRRLAYLGHADGLKpE 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1123 CSIAENIA-----YGdnsRAVSHEEIVRAAKEANIHQFIDslpdkynTRVGdkgtQLSGGQKQRIAIARALVRQPHILLL 1197
Cdd:COG4133   90 LTVRENLRfwaalYG---LRADREAIDEALEAVGLAGLAD-------LPVR----QLSAGQKRRVALARLLLSPAPLWLL 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 6755046  1198 DEATSALDTESEKVVQEALDKAREGRTCIVIA-HRLSTIQNADLIVV 1243
Cdd:COG4133  156 DEPFTALDAAGVALLAELIAAHLARGGAVLLTtHQPLELAAARVLDL 202
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
1036-1253 1.60e-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: 121.77  E-value: 1.60e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1036 NGVQFNYPTRPnipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGIVS 1115
Cdd:cd03214    3 ENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1116 QepilfdcsiaeniaygdnsravsheeivrAAKEANIHQFIDSLpdkYNTrvgdkgtqLSGGQKQRIAIARALVRQPHIL 1195
Cdd:cd03214   80 Q-----------------------------ALELLGLAHLADRP---FNE--------LSGGERQRVLLARALAQEPPIL 119
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6755046  1196 LLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVIENGKVKEHG 1253
Cdd:cd03214  120 LLDEPTSHLDIAHQIELLELLRRlaRERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
1033-1254 2.40e-31

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 126.45  E-value: 2.40e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1033 VKFNGVQFNYPT-RPNIPVLQGLSLEVKKGQTLALVGSSGCGKST---VVQLLERfydPMAGSVFLDGKEIKQLNVQWLR 1108
Cdd:PRK11153    2 IELKNISKVFPQgGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTlirCINLLER---PTSGRVLVDGQDLTALSEKELR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1109 A---HLGIVSQE-PILFDCSIAENIAYGdnsravshEEIVRAAKeANIHQFIDSLPDkyntRVG--DKG----TQLSGGQ 1178
Cdd:PRK11153   79 KarrQIGMIFQHfNLLSSRTVFDNVALP--------LELAGTPK-AEIKARVTELLE----LVGlsDKAdrypAQLSGGQ 145
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6755046   1179 KQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKA-RE-GRTCIVIAHRLSTI-QNADLIVVIENGKVKEHGT 1254
Cdd:PRK11153  146 KQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDInRElGLTIVLITHEMDVVkRICDRVAVIDAGRLVEQGT 224
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
1046-1258 2.65e-31

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: 123.22  E-value: 2.65e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1046 PNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQwlRAHLGIVSQEPILF-DCS 1124
Cdd:cd03296   13 GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVGFVFQHYALFrHMT 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1125 IAENIAYGDNSRAVShEEIVRAAKEANIHQFI-----DSLPDKYNTrvgdkgtQLSGGQKQRIAIARALVRQPHILLLDE 1199
Cdd:cd03296   91 VFDNVAFGLRVKPRS-ERPPEAEIRAKVHELLklvqlDWLADRYPA-------QLSGGQRQRVALARALAVEPKVLLLDE 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6755046  1200 ATSALDTESEKVVQEALDKARE--GRTCIVIAHRLS-TIQNADLIVVIENGKVKEHGTHQQL 1258
Cdd:cd03296  163 PFGALDAKVRKELRRWLRRLHDelHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPDEV 224
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
1046-1249 2.87e-31

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 129.75  E-value: 2.87e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1046 PNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNV-QWLRAHLGIVSQEPILF-DC 1123
Cdd:COG1129   15 GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPrDAQAAGIAIIHQELNLVpNL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1124 SIAENIAYGD---NSRAVSHEEIVRAAKEA----NIHqfIDslPDkynTRVGDkgtqLSGGQKQRIAIARALVRQPHILL 1196
Cdd:COG1129   95 SVAENIFLGReprRGGLIDWRAMRRRARELlarlGLD--ID--PD---TPVGD----LSVAQQQLVEIARALSRDARVLI 163
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 6755046  1197 LDEATSAL-DTESE---KVVQEaLdkAREGRTCIVIAHRLSTIQN-ADLIVVIENGKV 1249
Cdd:COG1129  164 LDEPTASLtEREVErlfRIIRR-L--KAQGVAIIYISHRLDEVFEiADRVTVLRDGRL 218
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
1033-1249 3.16e-31

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: 122.52  E-value: 3.16e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1033 VKFNGVQFNYPtrPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLN---VQWLRA 1109
Cdd:cd03292    1 IEFINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraIPYLRR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1110 HLGIVSQE-PILFDCSIAENIAYGDNSRAVSHEEIVRAAKEA----NIHQFIDSLPdkyntrvgdkgTQLSGGQKQRIAI 1184
Cdd:cd03292   79 KIGVVFQDfRLLPDRNVYENVAFALEVTGVPPREIRKRVPAAlelvGLSHKHRALP-----------AELSGGEQQRVAI 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6755046  1185 ARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNA--DLIVVIENGKV 1249
Cdd:cd03292  148 ARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTtrHRVIALERGKL 214
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
1034-1253 3.25e-31

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: 122.26  E-value: 3.25e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1034 KFNGVQFNYPTRPnipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLnvqwlRAHLGI 1113
Cdd:cd03235    1 EVEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGY 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1114 VSQEPIL---FDCSIAENIAYGDNSRAVSHEEIVRAAKEAnIHQFIDS--LPDKYNTRVGdkgtQLSGGQKQRIAIARAL 1188
Cdd:cd03235   73 VPQRRSIdrdFPISVRDVVLMGLYGHKGLFRRLSKADKAK-VDEALERvgLSELADRQIG----ELSGGQQQRVLLARAL 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6755046  1189 VRQPHILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVIeNGKVKEHG 1253
Cdd:cd03235  148 VQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEyFDRVLLL-NRTVVASG 213
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
391-617 6.41e-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: 121.77  E-value: 6.41e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   391 LEFKNVHFNYPsrsEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRY-LREII 469
Cdd:cd03224    1 LEVENLNAGYG---KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   470 GVVSQEPVLFAT-TIAENIRYGREDVTMDEIEKAVKEAnaYDFIMKLphqfDTLVGERGAQLSGGQKQRIAIARALVRNP 548
Cdd:cd03224   78 GYVPEGRRIFPElTVEENLLLGAYARRRAKRKARLERV--YELFPRL----KERRKQLAGTLSGGEQQMLAIARALMSRP 151
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6755046   549 KILLLDEATSALdteSEAVVQ---AALDKAREGRTTIVI----AHRLSTVrnADVIAGFDGGVIVEQGNHDELMRE 617
Cdd:cd03224  152 KLLLLDEPSEGL---APKIVEeifEAIRELRDEGVTILLveqnARFALEI--ADRAYVLERGRVVLEGTAAELLAD 222
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
409-613 7.29e-31

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: 122.06  E-value: 7.29e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   409 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRylREIIGVVSQEPVLFA-TTIAENI 487
Cdd:cd03299   15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFPhMTVYKNI 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   488 RYGREDVTMD--EIEKAVKEANAydfIMKLPHqfdtLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESE 565
Cdd:cd03299   93 AYGLKKRKVDkkEIERKVLEIAE---MLGIDH----LLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTK 165
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 6755046   566 AVVQAALDKARE--GRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDE 613
Cdd:cd03299  166 EKLREELKKIRKefGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEE 216
cbiO PRK13642
energy-coupling factor transporter ATPase;
391-614 7.78e-31

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 123.28  E-value: 7.78e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    391 LEFKNVHFNYPSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIG 470
Cdd:PRK13642    5 LEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    471 VVSQEP--VLFATTIAENIRYGRED--VTMDEIEKAVKEA----NAYDFIMKLPhqfdtlvgergAQLSGGQKQRIAIAR 542
Cdd:PRK13642   85 MVFQNPdnQFVGATVEDDVAFGMENqgIPREEMIKRVDEAllavNMLDFKTREP-----------ARLSGGQKQRVAVAG 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6755046    543 ALVRNPKILLLDEATSALDTESEAVVQAALDKAREGR--TTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDEL 614
Cdd:PRK13642  154 IIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSEL 227
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
1042-1258 1.09e-30

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: 121.07  E-value: 1.09e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1042 YPTRPNiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQlNVQWLRAHLGIVSQEPILF 1121
Cdd:cd03263   10 YKKGTK-PAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGYCPQFDALF 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1122 D-CSIAENIAYGDNSRAVSHEEIvraakEANIHQFID--SLPDKYNTRVGDkgtqLSGGQKQRIAIARALVRQPHILLLD 1198
Cdd:cd03263   88 DeLTVREHLRFYARLKGLPKSEI-----KEEVELLLRvlGLTDKANKRART----LSGGMKRKLSLAIALIGGPSVLLLD 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6755046  1199 EATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQL 1258
Cdd:cd03263  159 EPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
1050-1254 1.16e-30

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: 121.39  E-value: 1.16e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQwLRAHLGIVS--QEPILF-DCSIA 1126
Cdd:cd03219   15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPH-EIARLGIGRtfQIPRLFpELTVL 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1127 ENI---AYGDNSRAVSHEEIVRAAKEAN--IHQFIDS--LPDKYNTRVGDkgtqLSGGQKQRIAIARALVRQPHILLLDE 1199
Cdd:cd03219   94 ENVmvaAQARTGSGLLLARARREEREARerAEELLERvgLADLADRPAGE----LSYGQQRRLEIARALATDPKLLLLDE 169
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 6755046  1200 ATSAL-DTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGT 1254
Cdd:cd03219  170 PAAGLnPEETEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGT 226
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
1051-1258 1.31e-30

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


Pssm-ID: 443658 [Multi-domain]  Cd Length: 329  Bit Score: 124.07  E-value: 1.31e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1051 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLN---VQWLRAHLGIVSQEP--------- 1118
Cdd:COG4608   34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSgreLRPLRRRMQMVFQDPyaslnprmt 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1119 ---IlfdcsIAENIAYgdnsravsHEEIVRAAKEANIHQFIDslpdkyntRVGDKGT-------QLSGGQKQRIAIARAL 1188
Cdd:COG4608  114 vgdI-----IAEPLRI--------HGLASKAERRERVAELLE--------LVGLRPEhadryphEFSGGQRQRIGIARAL 172
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6755046  1189 VRQPHILLLDEATSALDtesekV-VQ-------EALdKAREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQL 1258
Cdd:COG4608  173 ALNPKLIVCDEPVSALD-----VsIQaqvlnllEDL-QDELGLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDEL 245
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
391-609 1.52e-30

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: 120.44  E-value: 1.52e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   391 LEFKNVHFNYPsrsEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRtiNVRYLREIIG 470
Cdd:cd03301    1 VELENVTKRFG---NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVT--DLPPKDRDIA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   471 VVSQEPVLFA-TTIAENIRYG--REDVTMDEIEKAVKEANAydfIMKLPHqfdtLVGERGAQLSGGQKQRIAIARALVRN 547
Cdd:cd03301   76 MVFQNYALYPhMTVYDNIAFGlkLRKVPKDEIDERVREVAE---LLQIEH----LLDRKPKQLSGGQRQRVALGRAIVRE 148
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6755046   548 PKILLLDEATSALDTESEAVVQAALDK--AREGRTTIVIAH-RLSTVRNADVIAGFDGGVIVEQG 609
Cdd:cd03301  149 PKVFLMDEPLSNLDAKLRVQMRAELKRlqQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
407-614 1.69e-30

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 121.40  E-value: 1.69e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    407 QILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVV-----SIDGQdiRTIN-----VRYLREIIGVVSQEP 476
Cdd:PRK11264   17 TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgdiTIDTA--RSLSqqkglIRQLRQHVGFVFQNF 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    477 VLFA-TTIAENIRYGreDVTMDEIEKAVKEANAYDFIMKLphqfdTLVGERGA---QLSGGQKQRIAIARALVRNPKILL 552
Cdd:PRK11264   95 NLFPhRTVLENIIEG--PVIVKGEPKEEATARARELLAKV-----GLAGKETSyprRLSGGQQQRVAIARALAMRPEVIL 167
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6755046    553 LDEATSALDTESEAVVQAALDK-AREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDEL 614
Cdd:PRK11264  168 FDEPTSALDPELVGEVLNTIRQlAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKAL 231
cbiO PRK13650
energy-coupling factor transporter ATPase;
388-595 2.12e-30

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 122.15  E-value: 2.12e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    388 MGN-LEFKNVHFNYPSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLR 466
Cdd:PRK13650    1 MSNiIEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    467 EIIGVVSQEP--VLFATTIAENIRYGRED--VTMDEIEKAVKEA----NAYDFIMKLPhqfdtlvgergAQLSGGQKQRI 538
Cdd:PRK13650   81 HKIGMVFQNPdnQFVGATVEDDVAFGLENkgIPHEEMKERVNEAlelvGMQDFKEREP-----------ARLSGGQKQRV 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 6755046    539 AIARALVRNPKILLLDEATSALDTESEAVVQAALDKARE--GRTTIVIAHRLSTVRNAD 595
Cdd:PRK13650  150 AIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEVALSD 208
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
1033-1258 2.15e-30

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 121.78  E-value: 2.15e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1033 VKFNGVQFNYPTRPNIpVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLG 1112
Cdd:PRK13648    8 IVFKNVSFQYQSDASF-TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1113 IVSQEPI-LFDCSIAE-NIAYGDNSRAVSHEEIVR----AAKEANIHQFIDSLPDkyntrvgdkgtQLSGGQKQRIAIAR 1186
Cdd:PRK13648   87 IVFQNPDnQFVGSIVKyDVAFGLENHAVPYDEMHRrvseALKQVDMLERADYEPN-----------ALSGGQKQRVAIAG 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6755046   1187 ALVRQPHILLLDEATSALDTESEKVVQEALDKAREGR--TCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQL 1258
Cdd:PRK13648  156 VLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
391-617 3.19e-30

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: 120.03  E-value: 3.19e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   391 LEFKNVHFNYPSrseVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIrtINVRYLREIIG 470
Cdd:cd03300    1 IELENVSKFYGG---FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--TNLPPHKRPVN 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   471 VVSQEPVLFA-TTIAENIRYG--REDVTMDEIEKAVKEAnaydfiMKLPhQFDTLVGERGAQLSGGQKQRIAIARALVRN 547
Cdd:cd03300   76 TVFQNYALFPhLTVFENIAFGlrLKKLPKAEIKERVAEA------LDLV-QLEGYANRKPSQLSGGQQQRVAIARALVNE 148
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6755046   548 PKILLLDEATSALDTESEAVVQAALDK--AREGRTTIVIAHRLS---TVrnADVIAGFDGGVIVEQGNHDELMRE 617
Cdd:cd03300  149 PKVLLLDEPLGALDLKLRKDMQLELKRlqKELGITFVFVTHDQEealTM--SDRIAVMNKGKIQQIGTPEEIYEE 221
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
391-609 4.44e-30

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 120.53  E-value: 4.44e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    391 LEFKNVHFNYPSRsevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDpLEGVVSIDG------QDI--RTINV 462
Cdd:PRK14258    8 IKVNNLSFYYDTQ---KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEGrveffnQNIyeRRVNL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    463 RYLREIIGVVSQEPVLFATTIAENIRYG------REDVTMDEI-EKAVKEANAYDFIMKLPHQfdtlvgeRGAQLSGGQK 535
Cdd:PRK14258   84 NRLRRQVSMVHPKPNLFPMSVYDNVAYGvkivgwRPKLEIDDIvESALKDADLWDEIKHKIHK-------SALDLSGGQQ 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    536 QRIAIARALVRNPKILLLDEATSALDTESEAVVQAALD--KAREGRTTIVIAHRLSTV-RNADVIAGFDG-----GVIVE 607
Cdd:PRK14258  157 QRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVSHNLHQVsRLSDFTAFFKGnenriGQLVE 236

                  ..
gi 6755046    608 QG 609
Cdd:PRK14258  237 FG 238
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
1051-1269 5.42e-30

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 120.61  E-value: 5.42e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1051 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGIVSQEP--ILFDCSIAEN 1128
Cdd:PRK13647   21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQDPddQVFSSTVWDD 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1129 IAYGDNSRAVSHEEIVRAAKEA----NIHQFIDSLPdkyntrvgdkgTQLSGGQKQRIAIARALVRQPHILLLDEATSAL 1204
Cdd:PRK13647  101 VAFGPVNMGLDKDEVERRVEEAlkavRMWDFRDKPP-----------YHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYL 169
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6755046   1205 DTESEKVVQEALDK-AREGRTCIVIAHRLS-TIQNADLIVVIENGKVKEHG-----THQQLLAQKGIYFSMV 1269
Cdd:PRK13647  170 DPRGQETLMEILDRlHNQGKTVIVATHDVDlAAEWADQVIVLKEGRVLAEGdksllTDEDIVEQAGLRLPLV 241
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
1044-1246 1.18e-29

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


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 117.58  E-value: 1.18e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1044 TRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDP---MAGSVFLDGKEIKQLNVQwlRAHLGIVSQEPIL 1120
Cdd:COG4136   10 TLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAE--QRRIGILFQDDLL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1121 FD-CSIAENIAYG---DNSRAVSHEEIVRAAKEANIHQFIDSLPDkyntrvgdkgtQLSGGQKQRIAIARALVRQPHILL 1196
Cdd:COG4136   88 FPhLSVGENLAFAlppTIGRAQRRARVEQALEEAGLAGFADRDPA-----------TLSGGQRARVALLRALLAEPRALL 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 6755046  1197 LDEATSALDTE-SEKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIVVIEN 1246
Cdd:COG4136  157 LDEPFSKLDAAlRAQFREFVFEQIRQrGIPALLVTHDEEDAPAAGRVLDLGN 208
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
1051-1249 1.29e-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: 117.78  E-value: 1.29e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1051 LQGLSLEVK---KGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEI----KQLNVQWLRAHLGIVSQEPILF-D 1122
Cdd:cd03297   10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdsrKKINLPPQQRKIGLVFQQYALFpH 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1123 CSIAENIAYG-----DNSRAVSHEEIVRAAKeanihqfIDSLPDKYNTrvgdkgtQLSGGQKQRIAIARALVRQPHILLL 1197
Cdd:cd03297   90 LNVRENLAFGlkrkrNREDRISVDELLDLLG-------LDHLLNRYPA-------QLSGGEKQRVALARALAAQPELLLL 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 6755046  1198 DEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVIENGKV 1249
Cdd:cd03297  156 DEPFSALDRALRLQLLPELKQikKNLNIPVIFVTHDLSEAEYlADRIVVMEDGRL 210
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
391-561 1.32e-29

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 122.36  E-value: 1.32e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    391 LEFKNVHFNYPSRsevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDI-------RTINVr 463
Cdd:PRK09452   15 VELRGISKSFDGK---EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIthvpaenRHVNT- 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    464 ylreiigvVSQEPVLFA-TTIAENIRYG--REDVTMDEIEKAVKEAnaydfiMKLPhQFDTLVGERGAQLSGGQKQRIAI 540
Cdd:PRK09452   91 --------VFQSYALFPhMTVFENVAFGlrMQKTPAAEITPRVMEA------LRMV-QLEEFAQRKPHQLSGGQQQRVAI 155
                         170       180
                  ....*....|....*....|.
gi 6755046    541 ARALVRNPKILLLDEATSALD 561
Cdd:PRK09452  156 ARAVVNKPKVLLLDESLSALD 176
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
391-618 1.74e-29

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 119.07  E-value: 1.74e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    391 LEFKNVHFNYPSRSEVqiLKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIG 470
Cdd:PRK13647    5 IEVEDLHFRYKDGTKA--LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    471 VVSQEP--VLFATTIAENIRYGRED--VTMDEIEKAVKEA----NAYDFIMKLPHqfdtlvgergaQLSGGQKQRIAIAR 542
Cdd:PRK13647   83 LVFQDPddQVFSSTVWDDVAFGPVNmgLDKDEVERRVEEAlkavRMWDFRDKPPY-----------HLSYGQKKRVAIAG 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6755046    543 ALVRNPKILLLDEATSALDTESEAVVQAALDK-AREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDELMREK 618
Cdd:PRK13647  152 VLAMDPDVIVLDEPMAYLDPRGQETLMEILDRlHNQGKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDKSLLTDED 229
nickel_nikE TIGR02769
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ...
403-608 3.36e-29

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: 117.98  E-value: 3.36e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     403 RSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTIN---VRYLREIIGVVSQE---P 476
Cdd:TIGR02769   21 KQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDrkqRRAFRRDVQLVFQDspsA 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     477 VLFATTIAENIRYGREDVT-MDEIEKAVKEANAYDfIMKLPhqfDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDE 555
Cdd:TIGR02769  101 VNPRMTVRQIIGEPLRHLTsLDESEQKARIAELLD-MVGLR---SEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDE 176
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 6755046     556 ATSALDTESEAVVQAALDK--AREGRTTIVIAHRLSTV-RNADVIAGFDGGVIVEQ 608
Cdd:TIGR02769  177 AVSNLDMVLQAVILELLRKlqQAFGTAYLFITHDLRLVqSFCQRVAVMDKGQIVEE 232
ABC_6TM_bac_exporter_ABCB8_10_like cd18575
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ...
146-361 5.96e-29

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: 117.97  E-value: 5.96e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   146 IRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDKIGMFFQSITTFLAGFIIGFISGWKLTLVILAVSPLIG 225
Cdd:cd18575   71 LRKAVFAHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVV 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   226 LSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQKELERYNKNLEEAKNVGIKKAITASISIGIAYLLV 305
Cdd:cd18575  151 LPIILFGRRVRRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRARALLTALVIFLV 230
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 6755046   306 YASYALAFWYGTSLVLSNEYSIGEVLT-VFFSILLGTfSIGHLAPNIEAFANARGAA 361
Cdd:cd18575  231 FGAIVFVLWLGAHDVLAGRMSAGELSQfVFYAVLAAG-SVGALSEVWGDLQRAAGAA 286
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
1050-1261 6.04e-29

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 119.82  E-value: 6.04e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQwlRAHLGIVSQEPILF-DCSIAEN 1128
Cdd:PRK11432   21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ--QRDICMVFQSYALFpHMSLGEN 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1129 IAYGDNSRAVSHEEIVRAAKEA----NIHQFIDSLPDkyntrvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEATSAL 1204
Cdd:PRK11432   99 VGYGLKMLGVPKEERKQRVKEAlelvDLAGFEDRYVD-----------QISGGQQQRVALARALILKPKVLLFDEPLSNL 167
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6755046   1205 DTESEKVVQEaldKARE-----GRTCIVIAHRLS-TIQNADLIVVIENGKVKEHGTHQQLLAQ 1261
Cdd:PRK11432  168 DANLRRSMRE---KIRElqqqfNITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQELYRQ 227
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
1046-1249 6.24e-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: 114.06  E-value: 6.24e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1046 PNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVqwlrahlgivsqepilfdcsi 1125
Cdd:cd03216   11 GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASP--------------------- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1126 aeniaygdnsravsheeivRAAKEANIhQFIdslpdkyntrvgdkgTQLSGGQKQRIAIARALVRQPHILLLDEATSAL- 1204
Cdd:cd03216   70 -------------------RDARRAGI-AMV---------------YQLSVGERQMVEIARALARNARLLILDEPTAALt 114
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 6755046  1205 DTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIENGKV 1249
Cdd:cd03216  115 PAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEiADRVTVLRDGRV 160
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
1051-1232 7.03e-29

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 117.19  E-value: 7.03e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1051 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMA-----GSVFLDGKEI--KQLNVQWLRAHLGIVSQEPILFDC 1123
Cdd:PRK14243   26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPgfrveGKVTFHGKNLyaPDVDPVEVRRRIGMVFQKPNPFPK 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1124 SIAENIAYGD--NSRAVSHEEIV-RAAKEAnihqfidSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEA 1200
Cdd:PRK14243  106 SIYDNIAYGAriNGYKGDMDELVeRSLRQA-------ALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEP 178
                         170       180       190
                  ....*....|....*....|....*....|..
gi 6755046   1201 TSALDTESEKVVQEALDKAREGRTCIVIAHRL 1232
Cdd:PRK14243  179 CSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
391-618 7.89e-29

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: 116.72  E-value: 7.89e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   391 LEFKNVHFnypSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEG-VVSIDGQDIRTINVRYLREII 469
Cdd:COG1119    4 LELRNVTV---RRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKRI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   470 GVVS---------QEPVL-------FATTiaeniryGR-EDVTMDEIEKAVKeanaydfIMKLPHqFDTLVGERGAQLSG 532
Cdd:COG1119   81 GLVSpalqlrfprDETVLdvvlsgfFDSI-------GLyREPTDEQRERARE-------LLELLG-LAHLADRPFGTLSQ 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   533 GQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDK-AREGRTTIV-IAHRLStvrnaDVIAGFD------GGV 604
Cdd:COG1119  146 GEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKlAAEGAPTLVlVTHHVE-----EIPPGIThvlllkDGR 220
                        250
                 ....*....|....
gi 6755046   605 IVEQGNHDELMREK 618
Cdd:COG1119  221 VVAAGPKEEVLTSE 234
ABC_6TM_ABCB10_like cd18573
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ...
712-968 1.04e-28

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: 117.62  E-value: 1.04e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   712 GVLCAVINGCIQPVFAIVFSRIVGVFS-RDDDHETKRQNCNLFSLFFLVMGLISFVTYFFQGFTFGKAGEILTKRVRYMV 790
Cdd:cd18573    1 ALALLLVSSAVTMSVPFAIGKLIDVASkESGDIEIFGLSLKTFALALLGVFVVGAAANFGRVYLLRIAGERIVARLRKRL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   791 FKSMLRQDISWFDDHKnsTGSLTTRLASDASSVKGAMGARLAVVTQNVANLGTGVILSLVYGWQLTLLLVVIIPLIVLGG 870
Cdd:cd18573   81 FKSILRQDAAFFDKNK--TGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   871 IIEMKLLSGQALKDKKQLEISGKIATEAIENFRTIVSLTREQKFETMYAQSLQVPYRNAMKKAHVFGITFSFTQAMMYFS 950
Cdd:cd18573  159 VFYGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLS 238
                        250
                 ....*....|....*...
gi 6755046   951 YAACFRFGAYLVAQQLMT 968
Cdd:cd18573  239 LLSVLYYGGSLVASGELT 256
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
407-607 1.37e-28

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 116.32  E-value: 1.37e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    407 QILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTIN---VRYLREIIGVVSQEP---VLFA 480
Cdd:PRK10419   26 TVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqRKAFRRDIQMVFQDSisaVNPR 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    481 TTIAENIRYG-REDVTMDEIEKAVKEANAYDfIMKLPhqfDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSA 559
Cdd:PRK10419  106 KTVREIIREPlRHLLSLDKAERLARASEMLR-AVDLD---DSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSN 181
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 6755046    560 LDTESEAVVQAALDKAREGRTT--IVIAHRLSTV-RNADVIAGFDGGVIVE 607
Cdd:PRK10419  182 LDLVLQAGVIRLLKKLQQQFGTacLFITHDLRLVeRFCQRVMVMDNGQIVE 232
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
391-584 1.96e-28

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: 114.84  E-value: 1.96e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   391 LEFKNVHFNYPSRS-EVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTIN----VRYL 465
Cdd:COG4181    9 IELRGLTKTVGTGAgELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDedarARLR 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   466 REIIGVVSQEPVLFAT-TIAENI-----RYGREDVTmdeiEKAVKEANAYDfimklphqfdtlVGERG----AQLSGGQK 535
Cdd:COG4181   89 ARHVGFVFQSFQLLPTlTALENVmlpleLAGRRDAR----ARARALLERVG------------LGHRLdhypAQLSGGEQ 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 6755046   536 QRIAIARALVRNPKILLLDEATSALDTESEAVVQAAL-DKAREGRTTIVI 584
Cdd:COG4181  153 QRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLfELNRERGTTLVL 202
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
1046-1253 1.98e-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: 114.27  E-value: 1.98e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1046 PNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKqlNVQWLRAHLGIVSQEPILF-DCS 1124
Cdd:cd03301   11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVT--DLPPKDRDIAMVFQNYALYpHMT 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1125 IAENIAYGDNSRAVSHEEIVR----AAKEANIHQFIDSLPdkyntrvgdkgTQLSGGQKQRIAIARALVRQPHILLLDEA 1200
Cdd:cd03301   89 VYDNIAFGLKLRKVPKDEIDErvreVAELLQIEHLLDRKP-----------KQLSGGQRQRVALGRAIVREPKVFLMDEP 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 6755046  1201 TSALDTESEKVVQEALDK--AREGRTCIVIAH-RLSTIQNADLIVVIENGKVKEHG 1253
Cdd:cd03301  158 LSNLDAKLRVQMRAELKRlqQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
391-617 2.36e-28

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 115.96  E-value: 2.36e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    391 LEFKNVHFNYPSRSEVQ---ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTI-NVRYLR 466
Cdd:PRK13633    5 IKCKNVSYKYESNEESTeklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEeNLWDIR 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    467 EIIGVVSQEP--VLFATTIAENIRYGRED--VTMDEIEKAVKEA----NAYDFIMKLPHQfdtlvgergaqLSGGQKQRI 538
Cdd:PRK13633   85 NKAGMVFQNPdnQIVATIVEEDVAFGPENlgIPPEEIRERVDESlkkvGMYEYRRHAPHL-----------LSGGQKQRV 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    539 AIARALVRNPKILLLDEATSALDTESEAVVQAALDK--AREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMR 616
Cdd:PRK13633  154 AIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKElnKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFK 233

                  .
gi 6755046    617 E 617
Cdd:PRK13633  234 E 234
ABC_6TM_AtABCB27_like cd18780
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ...
724-968 2.50e-28

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: 116.58  E-value: 2.50e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   724 PVFaivFSRIVGVFSRD--DDHETKRQNCNLFSLFFLVMGLISFVTYFFQGFTFGKAGEILTKRVRYMVFKSMLRQDISW 801
Cdd:cd18780   16 PYF---FGQVIDAVTNHsgSGGEEALRALNQAVLILLGVVLIGSIATFLRSWLFTLAGERVVARLRKRLFSAIIAQEIAF 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   802 FDdhKNSTGSLTTRLASDASSVKGAMGARLAVVTQNVANLGTGVILSLVYGWQLTLLLVVIIPLIVLGGIIEMKLLSGQA 881
Cdd:cd18780   93 FD--VTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAVIYGKYVRKLS 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   882 LKDKKQLEISGKIATEAIENFRTIVSLTREQKFETMYAQSLQVPYRNAMKKAHVFGITFSFTQAMMYFSYAACFRFGAYL 961
Cdd:cd18780  171 KKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQLAIVLVLWYGGRL 250

                 ....*..
gi 6755046   962 VAQQLMT 968
Cdd:cd18780  251 VIDGELT 257
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
1049-1259 3.63e-28

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 114.42  E-value: 3.63e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1049 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIK--QLNVQWLRAHLGIVSQEPILFDCSIA 1126
Cdd:PRK09493   15 QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQEAGMVFQQFYLFPHLTA 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1127 -ENIAYGDNSravsheeiVRAAKEANIHQFIDSLPDKYN--TRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSA 1203
Cdd:PRK09493   95 lENVMFGPLR--------VRGASKEEAEKQARELLAKVGlaERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSA 166
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 6755046   1204 LDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLL 1259
Cdd:PRK09493  167 LDPElRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLI 224
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
390-616 3.71e-28

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 114.08  E-value: 3.71e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   390 NLEFKNVHFNYpsrsEVQILKgLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVrYLREIi 469
Cdd:COG3840    1 MLRLDDLTYRY----GDFPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPP-AERPV- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   470 GVVSQEPVLFA-TTIAENI--------RYGREDVTmdEIEKAVKEANAYDFIMKLPhqfdtlvgergAQLSGGQKQRIAI 540
Cdd:COG3840   74 SMLFQENNLFPhLTVAQNIglglrpglKLTAEQRA--QVEQALERVGLAGLLDRLP-----------GQLSGGQRQRVAL 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   541 ARALVRNPKILLLDEATSALD----TESEAVVQaalDKARE-GRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDEL 614
Cdd:COG3840  141 ARCLVRKRPILLLDEPFSALDpalrQEMLDLVD---ELCRErGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAAL 217

                 ..
gi 6755046   615 MR 616
Cdd:COG3840  218 LD 219
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
1051-1241 4.84e-28

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 114.49  E-value: 4.84e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1051 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD-----PMAGSVFLDGKEI---KQLNVQwLRAHLGIVSQEPILFD 1122
Cdd:PRK14239   21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIyspRTDTVD-LRKEIGMVFQQPNPFP 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1123 CSIAENIAYGDNSRAVSHEEIVRAAKEANIHQfiDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATS 1202
Cdd:PRK14239  100 MSIYENVVYGLRLKGIKDKQVLDEAVEKSLKG--ASIWDEVKDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTS 177
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 6755046   1203 ALDTESEKVVQEALDKAREGRTCIVIAHrlsTIQNADLI 1241
Cdd:PRK14239  178 ALDPISAGKIEETLLGLKDDYTMLLVTR---SMQQASRI 213
cbiO PRK13640
energy-coupling factor transporter ATPase;
1033-1254 5.39e-28

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 115.28  E-value: 5.39e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1033 VKFNGVQFNYPTRPNiPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGS---VFLDGKEIKQLNVQWLRA 1109
Cdd:PRK13640    6 VEFKHVSFTYPDSKK-PALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAKTVWDIRE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1110 HLGIVSQEP--ILFDCSIAENIAYGDNSRAVSHEEIVR----AAKEANIHQFIDSLPdkyntrvgdkgTQLSGGQKQRIA 1183
Cdd:PRK13640   85 KVGIVFQNPdnQFVGATVGDDVAFGLENRAVPRPEMIKivrdVLADVGMLDYIDSEP-----------ANLSGGQKQRVA 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6755046   1184 IARALVRQPHILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQNADLIVVIENGKVKEHGT 1254
Cdd:PRK13640  154 IAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGS 226
ABC_6TM_MsbA_like cd18552
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ...
143-339 9.79e-28

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: 114.44  E-value: 9.79e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   143 IHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDKIGMFFQSITTFLAGFIIGFISGWKLTLVILAVSP 222
Cdd:cd18552   71 VRDLRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLP 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   223 LIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQKELERYNKNLEEAKNVGIKKAITASISIGIAY 302
Cdd:cd18552  151 LAALPIRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLME 230
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 6755046   303 LLVYASYALAFWYGTSLVLSNEYSIGEVLTVFFSILL 339
Cdd:cd18552  231 LLGAIAIALVLWYGGYQVISGELTPGEFISFITALLL 267
cbiO PRK13637
energy-coupling factor transporter ATPase;
405-617 1.05e-27

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 114.37  E-value: 1.05e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    405 EVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDI--RTINVRYLREIIGVVSQEP--VLFA 480
Cdd:PRK13637   19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIRKKVGLVFQYPeyQLFE 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    481 TTIAENIRYGREDVTM--DEIEKAVKEANAydfIMKLPhqFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATS 558
Cdd:PRK13637   99 ETIEKDIAFGPINLGLseEEIENRVKRAMN---IVGLD--YEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTA 173
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6755046    559 ALD--TESEAVVQAALDKAREGRTTIVIAHRLSTV-RNADVIAGFDGGVIVEQGNHDELMRE 617
Cdd:PRK13637  174 GLDpkGRDEILNKIKELHKEYNMTIILVSHSMEDVaKLADRIIVMNKGKCELQGTPREVFKE 235
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
1047-1260 1.15e-27

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: 112.77  E-value: 1.15e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1047 NIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVqWLRAHLGI--VSQEPILF-DC 1123
Cdd:COG0410   15 GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPP-HRIARLGIgyVPEGRRIFpSL 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1124 SIAENI---AYGDNSRAVSHEEIVRAA------KEanihqfidslpdkyntRVGDKGTQLSGGQKQRIAIARALVRQPHI 1194
Cdd:COG0410   94 TVEENLllgAYARRDRAEVRADLERVYelfprlKE----------------RRRQRAGTLSGGEQQMLAIGRALMSRPKL 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6755046  1195 LLLDEATSALdteSEKVVQEALDK----AREGRTCIVI---AHRLSTIqnADLIVVIENGKVKEHGTHQQLLA 1260
Cdd:COG0410  158 LLLDEPSLGL---APLIVEEIFEIirrlNREGVTILLVeqnARFALEI--ADRAYVLERGRIVLEGTAAELLA 225
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
391-563 1.16e-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: 112.82  E-value: 1.16e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   391 LEFKNVHFNYPSrseVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRylREIIG 470
Cdd:cd03296    3 IEVRNVSKRFGD---FVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   471 VVSQEPVLFA-TTIAENIRYG------REDVTMDEIEKAVKEanaydfIMKLPhQFDTLVGERGAQLSGGQKQRIAIARA 543
Cdd:cd03296   78 FVFQHYALFRhMTVFDNVAFGlrvkprSERPPEAEIRAKVHE------LLKLV-QLDWLADRYPAQLSGGQRQRVALARA 150
                        170       180
                 ....*....|....*....|
gi 6755046   544 LVRNPKILLLDEATSALDTE 563
Cdd:cd03296  151 LAVEPKVLLLDEPFGALDAK 170
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
391-610 1.45e-27

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: 111.10  E-value: 1.45e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   391 LEFKNVHF---NYPSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTtvqLM-----QRLYDPLEGVVSIDGQDIRTINV 462
Cdd:cd03213    4 LSFRNLTVtvkSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKST---LLnalagRRTGLGVSGEVLINGRPLDKRSF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   463 RYlreIIGVVSQEPVLFAT-TIAENIrygredvtmdeiekavkeanayDFIMKLphqfdtlvgeRGaqLSGGQKQRIAIA 541
Cdd:cd03213   81 RK---IIGYVPQDDILHPTlTVRETL----------------------MFAAKL----------RG--LSGGERKRVSIA 123
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   542 RALVRNPKILLLDEATSALDTESEAVVQAALDK-AREGRTTIVIAHRLSTvrnaDVIAGFDGGVIVEQGN 610
Cdd:cd03213  124 LELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRlADTGRTIICSIHQPSS----EIFELFDKLLLLSQGR 189
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
409-609 1.52e-27

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: 111.62  E-value: 1.52e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   409 LKGLNLKVK---SGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQ---DIR-TINVRYLREIIGVVSQEPVLFA- 480
Cdd:cd03297   10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfDSRkKINLPPQQRKIGLVFQQYALFPh 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   481 TTIAENIRYGREDVTMDEIEKAVKEANAYdfimklpHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSAL 560
Cdd:cd03297   90 LNVRENLAFGLKRKRNREDRISVDELLDL-------LGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSAL 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 6755046   561 DTESEAVVQAALDK--AREGRTTIVIAHRLSTV-RNADVIAGFDGGVIVEQG 609
Cdd:cd03297  163 DRALRLQLLPELKQikKNLNIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
cbiO PRK13644
energy-coupling factor transporter ATPase;
1033-1260 2.05e-27

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 113.16  E-value: 2.05e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1033 VKFNGVQFNYPTrpNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLN-VQWLRAHL 1111
Cdd:PRK13644    2 IRLENVSYSYPD--GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1112 GIVSQEP--ILFDCSIAENIAYGDNSRAVSHEEIVRAAKEAnihqFIDSLPDKYNTRvgdKGTQLSGGQKQRIAIARALV 1189
Cdd:PRK13644   80 GIVFQNPetQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRA----LAEIGLEKYRHR---SPKTLSGGQGQCVALAGILT 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6755046   1190 RQPHILLLDEATSALDTESEKVVQEALDKA-REGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLA 1260
Cdd:PRK13644  153 MEPECLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLS 224
cbiO PRK13640
energy-coupling factor transporter ATPase;
391-634 2.10e-27

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 113.36  E-value: 2.10e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    391 LEFKNVHFNYPSrSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDP---LEGVVSIDGQDIRTINVRYLRE 467
Cdd:PRK13640    6 VEFKHVSFTYPD-SKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWDIRE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    468 IIGVVSQEP--VLFATTIAENIRYGRED--VTMDEIEKAVKEANA----YDFIMKLPhqfdtlvgergAQLSGGQKQRIA 539
Cdd:PRK13640   85 KVGIVFQNPdnQFVGATVGDDVAFGLENraVPRPEMIKIVRDVLAdvgmLDYIDSEP-----------ANLSGGQKQRVA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    540 IARALVRNPKILLLDEATSALDTESEAVVQAALDKARE--GRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDElmre 617
Cdd:PRK13640  154 IAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVE---- 229
                         250
                  ....*....|....*..
gi 6755046    618 kgIYFKLVMTQTRGNEI 634
Cdd:PRK13640  230 --IFSKVEMLKEIGLDI 244
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
1049-1247 2.60e-27

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 118.76  E-value: 2.60e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1049 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFL-DGKEIkqlnvqwlrahLgIVSQEPILFDCSIAE 1127
Cdd:COG4178  377 PLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARV-----------L-FLPQRPYLPLGTLRE 444
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1128 NIAYGDNSRAVSHEEIVRAAKEANIHQFIDSLpdkynTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTE 1207
Cdd:COG4178  445 ALLYPATAEAFSDAELREALEAVGLGHLAERL-----DEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEE 519
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 6755046  1208 SEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENG 1247
Cdd:COG4178  520 NEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLELTGD 559
nickel_nikE TIGR02769
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ...
1049-1262 2.76e-27

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: 112.59  E-value: 2.76e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    1049 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRA---HLGIVSQEpilfdcsi 1125
Cdd:TIGR02769   25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAfrrDVQLVFQD-------- 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    1126 aeniAYGDNSRAVSHEEIVR-----------AAKEANIHQFID--SLPDKYNTRVgdkGTQLSGGQKQRIAIARALVRQP 1192
Cdd:TIGR02769   97 ----SPSAVNPRMTVRQIIGeplrhltsldeSEQKARIAELLDmvGLRSEDADKL---PRQLSGGQLQRINIARALAVKP 169
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6755046    1193 HILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLLAQK 1262
Cdd:TIGR02769  170 KLIVLDEAVSNLDMVLQAVILELLRKlqQAFGTAYLFITHDLRLVQSfCQRVAVMDKGQIVEECDVAQLLSFK 242
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
391-606 2.90e-27

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: 109.06  E-value: 2.90e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   391 LEFKNVHFNYPSrseVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREI-I 469
Cdd:cd03216    1 LELRGITKRFGG---VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAgI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   470 GVVSQepvlfattiaenirygredvtmdeiekavkeanaydfimklphqfdtlvgergaqLSGGQKQRIAIARALVRNPK 549
Cdd:cd03216   78 AMVYQ-------------------------------------------------------LSVGERQMVEIARALARNAR 102
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 6755046   550 ILLLDEATSAL-DTESEAVVQAALDKAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIV 606
Cdd:cd03216  103 LLILDEPTAALtPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
391-633 2.97e-27

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 112.54  E-value: 2.97e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    391 LEFKNVHFNYPSrSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIG 470
Cdd:PRK13648    8 IVFKNVSFQYQS-DASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    471 VVSQEP--VLFATTIAENIRYGRED--VTMDEIEKAVKEA----NAYDFIMKLPHQfdtlvgergaqLSGGQKQRIAIAR 542
Cdd:PRK13648   87 IVFQNPdnQFVGSIVKYDVAFGLENhaVPYDEMHRRVSEAlkqvDMLERADYEPNA-----------LSGGQKQRVAIAG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    543 ALVRNPKILLLDEATSALDTESEAVVQAALDKAREGR--TTIVIAHRLSTVRNADVIAGFDGGVIVEQG------NHDEL 614
Cdd:PRK13648  156 VLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGtpteifDHAEE 235
                         250       260
                  ....*....|....*....|.
gi 6755046    615 MREKG--IYFKLVMTQTRGNE 633
Cdd:PRK13648  236 LTRIGldLPFPIKINQMLGHQ 256
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
384-618 3.22e-27

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 113.02  E-value: 3.22e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    384 PDSImgnLEFKNVHFNYPSRSEVqiLKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQ--DIRTIN 461
Cdd:PRK13636    2 EDYI---LKVEELNYNYSDGTHA--LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    462 VRYLREIIGVVSQEP--VLFATTIAENIRYGREDVTM--DEIEKAVKEANAYDFIMKLPHQfdtlvgeRGAQLSGGQKQR 537
Cdd:PRK13636   77 LMKLRESVGMVFQDPdnQLFSASVYQDVSFGAVNLKLpeDEVRKRVDNALKRTGIEHLKDK-------PTHCLSFGQKKR 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    538 IAIARALVRNPKILLLDEATSALDTE--SEaVVQAALDKAREGRTTIVIA-HRLSTVR-NADVIAGFDGGVIVEQGNHDE 613
Cdd:PRK13636  150 VAIAGVLVMEPKVLVLDEPTAGLDPMgvSE-IMKLLVEMQKELGLTIIIAtHDIDIVPlYCDNVFVMKEGRVILQGNPKE 228

                  ....*
gi 6755046    614 LMREK 618
Cdd:PRK13636  229 VFAEK 233
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
845-1265 3.48e-27

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: 120.44  E-value: 3.48e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     845 VILSLVYGWQ-----LTLLLVVIIPLIVLGGIIEMKLLSGQaLKDKKQLEISGKIATEAIENFRTIV----SLTREQKFE 915
Cdd:TIGR00957  445 VILALYFLWLnlgpsVLAGVAVMVLMVPLNAVMAMKTKTYQ-VAHMKSKDNRIKLMNEILNGIKVLKlyawELAFLDKVE 523
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     916 TMYAQSLQVpyrnaMKKAHVFGITFSFTQAMMYFSYAACfRFGAYLVAQQlmtfENVMLVFSAVVfgAMAAGNTSSFA-- 993
Cdd:TIGR00957  524 GIRQEELKV-----LKKSAYLHAVGTFTWVCTPFLVALI-TFAVYVTVDE----NNILDAEKAFV--SLALFNILRFPln 591
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     994 --PDYAKAKVSAS---HIIRIIEKTPEIDSYSTEGLKPTLLEGN-VKFNGVQFNYpTRPNIPVLQGLSLEVKKGQTLALV 1067
Cdd:TIGR00957  592 ilPMVISSIVQASvslKRLRIFLSHEELEPDSIERRTIKPGEGNsITVHNATFTW-ARDLPPTLNGITFSIPEGALVAVV 670
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    1068 GSSGCGKSTVVQLLERFYDPMAGSVFLDGKeikqlnvqwlrahLGIVSQEPILFDCSIAENIAYGDNSRAVSHEEIVRAA 1147
Cdd:TIGR00957  671 GQVGCGKSSLLSALLAEMDKVEGHVHMKGS-------------VAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEAC 737
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    1148 KeanIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEAL---DKAREGRT 1224
Cdd:TIGR00957  738 A---LLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVigpEGVLKNKT 814
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|.
gi 6755046    1225 CIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQKGIY 1265
Cdd:TIGR00957  815 RILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAF 855
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
391-614 3.89e-27

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 117.04  E-value: 3.89e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   391 LEFKNVHFNYPSrseVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREI-I 469
Cdd:COG1129    5 LEMRGISKSFGG---VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAgI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   470 GVVSQEPVLFAT-TIAENIRYGREDVT---MD--EIEKAVKEANAYdfiMKLPHQFDTLVGErgaqLSGGQKQRIAIARA 543
Cdd:COG1129   82 AIIHQELNLVPNlSVAENIFLGREPRRgglIDwrAMRRRARELLAR---LGLDIDPDTPVGD----LSVAQQQLVEIARA 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6755046   544 LVRNPKILLLDEATSAL-DTESEAVVQAALDKAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDEL 614
Cdd:COG1129  155 LSRDARVLILDEPTASLtEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEiADRVTVLRDGRLVGTGPVAEL 227
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
1046-1247 4.06e-27

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: 110.50  E-value: 4.06e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1046 PNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAH----LGIVSQEPILF 1121
Cdd:cd03290   12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWLL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1122 DCSIAENIAYGDNSRAVSHEEIVRAAkeaNIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEAT 1201
Cdd:cd03290   92 NATVEENITFGSPFNKQRYKAVTDAC---SLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPF 168
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 6755046  1202 SALDTE-SEKVVQEALDK--AREGRTCIVIAHRLSTIQNADLIVVIENG 1247
Cdd:cd03290  169 SALDIHlSDHLMQEGILKflQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
1050-1251 4.06e-27

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: 110.99  E-value: 4.06e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQL---LERfydPMAGSVFLDGKEIKQLN----VQWLRAHLGIVSQE----P 1118
Cdd:COG4181   27 ILKGISLEVEAGESVAIVGASGSGKSTLLGLlagLDR---PTSGTVRLAGQDLFALDedarARLRARHVGFVFQSfqllP 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1119 ILfdcSIAEN------IAYGDNSRAVSHEEIVRAAKEANIHQFidslPdkyntrvgdkgTQLSGGQKQRIAIARALVRQP 1192
Cdd:COG4181  104 TL---TALENvmlpleLAGRRDARARARALLERVGLGHRLDHY----P-----------AQLSGGEQQRVALARAFATEP 165
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6755046  1193 HILLLDEATSALDTESEKVVQEAL-DKARE-GRTCIVIAHRLSTIQNADLIVVIENGKVKE 1251
Cdd:COG4181  166 AILFADEPTGNLDAATGEQIIDLLfELNRErGTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
cbiO PRK13637
energy-coupling factor transporter ATPase;
1051-1254 4.52e-27

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 112.45  E-value: 4.52e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1051 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEI--KQLNVQWLRAHLGIVSQEP--ILFDCSIA 1126
Cdd:PRK13637   23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIRKKVGLVFQYPeyQLFEETIE 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1127 ENIAYGDNSRAVSHEEIVRAAKEAnihqfIDSLPDKYNTrVGDKGT-QLSGGQKQRIAIARALVRQPHILLLDEATSALD 1205
Cdd:PRK13637  103 KDIAFGPINLGLSEEEIENRVKRA-----MNIVGLDYED-YKDKSPfELSGGQKRRVAIAGVVAMEPKILILDEPTAGLD 176
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 6755046   1206 TeseKVVQEALDKARE-----GRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGT 1254
Cdd:PRK13637  177 P---KGRDEILNKIKElhkeyNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGT 228
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
1038-1262 4.91e-27

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 112.09  E-value: 4.91e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1038 VQFNYPTrpNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWL--RAHLGIVS 1115
Cdd:PRK13639    7 LKYSYPD--GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLevRKTVGIVF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1116 QEP--ILFDCSIAENIAYGDNSRAVSHEEIVRAAKEAnihqfidslpdkyNTRVGDKGTQ------LSGGQKQRIAIARA 1187
Cdd:PRK13639   85 QNPddQLFAPTVEEDVAFGPLNLGLSKEEVEKRVKEA-------------LKAVGMEGFEnkpphhLSGGQKKRVAIAGI 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6755046   1188 LVRQPHILLLDEATSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQ-NADLIVVIENGKVKEHGTHQQLLAQK 1262
Cdd:PRK13639  152 LAMKPEIIVLDEPTSGLDPMgASQIMKLLYDLNKEGITIIISTHDVDLVPvYADKVYVMSDGKIIKEGTPKEVFSDI 228
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
1033-1253 5.21e-27

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: 110.28  E-value: 5.21e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1033 VKFNGVQFNYPTRPnipvlQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQwlRAHLG 1112
Cdd:cd03298    1 VRLDKIRFSYGEQP-----MHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVS 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1113 IVSQEPILF-DCSIAENIAYGDNSR----AVSHEEIVRAAKEANIHQFIDSLPDkyntrvgdkgtQLSGGQKQRIAIARA 1187
Cdd:cd03298   74 MLFQENNLFaHLTVEQNVGLGLSPGlkltAEDRQAIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALARV 142
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6755046  1188 LVRQPHILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHG 1253
Cdd:cd03298  143 LVRDKPVLLLDEPFAALDPALRAEMLDLVLDlhAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
1050-1265 5.73e-27

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: 111.87  E-value: 5.73e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDpMAGSVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAENI 1129
Cdd:cd03289   19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTFRKNL 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1130 aygDNSRAVSHEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESE 1209
Cdd:cd03289   98 ---DPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITY 174
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 6755046  1210 KVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQKGIY 1265
Cdd:cd03289  175 QVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHF 230
cbiO PRK13642
energy-coupling factor transporter ATPase;
1040-1260 6.14e-27

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 112.11  E-value: 6.14e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1040 FNYPTRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGIVSQEP- 1118
Cdd:PRK13642   12 FKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQNPd 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1119 -ILFDCSIAENIAYGDNSRAVSHEEIVRAAKEANIHqfIDSLpdKYNTRvgdKGTQLSGGQKQRIAIARALVRQPHILLL 1197
Cdd:PRK13642   92 nQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLA--VNML--DFKTR---EPARLSGGQKQRVAVAGIIALRPEIIIL 164
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6755046   1198 DEATSALD----TESEKVVQEALDKARegRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLA 1260
Cdd:PRK13642  165 DESTSMLDptgrQEIMRVIHEIKEKYQ--LTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
388-609 1.00e-26

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 110.39  E-value: 1.00e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    388 MGNLEFKNVHFNYpsrSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYD-----PLEGVVSIDGQDIRTINV 462
Cdd:PRK14247    1 MNKIEIRDLKVSF---GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    463 RYLREIIGVVSQEPVLFAT-TIAENIRYG----REDVTMDEIEKAVKEANAYdfiMKLPHQFDTLVGERGAQLSGGQKQR 537
Cdd:PRK14247   78 IELRRRVQMVFQIPNPIPNlSIFENVALGlklnRLVKSKKELQERVRWALEK---AQLWDEVKDRLDAPAGKLSGGQQQR 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6755046    538 IAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAH-RLSTVRNADVIAGFDGGVIVEQG 609
Cdd:PRK14247  155 LCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWG 227
cbiO PRK13646
energy-coupling factor transporter ATPase;
391-618 1.06e-26

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 111.41  E-value: 1.06e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    391 LEFKNVHFNYPSRS--EVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDI----RTINVRY 464
Cdd:PRK13646    3 IRFDNVSYTYQKGTpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktKDKYIRP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    465 LREIIGVVSQ--EPVLFATTIAENIRYGREDVTMDeIEKAvkEANAYDFIMKLPHQFDTLvGERGAQLSGGQKQRIAIAR 542
Cdd:PRK13646   83 VRKRIGMVFQfpESQLFEDTVEREIIFGPKNFKMN-LDEV--KNYAHRLLMDLGFSRDVM-SQSPFQMSGGQMRKIAIVS 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6755046    543 ALVRNPKILLLDEATSALDTESEAVVQAALDKAR--EGRTTIVIAHRLSTV-RNADVIAGFDGGVIVEQGNHDELMREK 618
Cdd:PRK13646  159 ILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFKDK 237
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
391-586 1.13e-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: 109.52  E-value: 1.13e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   391 LEFKNVHFNYPSRSeVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTiNVRYLREIIG 470
Cdd:cd03263    1 LQIRNLTKTYKKGT-KPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   471 VVSQEPVLFAT-TIAENIRY-----GREDVTMDEiekavkEANAYDFIMKLPHQFDTLVGergaQLSGGQKQRIAIARAL 544
Cdd:cd03263   79 YCPQFDALFDElTVREHLRFyarlkGLPKSEIKE------EVELLLRVLGLTDKANKRAR----TLSGGMKRKLSLAIAL 148
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 6755046   545 VRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAH 586
Cdd:cd03263  149 IGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTH 190
ABC_6TM_TAP cd18572
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ...
709-971 1.26e-26

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: 111.48  E-value: 1.26e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   709 LLVGVLCAVINGCIqPVFAivfSRIVGVFSRDDDHETKRQNCNLFSLFFLVMGLISFvtyfFQGFTFGKAGEILTKRVRY 788
Cdd:cd18572    2 FVFLVVAALSELAI-PHYT---GAVIDAVVADGSREAFYRAVLLLLLLSVLSGLFSG----LRGGCFSYAGTRLVRRLRR 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   789 MVFKSMLRQDISWFDDHKnsTGSLTTRLASDASSVKGAMGARLAVVTQNVANLGTGVILSLVYGWQLTLLLVVIIPLIVL 868
Cdd:cd18572   74 DLFRSLLRQDIAFFDATK--TGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIAL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   869 -----GGIieMKLLSGQAlkdKKQLEISGKIATEAIENFRTIVSLTREQKFETMYAQSLQVPYRNAMKKAHVFGITFSFT 943
Cdd:cd18572  152 itkvyGRY--YRKLSKEI---QDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVN 226
                        250       260
                 ....*....|....*....|....*...
gi 6755046   944 QAMMYFSYAACFRFGAYLVAQQLMTFEN 971
Cdd:cd18572  227 TLLQNGTQVLVLFYGGHLVLSGRMSAGQ 254
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
391-616 1.30e-26

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: 109.69  E-value: 1.30e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   391 LEFKNVHFNYPsrsEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINV-RYLREII 469
Cdd:COG0410    4 LEVENLHAGYG---GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPhRIARLGI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   470 GVVSQEPVLFAT-TIAENIR---YGREDVtmDEIEKAVKEAnaYDFimklphqFDTLvGER----GAQLSGGQKQRIAIA 541
Cdd:COG0410   81 GYVPEGRRIFPSlTVEENLLlgaYARRDR--AEVRADLERV--YEL-------FPRL-KERrrqrAGTLSGGEQQMLAIG 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   542 RALVRNPKILLLDEATSALdteSEAVVQ---AALDKAREGRTTIVI----AHRLSTVrnADVIAGFDGGVIVEQGNHDEL 614
Cdd:COG0410  149 RALMSRPKLLLLDEPSLGL---APLIVEeifEIIRRLNREGVTILLveqnARFALEI--ADRAYVLERGRIVLEGTAAEL 223

                 ..
gi 6755046   615 MR 616
Cdd:COG0410  224 LA 225
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
405-615 1.39e-26

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 110.44  E-value: 1.39e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    405 EVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTI-------------NVRYLREIIGV 471
Cdd:PRK10619   17 EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlkvadknQLRLLRTRLTM 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    472 VSQEPVLFA-TTIAENIRygREDVTMDEIEKAVKEANAYDFIMKLPHQfDTLVGERGAQLSGGQKQRIAIARALVRNPKI 550
Cdd:PRK10619   97 VFQHFNLWShMTVLENVM--EAPIQVLGLSKQEARERAVKYLAKVGID-ERAQGKYPVHLSGGQQQRVSIARALAMEPEV 173
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6755046    551 LLLDEATSALDTESEAVVQAALDK-AREGRTTIVIAHRLSTVRNADVIAGF-DGGVIVEQGNHDELM 615
Cdd:PRK10619  174 LLFDEPTSALDPELVGEVLRIMQQlAEEGKTMVVVTHEMGFARHVSSHVIFlHQGKIEEEGAPEQLF 240
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...
1050-1249 1.40e-26

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: 110.13  E-value: 1.40e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVqWLRAHLGIVS--QEPILF-DCSIA 1126
Cdd:COG0411   19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPP-HRIARLGIARtfQNPRLFpELTVL 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1127 ENIAYG--------------DNSRAVSHEEIVRAAKEANIHQFidSLPDKYNTRVGDkgtqLSGGQKQRIAIARALVRQP 1192
Cdd:COG0411   98 ENVLVAaharlgrgllaallRLPRARREEREARERAEELLERV--GLADRADEPAGN----LSYGQQRRLEIARALATEP 171
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6755046  1193 HILLLDEATSAL-DTESEKVVqEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVIENGKV 1249
Cdd:COG0411  172 KLLLLDEPAAGLnPEETEELA-ELIRRLRDerGITILLIEHDMDLVMGlADRIVVLDFGRV 231
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
391-609 1.52e-26

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: 115.94  E-value: 1.52e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   391 LEFKN--VHFNYPSRsEVQILKGLNLKVKSGQTVALVGNSGCGKSTT----VQLMQRLYDPLEGVVSIDGQDIRTINVRY 464
Cdd:COG4172    7 LSVEDlsVAFGQGGG-TVEAVKGVSFDIAAGETLALVGESGSGKSVTalsiLRLLPDPAAHPSGSILFDGQDLLGLSERE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   465 LREI----IGVVSQEPV-----LFatTI----AENIR----YGREDVT------MDE--IEKAVKEANAYdfimklPHQf 519
Cdd:COG4172   86 LRRIrgnrIAMIFQEPMtslnpLH--TIgkqiAEVLRlhrgLSGAAARaralelLERvgIPDPERRLDAY------PHQ- 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   520 dtlvgergaqLSGGQKQRIAIARALVRNPKILLLDEATSALDteseAVVQAA-LD-----KAREGRTTIVIAHRLSTVRN 593
Cdd:COG4172  157 ----------LSGGQRQRVMIAMALANEPDLLIADEPTTALD----VTVQAQiLDllkdlQRELGMALLLITHDLGVVRR 222
                        250
                 ....*....|....*..
gi 6755046   594 -ADVIAGFDGGVIVEQG 609
Cdd:COG4172  223 fADRVAVMRQGEIVEQG 239
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
1049-1259 1.90e-26

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 109.86  E-value: 1.90e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1049 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGIVSQEPIL-FDCSIAE 1127
Cdd:PRK13548   16 TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFTVEE 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1128 NIAYGdnsrAVSHEEIVRAAKEanihqfidsLPDKYNTRVGDKG------TQLSGGQKQRIAIARALVR------QPHIL 1195
Cdd:PRK13548   96 VVAMG----RAPHGLSRAEDDA---------LVAAALAQVDLAHlagrdyPQLSGGEQQRVQLARVLAQlwepdgPPRWL 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6755046   1196 LLDEATSALD-TESEKVVQEALDKARE-GRTCIVIAHRLS-TIQNADLIVVIENGKVKEHGTHQQLL 1259
Cdd:PRK13548  163 LLDEPTSALDlAHQHHVLRLARQLAHErGLAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPAEVL 229
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
1050-1260 2.17e-26

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 109.45  E-value: 2.17e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEI--------KQLNVQWLRAHLGIVSQEPILF 1121
Cdd:PRK11264   18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtarslsqQKGLIRQLRQHVGFVFQNFNLF 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1122 DC-SIAENIAYGDN-SRAVSHEEIVRAAKEANIHQFIDSLPDKYNTRvgdkgtqLSGGQKQRIAIARALVRQPHILLLDE 1199
Cdd:PRK11264   98 PHrTVLENIIEGPViVKGEPKEEATARARELLAKVGLAGKETSYPRR-------LSGGQQQRVAIARALAMRPEVILFDE 170
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6755046   1200 ATSALDTEsekVVQEALDK----AREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLLA 1260
Cdd:PRK11264  171 PTSALDPE---LVGEVLNTirqlAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFA 233
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
390-612 3.08e-26

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


Pssm-ID: 443326 [Multi-domain]  Cd Length: 242  Bit Score: 108.95  E-value: 3.08e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   390 NLEFKNVHFNYPSrseVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDG------QDIRTINVR 463
Cdd:COG4161    2 SIQLKNINCFYGS---HQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   464 YLREIIGVVSQE----PVLfatTIAENIrygredvtmdeIEKAVK-----EANAYDFIMKLPH--QFDTLVGERGAQLSG 532
Cdd:COG4161   79 LLRQKVGMVFQQynlwPHL---TVMENL-----------IEAPCKvlglsKEQAREKAMKLLArlRLTDKADRFPLHLSG 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   533 GQKQRIAIARALVRNPKILLLDEATSALDTESEA-VVQAALDKAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGN 610
Cdd:COG4161  145 GQQQRVAIARALMMEPQVLLFDEPTAALDPEITAqVVEIIRELSQTGITQVIVTHEVEFARKvASQVVYMEKGRIIEQGD 224

                 ..
gi 6755046   611 HD 612
Cdd:COG4161  225 AS 226
cbiO PRK13649
energy-coupling factor transporter ATPase;
1049-1254 3.11e-26

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 109.83  E-value: 3.11e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1049 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEI----KQLNVQWLRAHLGIVSQ--EPILFD 1122
Cdd:PRK13649   21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstsKNKDIKQIRKKVGLVFQfpESQLFE 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1123 CSIAENIAYGDNSRAVSHEEIVRAAKEA-NIHQFIDSLPDKyntrvgdKGTQLSGGQKQRIAIARALVRQPHILLLDEAT 1201
Cdd:PRK13649  101 ETVLKDVAFGPQNFGVSQEEAEALAREKlALVGISESLFEK-------NPFELSGGQMRRVAIAGILAMEPKILVLDEPT 173
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 6755046   1202 SALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGT 1254
Cdd:PRK13649  174 AGLDPKGRKELMTLFKKLHQsGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGK 228
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
1049-1261 3.21e-26

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: 114.78  E-value: 3.21e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1049 PVLQGLSLEVKKGQTLALVGSSGCGKS----TVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRA----HLGIVSQEPI- 1119
Cdd:COG4172   24 EAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRirgnRIAMIFQEPMt 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1120 ----LFdcSIAENIA-----YGDNSRAVSHEEIVRAAKEANIHQfidslPDKyntRVGDKGTQLSGGQKQRIAIARALVR 1190
Cdd:COG4172  104 slnpLH--TIGKQIAevlrlHRGLSGAAARARALELLERVGIPD-----PER---RLDAYPHQLSGGQRQRVMIAMALAN 173
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6755046  1191 QPHILLLDEATSALDTesekVVQ-EALD-----KAREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLLAQ 1261
Cdd:COG4172  174 EPDLLIADEPTTALDV----TVQaQILDllkdlQRELGMALLLITHDLGVVRRfADRVAVMRQGEIVEQGPTAELFAA 247
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
1033-1260 3.61e-26

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 110.11  E-value: 3.61e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1033 VKFNGVQFNYptRPNIP----VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEI----KQLNV 1104
Cdd:PRK13634    3 ITFQKVEHRY--QYKTPferrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkKNKKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1105 QWLRAHLGIVSQ--EPILFDCSIAENIAYGDNSRAVSHEEIVRAAKEAnihqfID--SLPDKYNTRvgdKGTQLSGGQKQ 1180
Cdd:PRK13634   81 KPLRKKVGIVFQfpEHQLFEETVEKDICFGPMNFGVSEEDAKQKAREM-----IElvGLPEELLAR---SPFELSGGQMR 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1181 RIAIARALVRQPHILLLDEATSALDTESEKVVQE---ALDKaREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQ 1256
Cdd:PRK13634  153 RVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEmfyKLHK-EKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPR 231

                  ....
gi 6755046   1257 QLLA 1260
Cdd:PRK13634  232 EIFA 235
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
391-561 3.67e-26

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 111.35  E-value: 3.67e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    391 LEFKNVHFNYPSRSevqILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDI--RTINVRYlrei 468
Cdd:PRK11432    7 VVLKNITKRFGSNT---VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVthRSIQQRD---- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    469 IGVVSQEPVLFA-TTIAENIRYG--REDVTMDEIEKAVKEANAydfIMKLPHQFDTLVGergaQLSGGQKQRIAIARALV 545
Cdd:PRK11432   80 ICMVFQSYALFPhMSLGENVGYGlkMLGVPKEERKQRVKEALE---LVDLAGFEDRYVD----QISGGQQQRVALARALI 152
                         170
                  ....*....|....*.
gi 6755046    546 RNPKILLLDEATSALD 561
Cdd:PRK11432  153 LKPKVLLFDEPLSNLD 168
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
1033-1235 4.66e-26

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 108.97  E-value: 4.66e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1033 VKFNGVQFNYPTRPnipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDpMAGSVFLDGK-EI-------KQLNV 1104
Cdd:PRK14258    8 IKVNNLSFYYDTQK---ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEGRvEFfnqniyeRRVNL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1105 QWLRAHLGIVSQEPILFDCSIAENIAYGDN----SRAVSHEEIVRAAKEANihqfidSLPDKYNTRVGDKGTQLSGGQKQ 1180
Cdd:PRK14258   84 NRLRRQVSMVHPKPNLFPMSVYDNVAYGVKivgwRPKLEIDDIVESALKDA------DLWDEIKHKIHKSALDLSGGQQQ 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 6755046   1181 RIAIARALVRQPHILLLDEATSALDTESEKVVQEALD--KAREGRTCIVIAHRLSTI 1235
Cdd:PRK14258  158 RLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVSHNLHQV 214
TauB COG4525
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
388-561 4.67e-26

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


Pssm-ID: 443596 [Multi-domain]  Cd Length: 262  Bit Score: 108.80  E-value: 4.67e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   388 MGNLEFKNVHFNYP-SRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRylR 466
Cdd:COG4525    1 MSMLTVRHVSVRYPgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGAD--R 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   467 eiiGVVSQEPVLFA-TTIAENIRYGredVTMDEIEKAVKEANAydfimklpHQFDTLVGERGA------QLSGGQKQRIA 539
Cdd:COG4525   79 ---GVVFQKDALLPwLNVLDNVAFG---LRLRGVPKAERRARA--------EELLALVGLADFarrriwQLSGGMRQRVG 144
                        170       180
                 ....*....|....*....|..
gi 6755046   540 IARALVRNPKILLLDEATSALD 561
Cdd:COG4525  145 IARALAADPRFLLMDEPFGALD 166
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
1051-1247 4.72e-26

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: 107.94  E-value: 4.72e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    1051 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLrahlgIVSQEPILFD-CSIAENI 1129
Cdd:TIGR01184    1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPwLTVRENI 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    1130 AYGDNS--RAVSHEEivraaKEANIHQFIDSLPdkyNTRVGDKG-TQLSGGQKQRIAIARALVRQPHILLLDEATSALDT 1206
Cdd:TIGR01184   76 ALAVDRvlPDLSKSE-----RRAIVEEHIALVG---LTEAADKRpGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDA 147
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 6755046    1207 ESEKVVQEALDKARE--GRTCIVIAHRL-STIQNADLIVVIENG 1247
Cdd:TIGR01184  148 LTRGNLQEELMQIWEehRVTVLMVTHDVdEALLLSDRVVMLTNG 191
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
1033-1259 6.42e-26

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: 108.25  E-value: 6.42e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1033 VKFNGVQFNYPTRPnipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAG-SVFLDGKEIKQLNVQWLRAHL 1111
Cdd:COG1119    4 LELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKRI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1112 GIVS---QEPILFDCSIAENIAYGDNS-----RAVSHEEIVRAakEANIHQF-IDSLPDK-YNTrvgdkgtqLSGGQKQR 1181
Cdd:COG1119   81 GLVSpalQLRFPRDETVLDVVLSGFFDsiglyREPTDEQRERA--RELLELLgLAHLADRpFGT--------LSQGEQRR 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1182 IAIARALVRQPHILLLDEATSALDTESEKVVQEALDK-AREGRTCIV-IAHRL----STIQNAdliVVIENGKVKEHGTH 1255
Cdd:COG1119  151 VLIARALVKDPELLILDEPTAGLDLGARELLLALLDKlAAEGAPTLVlVTHHVeeipPGITHV---LLLKDGRVVAAGPK 227

                 ....
gi 6755046  1256 QQLL 1259
Cdd:COG1119  228 EEVL 231
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
409-616 6.96e-26

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: 107.52  E-value: 6.96e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   409 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRylrEI----IGVVSQEPVLFAT-TI 483
Cdd:cd03219   16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPH---EIarlgIGRTFQIPRLFPElTV 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   484 AENIRYG-----REDVTMDEIEKAVKEANAYDF----IMKLPHQFDTLVGErgaqLSGGQKQRIAIARALVRNPKILLLD 554
Cdd:cd03219   93 LENVMVAaqartGSGLLLARARREEREARERAEelleRVGLADLADRPAGE----LSYGQQRRLEIARALATDPKLLLLD 168
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6755046   555 EATSAL-DTESEAVVQAALDKAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDELMR 616
Cdd:cd03219  169 EPAAGLnPEETEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRN 232
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
403-609 7.18e-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: 7.18e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   403 RSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQL-MQRLYDP--LEGVVSIDGQDIRtinvRYL-REIIGVVSQEPVL 478
Cdd:cd03234   17 NKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAiSGRVEGGgtTSGQILFNGQPRK----PDQfQKCVAYVRQDDIL 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   479 FAT-TIAENIRYGREDVTMDEIEKAVKEANAYDFIMKLPHqfDTLVG-ERGAQLSGGQKQRIAIARALVRNPKILLLDEA 556
Cdd:cd03234   93 LPGlTVRETLTYTAILRLPRKSSDAIRKKRVEDVLLRDLA--LTRIGgNLVKGISGGERRRVSIAVQLLWDPKVLILDEP 170
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 6755046   557 TSALDTESE-AVVQAALDKAREGRTTIVIAH--RLSTVRNADVIAGFDGGVIVEQG 609
Cdd:cd03234  171 TSGLDSFTAlNLVSTLSQLARRNRIVILTIHqpRSDLFRLFDRILLLSSGEIVYSG 226
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
391-609 7.89e-26

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: 106.51  E-value: 7.89e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   391 LEFKNVHFNYPSRsevQILKGLNLKVKSGQTvALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRtINVRYLREIIG 470
Cdd:cd03264    1 LQLENLTKRYGKK---RALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVL-KQPQKLRRRIG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   471 VVSQEPVLFAT-TIAENIRY-----GREDVTMD-EIEKAVKEANAYDFimklphqfdtlVGERGAQLSGGQKQRIAIARA 543
Cdd:cd03264   76 YLPQEFGVYPNfTVREFLDYiawlkGIPSKEVKaRVDEVLELVNLGDR-----------AKKKIGSLSGGMRRRVGIAQA 144
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6755046   544 LVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQG 609
Cdd:cd03264  145 LVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
1047-1261 7.96e-26

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 108.64  E-value: 7.96e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1047 NIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQW-LRAHLGIVSQEPilfDCSI 1125
Cdd:PRK13633   22 EKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWdIRNKAGMVFQNP---DNQI 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1126 A-----ENIAYGDNSRAVSHEEIVR----AAKEANIHQFIDSLPDkyntrvgdkgtQLSGGQKQRIAIARALVRQPHILL 1196
Cdd:PRK13633   99 VativeEDVAFGPENLGIPPEEIRErvdeSLKKVGMYEYRRHAPH-----------LLSGGQKQRVAIAGILAMRPECII 167
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6755046   1197 LDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQ 1261
Cdd:PRK13633  168 FDEPTAMLDPSGRREVVNTIKElnKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFKE 234
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
409-601 1.16e-25

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 107.95  E-value: 1.16e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    409 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPL-----EGVVSIDGQDI--RTINVRYLREIIGVVSQEPVLFAT 481
Cdd:PRK14243   26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIpgfrvEGKVTFHGKNLyaPDVDPVEVRRRIGMVFQKPNPFPK 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    482 TIAENIRYGRE----DVTMDE-IEKAVKEANAYDFIMklphqfDTLvGERGAQLSGGQKQRIAIARALVRNPKILLLDEA 556
Cdd:PRK14243  106 SIYDNIAYGARingyKGDMDElVERSLRQAALWDEVK------DKL-KQSGLSLSGGQQQRLCIARAIAVQPEVILMDEP 178
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 6755046    557 TSALDTESEAVVQAALDKAREGRTTIVIAHRLSTV-RNADVIAGFD 601
Cdd:PRK14243  179 CSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAaRVSDMTAFFN 224
cbiO PRK13641
energy-coupling factor transporter ATPase;
1033-1262 1.23e-25

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 108.38  E-value: 1.23e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1033 VKFNGVqfNYPTRPNIPV----LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIK----QLNV 1104
Cdd:PRK13641    3 IKFENV--DYIYSPGTPMekkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1105 QWLRAHLGIVSQ--EPILFDCSIAENIAYGDNSRAVSHEEivraAKEANIhqfidslpdKYNTRVG------DKGT-QLS 1175
Cdd:PRK13641   81 KKLRKKVSLVFQfpEAQLFENTVLKDVEFGPKNFGFSEDE----AKEKAL---------KWLKKVGlsedliSKSPfELS 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1176 GGQKQRIAIARALVRQPHILLLDEATSALDTESEK-VVQEALDKAREGRTCIVIAHRLSTI-QNADLIVVIENGKVKEHG 1253
Cdd:PRK13641  148 GGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKeMMQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKLIKHA 227

                  ....*....
gi 6755046   1254 THQQLLAQK 1262
Cdd:PRK13641  228 SPKEIFSDK 236
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
391-614 1.57e-25

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 109.03  E-value: 1.57e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    391 LEFKN--VHFNYPSRSEV-----QILK---GLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTI 460
Cdd:PRK15079    9 LEVADlkVHFDIKDGKQWfwqppKTLKavdGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGM 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    461 NVRYLREI---IGVVSQEPV-------LFATTIAENIRYGREDVTMDEIEKAVKEANAY-----DFIMKLPHQFdtlvge 525
Cdd:PRK15079   89 KDDEWRAVrsdIQMIFQDPLaslnprmTIGEIIAEPLRTYHPKLSRQEVKDRVKAMMLKvgllpNLINRYPHEF------ 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    526 rgaqlSGGQKQRIAIARALVRNPKILLLDEATSALDTESEA-VVQAALDKARE-GRTTIVIAHRLSTVRN-ADVIAGFDG 602
Cdd:PRK15079  163 -----SGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAqVVNLLQQLQREmGLSLIFIAHDLAVVKHiSDRVLVMYL 237
                         250
                  ....*....|..
gi 6755046    603 GVIVEQGNHDEL 614
Cdd:PRK15079  238 GHAVELGTYDEV 249
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
1050-1261 1.68e-25

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 107.36  E-value: 1.68e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIK-------QLNV------QWLRAHLGIVSQ 1116
Cdd:PRK10619   20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgQLKVadknqlRLLRTRLTMVFQ 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1117 EPILFD-CSIAENIAYGDN-----SRAVSHEEIVRAAKEANIHqfiDSLPDKYNTrvgdkgtQLSGGQKQRIAIARALVR 1190
Cdd:PRK10619  100 HFNLWShMTVLENVMEAPIqvlglSKQEARERAVKYLAKVGID---ERAQGKYPV-------HLSGGQQQRVSIARALAM 169
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6755046   1191 QPHILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLLAQ 1261
Cdd:PRK10619  170 EPEVLLFDEPTSALDPELVGEVLRIMQQlAEEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLFGN 242
ABC_6TM_LmrA_like cd18551
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ...
141-361 2.09e-25

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: 107.90  E-value: 2.09e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   141 RQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDKIGMFFQSITTFLAGFIIGFISGWKLTLVILAV 220
Cdd:cd18551   66 RVVLDLRRRLWRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAV 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   221 SPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQKELERYNKNLEEAKNVGIKKAITASISIGI 300
Cdd:cd18551  146 VPLAFLIILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPL 225
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6755046   301 AYLLVYASYALAFWYGTSLVLSNEYSIGEVLTVFFSILLGTFSIGHLAPNIEAFANARGAA 361
Cdd:cd18551  226 MGLAVQLALLVVLGVGGARVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGAL 286
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
1050-1253 2.27e-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: 105.35  E-value: 2.27e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1050 VLQGLSLEVKKGQTlALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQlNVQWLRAHLGIVSQEPILFD-CSIAEN 1128
Cdd:cd03264   15 ALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGYLPQEFGVYPnFTVREF 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1129 IAY-----GDNSRAVsHEEIVRAAKEANihqfidsLPDKYNTRVGdkgtQLSGGQKQRIAIARALVRQPHILLLDEATSA 1203
Cdd:cd03264   93 LDYiawlkGIPSKEV-KARVDEVLELVN-------LGDRAKKKIG----SLSGGMRRRVGIAQALVGDPSILIVDEPTAG 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 6755046  1204 LDTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHG 1253
Cdd:cd03264  161 LDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
1051-1261 2.87e-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: 109.03  E-value: 2.87e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1051 LQGLSLEVK-----KGQTlALVGSSGCGKSTVVQL---LERfydPMAGSVFLDGkEIKQ--LNVQWLRAH---LGIVSQE 1117
Cdd:COG4148   11 RGGFTLDVDftlpgRGVT-ALFGPSGSGKTTLLRAiagLER---PDSGRIRLGG-EVLQdsARGIFLPPHrrrIGYVFQE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1118 PILFD-CSIAENIAYG-----DNSRAVSHEEIVRAAkeaNIHQFIDSLPDkyntrvgdkgtQLSGGQKQRIAIARALVRQ 1191
Cdd:COG4148   86 ARLFPhLSVRGNLLYGrkrapRAERRISFDEVVELL---GIGHLLDRRPA-----------TLSGGERQRVAIGRALLSS 151
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6755046  1192 PHILLLDEATSALDTESeKvvQEALDK----AREGRTCIV-IAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLLAQ 1261
Cdd:COG4148  152 PRLLLMDEPLAALDLAR-K--AEILPYlerlRDELDIPILyVSHSLDEVARlADHVVLLEQGRVVASGPLAEVLSR 224
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
1054-1262 3.15e-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: 108.66  E-value: 3.15e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    1054 LSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEI----KQLNVQWLRAHLGIVSQEPILF-DCSIAEN 1128
Cdd:TIGR02142   16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLfdsrKGIFLPPEKRRIGYVFQEARLFpHLSVRGN 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    1129 IAYG-----DNSRAVSHEEIVRAAkeaNIHQFIDSLPDKyntrvgdkgtqLSGGQKQRIAIARALVRQPHILLLDEATSA 1203
Cdd:TIGR02142   96 LRYGmkrarPSERRISFERVIELL---GIGHLLGRLPGR-----------LSGGEKQRVAIGRALLSSPRLLLMDEPLAA 161
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6755046    1204 LDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLLAQK 1262
Cdd:TIGR02142  162 LDDPRKYEILPYLERLHAefGIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWASP 223
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
1033-1253 3.24e-25

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: 104.61  E-value: 3.24e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1033 VKFNGVQFNYPTRPnipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWlrAHLG 1112
Cdd:cd03268    1 LKTNDLTKTYGKKR---VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAL--RRIG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1113 IVSQEPILFD-CSIAENIAYGDNSRAVSHEEIVRAAKEANIHQfidslpdkyntRVGDKGTQLSGGQKQRIAIARALVRQ 1191
Cdd:cd03268   76 ALIEAPGFYPnLTARENLRLLARLLGIRKKRIDEVLDVVGLKD-----------SAKKKVKGFSLGMKQRLGIALALLGN 144
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6755046  1192 PHILLLDEATSALDTESEKVVQEAL-DKAREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHG 1253
Cdd:cd03268  145 PDLLILDEPTNGLDPDGIKELRELIlSLRDQGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
ABC_6TM_YknU_like cd18542
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ...
120-336 3.58e-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: 3.58e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   120 IGAGVL--IVAYIQVSLWCLAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDKIGMFFQSIT 197
Cdd:cd18542   46 LGVALLrgVFRYLQGYLAEKASQKVAYDLRNDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVL 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   198 TFLAGFIIGFISGWKLTLVILAVSPLIGLSSALWA-KVLTSFTNKElQAYAKAGAVAEEVLAAIRTVIAFGGQQKELERY 276
Cdd:cd18542  126 LFIGALIIMFSINWKLTLISLAIIPFIALFSYVFFkKVRPAFEEIR-EQEGELNTVLQENLTGVRVVKAFAREDYEIEKF 204
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   277 NKNLEEAKNVGIKKAITASISIGIAYLLVYASYALAFWYGTSLVLSNEYSIGEvLTVFFS 336
Cdd:cd18542  205 DKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVLVLWVGGYLVINGEITLGE-LVAFIS 263
ABC_6TM_bac_exporter_ABCB8_10_like cd18576
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ...
712-997 3.84e-25

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: 106.80  E-value: 3.84e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   712 GVLCAVINGCIQPVFAIVFSRIVGVFSRDDDHEtkrqNCNLFSLFFLVMGLISFVTYFFQGFTFGKAGEILTKRVRYMVF 791
Cdd:cd18576    1 GLILLLLSSAIGLVFPLLAGQLIDAALGGGDTA----SLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLY 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   792 KSMLRQDISWFDDHKnsTGSLTTRLASDASSVKGAMGARLAVVTQNVANLGTGVILSLVYGWQLTLLLVVIIPLIVLGGI 871
Cdd:cd18576   77 RHLQRLPLSFFHERR--VGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAV 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   872 I---EMKLLSGQALkdkKQLEISGKIATEAIENFRTIVSLTREQkFETM-YAQSLQVPYRNAMKKAHVFGITFSFTQAMM 947
Cdd:cd18576  155 LfgrRIRKLSKKVQ---DELAEANTIVEETLQGIRVVKAFTRED-YEIErYRKALERVVKLALKRARIRALFSSFIIFLL 230
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 6755046   948 YFSYAACFRFGAYLVAQQLMTFENvmlVFSAVVFGAMAAGNTSSFAPDYA 997
Cdd:cd18576  231 FGAIVAVLWYGGRLVLAGELTAGD---LVAFLLYTLFIAGSIGSLADLYG 277
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
1047-1253 4.65e-25

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 105.77  E-value: 4.65e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1047 NIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD-----PMAGSVFLDGKEIKQLNVQWLRAHLGIVSQEP-IL 1120
Cdd:PRK14247   15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPnPI 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1121 FDCSIAENIAYG------DNSRAVSHEEIVRAAKEAnihQFIDSLPDKYNTRVGdkgtQLSGGQKQRIAIARALVRQPHI 1194
Cdd:PRK14247   95 PNLSIFENVALGlklnrlVKSKKELQERVRWALEKA---QLWDEVKDRLDAPAG----KLSGGQQQRLCIARALAFQPEV 167
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6755046   1195 LLLDEATSALDTESEKVVQEALDKAREGRTCIVIAH------RLStiqnaDLIVVIENGKVKEHG 1253
Cdd:PRK14247  168 LLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRIS-----DYVAFLYKGQIVEWG 227
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
1049-1262 4.69e-25

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 105.87  E-value: 4.69e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1049 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGIVSQEPIL-FDCSIAE 1127
Cdd:PRK11231   16 RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTpEGITVRE 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1128 NIAYGdNSRAVSH--------EEIVRAAKEANihqFIDSLPDKyntRVgdkgTQLSGGQKQRIAIARALVRQPHILLLDE 1199
Cdd:PRK11231   96 LVAYG-RSPWLSLwgrlsaedNARVNQAMEQT---RINHLADR---RL----TDLSGGQRQRAFLAMVLAQDTPVVLLDE 164
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6755046   1200 ATSALD----TESEKVVQEAldkAREGRTCIVIAHRLS-TIQNADLIVVIENGKVKEHGTHQQLLAQK 1262
Cdd:PRK11231  165 PTTYLDinhqVELMRLMREL---NTQGKTVVTVLHDLNqASRYCDHLVVLANGHVMAQGTPEEVMTPG 229
ABC_6TM_ABCB9_like cd18784
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ...
120-335 4.75e-25

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: 106.63  E-value: 4.75e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   120 IGAGVLIVAYIQVSLWCLAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDKIGMFFQSITTF 199
Cdd:cd18784   45 LAIASSVAAGIRGGLFTLAMARLNIRIRNLLFRSIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKA 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   200 LAGFIIGFISGWKLTLVILAVSPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQKELERYNKN 279
Cdd:cd18784  125 IGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYYKKLSKAVQDSLAKANEVAEETISSIRTVRSFANEDGEANRYSEK 204
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 6755046   280 LEEAKNVGIKKAITASISIGIAYLLVYASYALAFWYGTSLVLSNEYSiGEVLTVFF 335
Cdd:cd18784  205 LKDTYKLKIKEALAYGGYVWSNELTELALTVSTLYYGGHLVITGQIS-GGNLISFI 259
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
406-614 4.82e-25

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 107.74  E-value: 4.82e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    406 VQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTIN---VRYLREIIGVVSQ-------- 474
Cdd:PRK11308   28 VKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADpeaQKLLRQKIQIVFQnpygslnp 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    475 ---------EPVLFATTIAENIRygREDVtMDEIEKAVKEANAYDfimKLPHQFdtlvgergaqlSGGQKQRIAIARALV 545
Cdd:PRK11308  108 rkkvgqileEPLLINTSLSAAER--REKA-LAMMAKVGLRPEHYD---RYPHMF-----------SGGQRQRIAIARALM 170
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6755046    546 RNPKILLLDEATSALDTESEA-VVQAALDKAREGRTTIV-IAHRLSTVRNA--DVIAGFDGGViVEQGNHDEL 614
Cdd:PRK11308  171 LDPDVVVADEPVSALDVSVQAqVLNLMMDLQQELGLSYVfISHDLSVVEHIadEVMVMYLGRC-VEKGTKEQI 242
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
388-614 5.07e-25

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 108.58  E-value: 5.07e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    388 MGNLEFKNVhfnYPSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQdiRTINVRYLRE 467
Cdd:PRK11000    1 MASVTLRNV---TKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEK--RMNDVPPAER 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    468 IIGVVSQEPVLFA-TTIAENIRYGRE--DVTMDEIEKAVKEANAydfIMKLPHqfdtLVGERGAQLSGGQKQRIAIARAL 544
Cdd:PRK11000   76 GVGMVFQSYALYPhLSVAENMSFGLKlaGAKKEEINQRVNQVAE---VLQLAH----LLDRKPKALSGGQRQRVAIGRTL 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6755046    545 VRNPKILLLDEATSALDTESEavVQ-----AALDKaREGRTTIVIAH-RLSTVRNADVIAGFDGGVIVEQGNHDEL 614
Cdd:PRK11000  149 VAEPSVFLLDEPLSNLDAALR--VQmrieiSRLHK-RLGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
391-612 6.37e-25

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 105.10  E-value: 6.37e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    391 LEFKNVHFNYPSRsevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDG------QDIRTINVRY 464
Cdd:PRK11124    3 IQLNGINCFYGAH---QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAIRE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    465 LREIIGVVSQEPVLFA-TTIAENIrygredvtmdeIEKAVK-----EANAYDFIMKLphqFDTLVGERGA-----QLSGG 533
Cdd:PRK11124   80 LRRNVGMVFQQYNLWPhLTVQQNL-----------IEAPCRvlglsKDQALARAEKL---LERLRLKPYAdrfplHLSGG 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    534 QKQRIAIARALVRNPKILLLDEATSALDTESEA-VVQAALDKAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNH 611
Cdd:PRK11124  146 QQQRVAIARALMMEPQVLLFDEPTAALDPEITAqIVSIIRELAETGITQVIVTHEVEVARKtASRVVYMENGHIVEQGDA 225

                  .
gi 6755046    612 D 612
Cdd:PRK11124  226 S 226
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
1033-1262 7.92e-25

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 106.09  E-value: 7.92e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1033 VKFNGVQFNYPTrpNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEI--KQLNVQWLRAH 1110
Cdd:PRK13636    6 LKVEELNYNYSD--GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdySRKGLMKLRES 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1111 LGIVSQEP--ILFDCSIAENIAYGDNSRAVSHEEIVRAAKEANIHQFIDSLPDKyntrvgdKGTQLSGGQKQRIAIARAL 1188
Cdd:PRK13636   84 VGMVFQDPdnQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDK-------PTHCLSFGQKKRVAIAGVL 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6755046   1189 VRQPHILLLDEATSALD----TESEKVVQEALDKAreGRTCIVIAHRLSTIQ-NADLIVVIENGKVKEHGTHQQLLAQK 1262
Cdd:PRK13636  157 VMEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKEL--GLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAEK 233
cbiO PRK13649
energy-coupling factor transporter ATPase;
388-609 8.21e-25

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 105.60  E-value: 8.21e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    388 MGnLEFKNVHFNYPSRS--EVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTI----N 461
Cdd:PRK13649    1 MG-INLQNVSYTYQAGTpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTsknkD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    462 VRYLREIIGVVSQ--EPVLFATTIAENIRYGRED--VTMDEIEKAVKEANAYDFIMklphqfDTLVGERGAQLSGGQKQR 537
Cdd:PRK13649   80 IKQIRKKVGLVFQfpESQLFEETVLKDVAFGPQNfgVSQEEAEALAREKLALVGIS------ESLFEKNPFELSGGQMRR 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6755046    538 IAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIV-IAHRLSTVRN-ADVIAGFDGGVIVEQG 609
Cdd:PRK13649  154 VAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVlVTHLMDDVANyADFVYVLEKGKLVLSG 227
cbiO PRK13644
energy-coupling factor transporter ATPase;
391-617 8.26e-25

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 105.45  E-value: 8.26e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    391 LEFKNVHFNYPSRSEVqiLKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTIN-VRYLREII 469
Cdd:PRK13644    2 IRLENVSYSYPDGTPA--LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    470 GVVSQEP--VLFATTIAENIRYGREDVTMD--EIEKAVKEANAYDFIMKLPHQfdtlvgeRGAQLSGGQKQRIAIARALV 545
Cdd:PRK13644   80 GIVFQNPetQFVGRTVEEDLAFGPENLCLPpiEIRKRVDRALAEIGLEKYRHR-------SPKTLSGGQGQCVALAGILT 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6755046    546 RNPKILLLDEATSALDTES-EAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMRE 617
Cdd:PRK13644  153 MEPECLIFDEVTSMLDPDSgIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSD 225
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
407-563 8.59e-25

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 107.48  E-value: 8.59e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    407 QILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLReiIGVVSQEPVLFA-TTIAE 485
Cdd:PRK10851   16 QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRK--VGFVFQHYALFRhMTVFD 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    486 NIRYG------REDVTMDEIEKAVkeanaydfiMKLPH--QFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEAT 557
Cdd:PRK10851   94 NIAFGltvlprRERPNAAAIKAKV---------TQLLEmvQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPF 164

                  ....*.
gi 6755046    558 SALDTE 563
Cdd:PRK10851  165 GALDAQ 170
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
1049-1253 9.31e-25

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: 103.01  E-value: 9.31e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1049 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL--ERFYDPMAGSVFLDGKEIKQlnvQWLRAHLGIVSQEPILFDC-SI 1125
Cdd:cd03213   23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLDK---RSFRKIIGYVPQDDILHPTlTV 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1126 AENIAYgdnsravsheeivrAAKeanihqfidsLpdkyntrvgdKGtqLSGGQKQRIAIARALVRQPHILLLDEATSALD 1205
Cdd:cd03213  100 RETLMF--------------AAK----------L----------RG--LSGGERKRVSIALELVSNPSLLFLDEPTSGLD 143
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 6755046  1206 TESEKVVQEALDK-AREGRTCIVIAHRLST--IQNADLIVVIENGKVKEHG 1253
Cdd:cd03213  144 SSSALQVMSLLRRlADTGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
1050-1253 1.09e-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: 103.51  E-value: 1.09e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNvqwlRAHLGIVSQEPILF-DCSIAEN 1128
Cdd:cd03269   15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIGYLPEERGLYpKMKVIDQ 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1129 IAYGDNSRAVSHEEIVRAAKEAnIHQFidSLPDKYNTRVgdkgTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTES 1208
Cdd:cd03269   91 LVYLAQLKGLKKEEARRRIDEW-LERL--ELSEYANKRV----EELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVN 163
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 6755046  1209 EKVVQEAL-DKAREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHG 1253
Cdd:cd03269  164 VELLKDVIrELARAGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
404-602 1.14e-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: 103.56  E-value: 1.14e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   404 SEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVV----SIDGQDIRTINVRYLREIIGVVSQEPVLF 479
Cdd:cd03290   12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnKNESEPSFEATRSRNRYSVAYAAQKPWLL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   480 ATTIAENIRYGREdvTMDEIEKAVKEANAYD-FIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATS 558
Cdd:cd03290   92 NATVEENITFGSP--FNKQRYKAVTDACSLQpDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFS 169
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 6755046   559 ALDTE-SEAVVQAALDK--AREGRTTIVIAHRLSTVRNAD-VIAGFDG 602
Cdd:cd03290  170 ALDIHlSDHLMQEGILKflQDDKRTLVLVTHKLQYLPHADwIIAMKDG 217
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
391-611 1.36e-24

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 110.58  E-value: 1.36e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    391 LEFKNVHFNYPSRSE-VQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTIN----VRYL 465
Cdd:PRK10535    5 LELKDIRRSYPSGEEqVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDadalAQLR 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    466 REIIGVVSQEPVLFA-TTIAENIRYgreDVTMDEIEKAVKEANAYDFIMKLphQFDTLVGERGAQLSGGQKQRIAIARAL 544
Cdd:PRK10535   85 REHFGFIFQRYHLLShLTAAQNVEV---PAVYAGLERKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARAL 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6755046    545 VRNPKILLLDEATSALDTESEAVVQAALDKARE-GRTTIVIAHRLSTVRNAD-VIAGFDGGVIVEQGNH 611
Cdd:PRK10535  160 MNGGQVILADEPTGALDSHSGEEVMAILHQLRDrGHTVIIVTHDPQVAAQAErVIEIRDGEIVRNPPAQ 228
TauB COG4525
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
1034-1230 1.45e-24

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


Pssm-ID: 443596 [Multi-domain]  Cd Length: 262  Bit Score: 104.56  E-value: 1.45e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1034 KFNGVQFNYP-TRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNvqwlrAHLG 1112
Cdd:COG4525    5 TVRHVSVRYPgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPG-----ADRG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1113 IVSQEPILFD-CSIAENIAYGDNSRAVSHEEIVRAAKEanihqfidslpdkYNTRVGDKGT------QLSGGQKQRIAIA 1185
Cdd:COG4525   80 VVFQKDALLPwLNVLDNVAFGLRLRGVPKAERRARAEE-------------LLALVGLADFarrriwQLSGGMRQRVGIA 146
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 6755046  1186 RALVRQPHILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAH 1230
Cdd:COG4525  147 RALAADPRFLLMDEPFGALDALTREQMQELLLDvwQRTGKGVFLITH 193
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
1050-1259 1.89e-24

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 103.97  E-value: 1.89e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERF---YDP---MAGSVFLDGKEIKQLNVQWLRAHLGIVSQEPILF-D 1122
Cdd:PRK14246   25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiYDSkikVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNPFpH 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1123 CSIAENIAYGDNSRAVSHEEIVRAAKEANIHQFidSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATS 1202
Cdd:PRK14246  105 LSIYDNIAYPLKSHGIKEKREIKKIVEECLRKV--GLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 6755046   1203 ALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLL 1259
Cdd:PRK14246  183 MIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIF 240
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
1051-1261 2.38e-24

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 105.43  E-value: 2.38e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1051 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLN---VQWLRAHLGIVSQEPilfdcsiae 1127
Cdd:PRK11308   31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADpeaQKLLRQKIQIVFQNP--------- 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1128 niaYGD-NSRA----------VSHEEIVRAAKEANIHQFIdslpdkynTRVGDKGTQ-------LSGGQKQRIAIARALV 1189
Cdd:PRK11308  102 ---YGSlNPRKkvgqileeplLINTSLSAAERREKALAMM--------AKVGLRPEHydryphmFSGGQRQRIAIARALM 170
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6755046   1190 RQPHILLLDEATSALDTESE-KVVQEALDKAREGRTCIV-IAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLLAQ 1261
Cdd:PRK11308  171 LDPDVVVADEPVSALDVSVQaQVLNLMMDLQQELGLSYVfISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIFNN 245
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
1048-1267 3.64e-24

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 106.07  E-value: 3.64e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1048 IPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQlnVQWLRAHLGIVSQEPILF-DCSIA 1126
Cdd:PRK11607   32 QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSH--VPPYQRPINMMFQSYALFpHMTVE 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1127 ENIAYGDNSRAVSHEEIVRAAKE----ANIHQFIDSLPDkyntrvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEATS 1202
Cdd:PRK11607  110 QNIAFGLKQDKLPKAEIASRVNEmlglVHMQEFAKRKPH-----------QLSGGQRQRVALARSLAKRPKLLLLDEPMG 178
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6755046   1203 ALDTESEKVVQ-EALD-KAREGRTCIVIAH-RLSTIQNADLIVVIENGKVKEHGTHQQLLAQKGIYFS 1267
Cdd:PRK11607  179 ALDKKLRDRMQlEVVDiLERVGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYS 246
cbiO PRK13641
energy-coupling factor transporter ATPase;
391-609 3.97e-24

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 104.14  E-value: 3.97e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    391 LEFKNVHFNYPSRS--EVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIR----TINVRY 464
Cdd:PRK13641    3 IKFENVDYIYSPGTpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    465 LREIIGVVSQ--EPVLFATTIAENIRYGREDVTMDEiEKAVKEANAYDFIMKLPhqfDTLVGERGAQLSGGQKQRIAIAR 542
Cdd:PRK13641   83 LRKKVSLVFQfpEAQLFENTVLKDVEFGPKNFGFSE-DEAKEKALKWLKKVGLS---EDLISKSPFELSGGQMRRVAIAG 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6755046    543 ALVRNPKILLLDEATSALDTES-EAVVQAALDKAREGRTTIVIAHrlstvrNADVIAGFDGGVIV-EQG 609
Cdd:PRK13641  159 VMAYEPEILCLDEPAAGLDPEGrKEMMQLFKDYQKAGHTVILVTH------NMDDVAEYADDVLVlEHG 221
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
398-621 4.08e-24

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 104.93  E-value: 4.08e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    398 FNYPSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSID----GQDIRTI------------N 461
Cdd:PRK13631   31 FDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyiGDKKNNHelitnpyskkikN 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    462 VRYLREIIGVVSQEP--VLFATTIAENIRYGREDVTMDEIEkAVKEANAYDFIMKLPHQFDtlvgERGA-QLSGGQKQRI 538
Cdd:PRK13631  111 FKELRRRVSMVFQFPeyQLFKDTIEKDIMFGPVALGVKKSE-AKKLAKFYLNKMGLDDSYL----ERSPfGLSGGQKRRV 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    539 AIARALVRNPKILLLDEATSALDTESEA-VVQAALDKAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDELMR 616
Cdd:PRK13631  186 AIAGILAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVLEvADEVIVMDKGKILKTGTPYEIFT 265

                  ....*
gi 6755046    617 EKGIY 621
Cdd:PRK13631  266 DQHII 270
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
389-587 4.32e-24

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 108.36  E-value: 4.32e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   389 GNLEFKNVHFNYPSRSEvqILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSI-DGQDIrtinvryLre 467
Cdd:COG4178  361 GALALEDLTLRTPDGRP--LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARV-------L-- 429
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   468 iigVVSQEPVLFATTIAENIRY--GREDVTMDEIEKAVKEANaydfimkLPH---QFDTlVGERGAQLSGGQKQRIAIAR 542
Cdd:COG4178  430 ---FLPQRPYLPLGTLREALLYpaTAEAFSDAELREALEAVG-------LGHlaeRLDE-EADWDQVLSLGEQQRLAFAR 498
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 6755046   543 ALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHR 587
Cdd:COG4178  499 LLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR 543
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
391-561 4.36e-24

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 102.10  E-value: 4.36e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    391 LEFKNVHFNYPSRsevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIG 470
Cdd:PRK10247    8 LQLQNVGYLAGDA---KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVS 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    471 VVSQEPVLFATTIAENIRYGRedvtmdEIEKAVKEANAY-DFIMK--LPhqfDTLVGERGAQLSGGQKQRIAIARALVRN 547
Cdd:PRK10247   85 YCAQTPTLFGDTVYDNLIFPW------QIRNQQPDPAIFlDDLERfaLP---DTILTKNIAELSGGEKQRISLIRNLQFM 155
                         170
                  ....*....|....
gi 6755046    548 PKILLLDEATSALD 561
Cdd:PRK10247  156 PKVLLLDEITSALD 169
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
388-561 4.36e-24

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


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 105.31  E-value: 4.36e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    388 MGNLEFKNVHFNYPSRseVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRyLRE 467
Cdd:PRK11650    1 MAGLKLQAVRKSYDGK--TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPA-DRD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    468 IiGVVSQEPVLFA-TTIAENIRYGREDVTM--DEIEKAVKEANAydfIMKLphqfDTLVGERGAQLSGGQKQRIAIARAL 544
Cdd:PRK11650   78 I-AMVFQNYALYPhMSVRENMAYGLKIRGMpkAEIEERVAEAAR---ILEL----EPLLDRKPRELSGGQRQRVAMGRAI 149
                         170
                  ....*....|....*..
gi 6755046    545 VRNPKILLLDEATSALD 561
Cdd:PRK11650  150 VREPAVFLFDEPLSNLD 166
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
401-609 4.88e-24

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: 101.68  E-value: 4.88e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   401 PSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTiNVRYLREIIGVVSQEPVLFA 480
Cdd:cd03266   13 DVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRLGFVSDSTGLYD 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   481 -TTIAENIRY--GREDVTMDEIEKAVKEanaydFIMKLphQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEAT 557
Cdd:cd03266   92 rLTARENLEYfaGLYGLKGDELTARLEE-----LADRL--GMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPT 164
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 6755046   558 SALDTESEAVVQAALDKAREGRTTIVIA-HRLSTV-RNADVIAGFDGGVIVEQG 609
Cdd:cd03266  165 TGLDVMATRALREFIRQLRALGKCILFStHIMQEVeRLCDRVVVLHRGRVVYEG 218
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
1040-1265 4.97e-24

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 104.55  E-value: 4.97e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1040 FNYPTRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQ----LL---------ERFY-----DPMAGSVFLDGKEIKq 1101
Cdd:PRK13631   31 FDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVThfngLIkskygtiqvGDIYigdkkNNHELITNPYSKKIK- 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1102 lNVQWLRAHLGIVSQEP--ILFDCSIAENIAYGDNSRAVSHEEivrAAKEANIHQFIDSLPDKYNTRvgdKGTQLSGGQK 1179
Cdd:PRK13631  110 -NFKELRRRVSMVFQFPeyQLFKDTIEKDIMFGPVALGVKKSE---AKKLAKFYLNKMGLDDSYLER---SPFGLSGGQK 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1180 QRIAIARALVRQPHILLLDEATSALDTESEK-VVQEALDKAREGRTCIVIAHRLSTI-QNADLIVVIENGKVKEHGTHQQ 1257
Cdd:PRK13631  183 RRVAIAGILAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVlEVADEVIVMDKGKILKTGTPYE 262

                  ....*...
gi 6755046   1258 LLAQKGIY 1265
Cdd:PRK13631  263 IFTDQHII 270
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
412-609 7.01e-24

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: 101.03  E-value: 7.01e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   412 LNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRylREIIGVVSQEPVLFA-TTIAENIRYG 490
Cdd:cd03298   17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVSMLFQENNLFAhLTVEQNVGLG 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   491 R------EDVTMDEIEKAVKEANAYDFIMKLPhqfdtlvgergAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTES 564
Cdd:cd03298   95 LspglklTAEDRQAIEVALARVGLAGLEKRLP-----------GELSGGERQRVALARVLVRDKPVLLLDEPFAALDPAL 163
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 6755046   565 EAVVQAALDK--AREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQG 609
Cdd:cd03298  164 RAEMLDLVLDlhAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
PTZ00243 PTZ00243
ABC transporter; Provisional
389-625 7.80e-24

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 109.48  E-value: 7.80e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    389 GNLEFKNVHFNYpsRSEVQ-ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLRE 467
Cdd:PTZ00243 1307 GSLVFEGVQMRY--REGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRR 1384
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    468 IIGVVSQEPVLFATTIAENIRYGREdVTMDEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALV-R 546
Cdd:PTZ00243 1385 QFSMIPQDPVLFDGTVRQNVDPFLE-ASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLkK 1463
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    547 NPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDEL-MREKGIYFKLV 625
Cdd:PTZ00243 1464 GSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELvMNRQSIFHSMV 1543
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
1043-1253 9.65e-24

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: 9.65e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1043 PTRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQlNVQWLRAHLGIVSQEPILFD 1122
Cdd:cd03266   13 DVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRLGFVSDSTGLYD 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1123 -CSIAENIAY-GDnsravsheeiVRAAKEANIHQFIDSLPDKY------NTRVGDkgtqLSGGQKQRIAIARALVRQPHI 1194
Cdd:cd03266   92 rLTARENLEYfAG----------LYGLKGDELTARLEELADRLgmeellDRRVGG----FSTGMRQKVAIARALVHDPPV 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6755046  1195 LLLDEATSALDTESEKVVQEALDKAREGRTCIVIA-HRLSTIQN-ADLIVVIENGKVKEHG 1253
Cdd:cd03266  158 LLLDEPTTGLDVMATRALREFIRQLRALGKCILFStHIMQEVERlCDRVVVLHRGRVVYEG 218
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
1055-1262 9.95e-24

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 101.20  E-value: 9.95e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1055 SLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEikQLNVQWLRAHLGIVSQEPILFD-CSIAENIAYGD 1133
Cdd:PRK10771   19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD--HTTTPPSRRPVSMLFQENNLFShLTVAQNIGLGL 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1134 NS----RAVSHEEIVRAAKEANIHQFIDSLPdkyntrvgdkgTQLSGGQKQRIAIARALVRQPHILLLDEATSALD---- 1205
Cdd:PRK10771   97 NPglklNAAQREKLHAIARQMGIEDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEPFSALDpalr 165
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 6755046   1206 TESEKVVQEALDkaREGRTCIVIAHRLS-TIQNADLIVVIENGKVKEHGTHQQLLAQK 1262
Cdd:PRK10771  166 QEMLTLVSQVCQ--ERQLTLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDELLSGK 221
cbiO PRK13643
energy-coupling factor transporter ATPase;
1033-1254 1.01e-23

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 102.89  E-value: 1.01e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1033 VKFNGVqfNYPTRPNIP----VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEI----KQLNV 1104
Cdd:PRK13643    2 IKFEKV--NYTYQPNSPfasrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVsstsKQKEI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1105 QWLRAHLGIVSQEP--ILFDCSIAENIAYGDNSRAVSHEEIVRAAKE-----ANIHQFIDSLPdkyntrvgdkgTQLSGG 1177
Cdd:PRK13643   80 KPVRKKVGVVFQFPesQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEklemvGLADEFWEKSP-----------FELSGG 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6755046   1178 QKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGT 1254
Cdd:PRK13643  149 QMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGT 227
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
405-609 1.11e-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: 100.37  E-value: 1.11e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   405 EVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDI-RTINVRylrEIIGVVSQEPVLFAT-T 482
Cdd:cd03268   12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYqKNIEAL---RRIGALIEAPGFYPNlT 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   483 IAENIR-----YGREDVTMDEIEKAVKEANAYDfimklphqfdtlvgERGAQLSGGQKQRIAIARALVRNPKILLLDEAT 557
Cdd:cd03268   89 ARENLRllarlLGIRKKRIDEVLDVVGLKDSAK--------------KKVKGFSLGMKQRLGIALALLGNPDLLILDEPT 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 6755046   558 SALDTESEAVVQAAL-DKAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQG 609
Cdd:cd03268  155 NGLDPDGIKELRELIlSLRDQGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
urea_trans_UrtE TIGR03410
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ...
391-618 1.40e-23

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: 100.68  E-value: 1.40e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     391 LEFKNVHFNYpsrSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDI-RTINVRYLREII 469
Cdd:TIGR03410    1 LEVSNLNVYY---GQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDItKLPPHERARAGI 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     470 GVVSQEPVLFAT-TIAENIRYGREdvTMDEIEKAVKeanayDFIMKL-PHQFDTLvGERGAQLSGGQKQRIAIARALVRN 547
Cdd:TIGR03410   78 AYVPQGREIFPRlTVEENLLTGLA--ALPRRSRKIP-----DEIYELfPVLKEML-GRRGGDLSGGQQQQLAIARALVTR 149
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6755046     548 PKILLLDEATSALDTESEAVVQAALDK--AREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDELMREK 618
Cdd:TIGR03410  150 PKLLLLDEPTEGIQPSIIKDIGRVIRRlrAEGGMAILLVEQYLDFARElADRYYVMERGRVVASGAGDELDEDK 223
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
706-1262 1.42e-23

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: 108.84  E-value: 1.42e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     706 WPYLLVGVLCAV--INGCIQPvfaIVFSRIVGVFsrDDDHETKRQNCnlfslFFLVMGL-ISFV--TYFFQGFTFGKAGE 780
Cdd:TIGR01271   80 WRFVFYGILLYFgeATKAVQP---LLLGRIIASY--DPFNAPEREIA-----YYLALGLcLLFIvrTLLLHPAIFGLHHL 149
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     781 ILTKRVRY--MVFKSMLRQDISWFDdhKNSTGSLTTRLASDASSVKGAMG-ARLAVVTQNVANLGTGVILSLVYGWQLTL 857
Cdd:TIGR01271  150 GMQMRIALfsLIYKKTLKLSSRVLD--KISTGQLVSLLSNNLNKFDEGLAlAHFVWIAPLQVILLMGLIWELLEVNGFCG 227
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     858 LLVVIIPLIVLGGIIEMKLlsgqALKDKKQLEISGKIA--TEAIENFRTIVSLTREQKFETMYAQSLQVPYRNAMKKAHV 935
Cdd:TIGR01271  228 LGFLILLALFQACLGQKMM----PYRDKRAGKISERLAitSEIIENIQSVKAYCWEEAMEKIIKNIRQDELKLTRKIAYL 303
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     936 fgitfsftqamMYFSYAACFrFGAYLVaqqlmtfenvmlVFSAVVFGAMAAG-------NTSSFA-----------PDYA 997
Cdd:TIGR01271  304 -----------RYFYSSAFF-FSGFFV------------VFLSVVPYALIKGiilrrifTTISYCivlrmtvtrqfPGAI 359
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     998 KAKVSASHIIRIIEKTPEIDSYSTEGLKPTLLE---GNVK----------FNGVQFNYPTR--PN--------------I 1048
Cdd:TIGR01271  360 QTWYDSLGAITKIQDFLCKEEYKTLEYNLTTTEvemVNVTaswdegigelFEKIKQNNKARkqPNgddglffsnfslyvT 439
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    1049 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKeikqlnvqwlrahLGIVSQEPILFDCSIAEN 1128
Cdd:TIGR01271  440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQTSWIMPGTIKDN 506
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    1129 IAYGDNSRAVSHEEIVRAAKeanIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTES 1208
Cdd:TIGR01271  507 IIFGLSYDEYRYTSVIKACQ---LEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVT 583
                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 6755046    1209 EKVVQEA-LDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQK 1262
Cdd:TIGR01271  584 EKEIFEScLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKR 638
ABC_6TM_TmrB_like cd18541
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ...
100-361 1.47e-23

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: 102.49  E-value: 1.47e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   100 IISNSSLEEEMAIYAYYYTGIGAGVLIVAYIQVSLWcLAAGRQI-HKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDV 178
Cdd:cd18541   29 LTAGTLTASQLLRYALLILLLALLIGIFRFLWRYLI-FGASRRIeYDLRNDLFAHLLTLSPSFYQKNRTGDLMARATNDL 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   179 SKINDGIGDKIGMFFQSITTFLAGFIIGFISGWKLTLVILAVSPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLA 258
Cdd:cd18541  108 NAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLVYRLGKKIHKRFRKVQEAFSDLSDRVQESFS 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   259 AIRTVIAFGGQQKELERYNKNLEEAKNVGIKKAITASISIGIAYLLVYASYALAFWYGTSLVLSNEYSIGEVLTvfFSIL 338
Cdd:cd18541  188 GIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLSFLIVLWYGGRLVIRGTITLGDLVA--FNSY 265
                        250       260
                 ....*....|....*....|....*...
gi 6755046   339 LG-----TFSIGHLAPNIEafanaRGAA 361
Cdd:cd18541  266 LGmliwpMMALGWVINLIQ-----RGAA 288
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
391-609 1.73e-23

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 101.07  E-value: 1.73e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    391 LEFKNVHFNYPSRsevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYD-----PLEGVVSIDGQDIRTINVR-- 463
Cdd:PRK14267    5 IETVNLRVYYGSN---HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSPDVDpi 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    464 YLREIIGVVSQEPVLFA-TTIAENIRYG-------REDVTMDE-IEKAVKEANAYDfimklphQFDTLVGERGAQLSGGQ 534
Cdd:PRK14267   82 EVRREVGMVFQYPNPFPhLTIYDNVAIGvklnglvKSKKELDErVEWALKKAALWD-------EVKDRLNDYPSNLSGGQ 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6755046    535 KQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHR-LSTVRNADVIAGFDGGVIVEQG 609
Cdd:PRK14267  155 RQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVG 230
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
408-618 2.49e-23

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 100.86  E-value: 2.49e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    408 ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIGVVSQEPVL-FATTIAEN 486
Cdd:PRK11231   17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTpEGITVREL 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    487 IRYGR------------EDVTMdeIEKAVKEAnaydfimklphQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLD 554
Cdd:PRK11231   97 VAYGRspwlslwgrlsaEDNAR--VNQAMEQT-----------RINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLD 163
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6755046    555 EATSALDTESEAVVQAALDKAR-EGRTTIVIAHRLSTV-RNADVIAGFDGGVIVEQGNHDELMREK 618
Cdd:PRK11231  164 EPTTYLDINHQVELMRLMRELNtQGKTVVTVLHDLNQAsRYCDHLVVLANGHVMAQGTPEEVMTPG 229
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
1050-1258 2.51e-23

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 103.24  E-value: 2.51e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQwlRAHLGIVSQEPILF-DCSIAEN 1128
Cdd:PRK10851   17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHAR--DRKVGFVFQHYALFrHMTVFDN 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1129 IAYGdNSRAVSHEEIVRAAKEANIHQFID-----SLPDKYNTrvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEATSA 1203
Cdd:PRK10851   95 IAFG-LTVLPRRERPNAAAIKAKVTQLLEmvqlaHLADRYPA-------QLSGGQKQRVALARALAVEPQILLLDEPFGA 166
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 6755046   1204 LDTESEKVVQEALDKARE--GRTCIVIAH-RLSTIQNADLIVVIENGKVKEHGTHQQL 1258
Cdd:PRK10851  167 LDAQVRKELRRWLRQLHEelKFTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
1050-1256 2.59e-23

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 100.47  E-value: 2.59e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDP------MAGSVFLDGKEIKQLNVQWLRAHLGIVSQE----PI 1119
Cdd:PRK11124   17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPrsgtlnIAGNHFDFSKTPSDKAIRELRRNVGMVFQQynlwPH 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1120 LfdcSIAEN-IAYGDNSRAVSHEEIVRAAKEA----NIHQFIDSLPdkyntrvgdkgTQLSGGQKQRIAIARALVRQPHI 1194
Cdd:PRK11124   97 L---TVQQNlIEAPCRVLGLSKDQALARAEKLlerlRLKPYADRFP-----------LHLSGGQQQRVAIARALMMEPQV 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6755046   1195 LLLDEATSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQ 1256
Cdd:PRK11124  163 LLFDEPTAALDPEiTAQIVSIIRELAETGITQVIVTHEVEVARKtASRVVYMENGHIVEQGDAS 226
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
423-564 2.94e-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: 102.87  E-value: 2.94e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   423 ALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDG---QDIRT-INV-RYLREIiGVVSQEPVLFAT-TIAENIRYGRedvtm 496
Cdd:COG4148   29 ALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlQDSARgIFLpPHRRRI-GYVFQEARLFPHlSVRGNLLYGR----- 102
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6755046   497 deieKAVKEANAYDfimklphQFDTLVG--------ERG-AQLSGGQKQRIAIARALVRNPKILLLDEATSALDTES 564
Cdd:COG4148  103 ----KRAPRAERRI-------SFDEVVEllgighllDRRpATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLAR 168
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
391-618 3.17e-23

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 101.25  E-value: 3.17e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    391 LEFKNVHFNYPSRS--EVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDI----RTINVRY 464
Cdd:PRK13634    3 ITFQKVEHRYQYKTpfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkKNKKLKP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    465 LREIIGVVSQ--EPVLFATTIAENIRYGREDVTMDEiEKAVKEANAYDFIMKLPHQ------FDtlvgergaqLSGGQKQ 536
Cdd:PRK13634   83 LRKKVGIVFQfpEHQLFEETVEKDICFGPMNFGVSE-EDAKQKAREMIELVGLPEEllarspFE---------LSGGQMR 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    537 RIAIARALVRNPKILLLDEATSALDTESEAVVQ---AALDKaREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHD 612
Cdd:PRK13634  153 RVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMemfYKLHK-EKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPR 231

                  ....*.
gi 6755046    613 ELMREK 618
Cdd:PRK13634  232 EIFADP 237
urea_trans_UrtE TIGR03410
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ...
1050-1254 3.25e-23

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: 99.52  E-value: 3.25e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWlRAHLGI--VSQEPILF-DCSIA 1126
Cdd:TIGR03410   15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHE-RARAGIayVPQGREIFpRLTVE 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    1127 ENIAYGDNSRAVSHEEIVraakeANIHQFIDSLPDKYNTRVGDkgtqLSGGQKQRIAIARALVRQPHILLLDEATSALDT 1206
Cdd:TIGR03410   94 ENLLTGLAALPRRSRKIP-----DEIYELFPVLKEMLGRRGGD----LSGGQQQQLAIARALVTRPKLLLLDEPTEGIQP 164
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 6755046    1207 ESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVIENGKVKEHGT 1254
Cdd:TIGR03410  165 SIIKDIGRVIRRlrAEGGMAILLVEQYLDfARELADRYYVMERGRVVASGA 215
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
412-618 3.34e-23

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: 102.88  E-value: 3.34e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     412 LNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDG---QDIRT-INVRYLREIIGVVSQEPVLFA-TTIAEN 486
Cdd:TIGR02142   16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlFDSRKgIFLPPEKRRIGYVFQEARLFPhLSVRGN 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     487 IRYGREDVTMDEieKAVKEANAYDfIMKLPHqfdtLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEA 566
Cdd:TIGR02142   96 LRYGMKRARPSE--RRISFERVIE-LLGIGH----LLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKY 168
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 6755046     567 VVQAALDK-AREGRTTIV-IAHRLSTV-RNADVIAGFDGGVIVEQGNHDELMREK 618
Cdd:TIGR02142  169 EILPYLERlHAEFGIPILyVSHSLQEVlRLADRVVVLEDGRVAAAGPIAEVWASP 223
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
1044-1251 3.52e-23

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 100.53  E-value: 3.52e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1044 TRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLN----------VQWL------ 1107
Cdd:PRK10419   21 KHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqrkafrrdIQMVfqdsis 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1108 ----RAHLGIVSQEPI--LFDCSIAEniaygdnsRAVSHEEIVRAAKEANIHqfIDSLPdkyntrvgdkgTQLSGGQKQR 1181
Cdd:PRK10419  101 avnpRKTVREIIREPLrhLLSLDKAE--------RLARASEMLRAVDLDDSV--LDKRP-----------PQLSGGQLQR 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6755046   1182 IAIARALVRQPHILLLDEATSALDteseKVVQ-EALD-----KAREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKE 1251
Cdd:PRK10419  160 VCLARALAVEPKLLILDEAVSNLD----LVLQaGVIRllkklQQQFGTACLFITHDLRLVERfCQRVMVMDNGQIVE 232
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
1048-1247 3.79e-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: 99.43  E-value: 3.79e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1048 IPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEikqlnvQW-------------LRAH-LGI 1113
Cdd:COG4778   24 LPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDG------GWvdlaqaspreilaLRRRtIGY 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1114 VSQ---------------EPILfdcsiaeniaygdnSRAVSHEEIVRAAKEA----NIHQFIDSLPDkyNTrvgdkgtqL 1174
Cdd:COG4778   98 VSQflrviprvsaldvvaEPLL--------------ERGVDREEARARARELlarlNLPERLWDLPP--AT--------F 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6755046  1175 SGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIV-IAHRLSTIQN-ADLIVVIENG 1247
Cdd:COG4778  154 SGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIgIFHDEEVREAvADRVVDVTPF 228
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
391-588 3.91e-23

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


Pssm-ID: 440718 [Multi-domain]  Cd Length: 264  Bit Score: 100.55  E-value: 3.91e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   391 LEFKNVH--FNYPSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVrYLR-E 467
Cdd:COG1101    2 LELKNLSktFNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPE-YKRaK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   468 IIGVVSQEPVL---FATTIAEN------------IRYGREDVTMDEIEKAVKEANaydfiMKLPHQFDTLVGergaQLSG 532
Cdd:COG1101   81 YIGRVFQDPMMgtaPSMTIEENlalayrrgkrrgLRRGLTKKRRELFRELLATLG-----LGLENRLDTKVG----LLSG 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 6755046   533 GQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDK--AREGRTTIVIAHRL 588
Cdd:COG1101  152 GQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKivEENNLTTLMVTHNM 209
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
1032-1255 4.02e-23

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


Pssm-ID: 443326 [Multi-domain]  Cd Length: 242  Bit Score: 99.70  E-value: 4.02e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1032 NVKFNGVQFNYPTRPnipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDG------KEIKQLNVQ 1105
Cdd:COG4161    2 SIQLKNINCFYGSHQ---ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1106 WLRAHLGIVSQE----PILfdcSIAENIAYG-----DNSRAVSHEEIVRAAKEANIHQFIDSLPdkyntrvgdkgTQLSG 1176
Cdd:COG4161   79 LLRQKVGMVFQQynlwPHL---TVMENLIEApckvlGLSKEQAREKAMKLLARLRLTDKADRFP-----------LHLSG 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1177 GQKQRIAIARALVRQPHILLLDEATSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGT 1254
Cdd:COG4161  145 GQQQRVAIARALMMEPQVLLFDEPTAALDPEiTAQVVEIIRELSQTGITQVIVTHEVEFARKvASQVVYMEKGRIIEQGD 224

                 .
gi 6755046  1255 H 1255
Cdd:COG4161  225 A 225
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
1046-1230 4.20e-23

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 100.16  E-value: 4.20e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1046 PNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNvqwlrAHLGIVSQ-EPILFDCS 1124
Cdd:PRK11248   12 GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG-----AERGVVFQnEGLLPWRN 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1125 IAENIAYGDNSRAVSheeivRAAKEANIHQFIdslpdkynTRVGDKGT------QLSGGQKQRIAIARALVRQPHILLLD 1198
Cdd:PRK11248   87 VQDNVAFGLQLAGVE-----KMQRLEIAHQML--------KKVGLEGAekryiwQLSGGQRQRVGIARALAANPQLLLLD 153
                         170       180       190
                  ....*....|....*....|....*....|....
gi 6755046   1199 EATSALDTESEKVVQEALDK--AREGRTCIVIAH 1230
Cdd:PRK11248  154 EPFGALDAFTREQMQTLLLKlwQETGKQVLLITH 187
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
409-615 4.76e-23

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


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 103.19  E-value: 4.76e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    409 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREI----IGVVSQEPVLFA-TTI 483
Cdd:PRK10070   44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVrrkkIAMVFQSFALMPhMTV 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    484 AENIRYGREdvtMDEIEKAVKEANAYDFIMKLphQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTE 563
Cdd:PRK10070  124 LDNTAFGME---LAGINAEERREKALDALRQV--GLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 6755046    564 SEAVVQAALDK--AREGRTTIVIAHRL-STVRNADVIAGFDGGVIVEQGNHDELM 615
Cdd:PRK10070  199 IRTEMQDELVKlqAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
393-618 4.84e-23

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 104.76  E-value: 4.84e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   393 FKNVHFNYPSRsevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGqdirtiNVRylreiIGVV 472
Cdd:COG0488    1 LENLSKSFGGR---PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK------GLR-----IGYL 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   473 SQEPVLFAT-TIAENIRYGREDVT-----MDEIEKAVK-----------------EANAYDF-------IMKL---PHQF 519
Cdd:COG0488   67 PQEPPLDDDlTVLDTVLDGDAELRaleaeLEELEAKLAepdedlerlaelqeefeALGGWEAearaeeiLSGLgfpEEDL 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   520 DTLVGErgaqLSGGQKQRIAIARALVRNPKILLLDEATSALDTES----EAVVqaaldKAREGrTTIVIAH-R--LSTVr 592
Cdd:COG0488  147 DRPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESiewlEEFL-----KNYPG-TVLVVSHdRyfLDRV- 215
                        250       260
                 ....*....|....*....|....*..
gi 6755046   593 nADVIAGFDGGVIVE-QGNHDELMREK 618
Cdd:COG0488  216 -ATRILELDRGKLTLyPGNYSAYLEQR 241
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
1032-1205 6.08e-23

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


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 102.23  E-value: 6.08e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1032 NVKFNGVQFNYPTrpNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQL---LERFydpMAGSVFLDGKEIKQLnvqwlr 1108
Cdd:PRK11650    3 GLKLQAVRKSYDG--KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMvagLERI---TSGEIWIGGRVVNEL------ 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1109 ahlgivsqEPILFDC-------------SIAENIAYGDNSRAVSHEEIVR----AAKEANIHQFIDSLPdkyntrvgdkg 1171
Cdd:PRK11650   72 --------EPADRDIamvfqnyalyphmSVRENMAYGLKIRGMPKAEIEErvaeAARILELEPLLDRKP----------- 132
                         170       180       190
                  ....*....|....*....|....*....|....
gi 6755046   1172 TQLSGGQKQRIAIARALVRQPHILLLDEATSALD 1205
Cdd:PRK11650  133 RELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
SufC COG0396
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ...
1049-1254 6.25e-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: 6.25e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1049 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL---ERfYDPMAGSVFLDGKEIKQLNVQwLRAHLGI-VS-QEPI---- 1119
Cdd:COG0396   14 EILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmghPK-YEVTSGSILLDGEDILELSPD-ERARAGIfLAfQYPVeipg 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1120 ------LfdcSIAENIAYGDNSRAV-SHEEIVRAAKEANihqfidsLPDKYNTR---VGdkgtqLSGGQKQRIAIARALV 1189
Cdd:COG0396   92 vsvsnfL---RTALNARRGEELSAReFLKLLKEKMKELG-------LDEDFLDRyvnEG-----FSGGEKKRNEILQMLL 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6755046  1190 RQPHILLLDEATSALDTESEKVVQEALDKAR-EGRTCIVIAH--RLSTIQNADLIVVIENGKVKEHGT 1254
Cdd:COG0396  157 LEPKLAILDETDSGLDIDALRIVAEGVNKLRsPDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGG 224
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
405-586 6.48e-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: 6.48e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   405 EVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQ----DI-----RTI-NVRylREIIGVVSQ 474
Cdd:COG4778   23 RLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLaqaspREIlALR--RRTIGYVSQ 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   475 epvlFATTIAeniRYGREDVTMDE-IEKAVKEANAYDFIMKLPHQFDtlVGERGAQL-----SGGQKQRIAIARALVRNP 548
Cdd:COG4778  101 ----FLRVIP---RVSALDVVAEPlLERGVDREEARARARELLARLN--LPERLWDLppatfSGGEQQRVNIARGFIADP 171
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 6755046   549 KILLLDEATSALDTESEAVVQAALDKAREGRTTIV-IAH 586
Cdd:COG4778  172 PLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIgIFH 210
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
409-614 8.73e-23

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: 98.21  E-value: 8.73e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   409 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTiNVRYLREIIGVVSQEPvlfattIAENIR 488
Cdd:cd03265   16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDL------SVDDEL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   489 YGREDVTM---------DEIEKAVKEANAYdfiMKLPHQFDTLVGergaQLSGGQKQRIAIARALVRNPKILLLDEATSA 559
Cdd:cd03265   89 TGWENLYIharlygvpgAERRERIDELLDF---VGLLEAADRLVK----TYSGGMRRRLEIARSLVHRPEVLFLDEPTIG 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 6755046   560 LDTESEAVVQAALDK--AREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDEL 614
Cdd:cd03265  162 LDPQTRAHVWEYIEKlkEEFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
1051-1249 8.73e-23

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 103.95  E-value: 8.73e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1051 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLN-VQWLRAHLGIVSQEPILFDC-SIAEN 1128
Cdd:COG3845   21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSpRDAIALGIGMVHQHFMLVPNlTVAEN 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1129 IAYGDNSRAVSHEEIVRAAKEanihqfIDSLPDKY------NTRVGDkgtqLSGGQKQRIAIARALVRQPHILLLDEATS 1202
Cdd:COG3845  101 IVLGLEPTKGGRLDRKAARAR------IRELSERYgldvdpDAKVED----LSVGEQQRVEILKALYRGARILILDEPTA 170
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 6755046  1203 AL-DTESEKVVqEALDK-AREGRTCIVIAHRLSTI-QNADLIVVIENGKV 1249
Cdd:COG3845  171 VLtPQEADELF-EILRRlAAEGKSIIFITHKLREVmAIADRVTVLRRGKV 219
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
408-614 1.06e-22

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 98.97  E-value: 1.06e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    408 ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQ------DIRTINVRYLREIIGVVSQEPVLFA- 480
Cdd:PRK14246   25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQPNPFPh 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    481 TTIAENIRYGREDVTMD---EIEKAVKEANAYDFIMKLPHqfDTLvGERGAQLSGGQKQRIAIARALVRNPKILLLDEAT 557
Cdd:PRK14246  105 LSIYDNIAYPLKSHGIKekrEIKKIVEECLRKVGLWKEVY--DRL-NSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 6755046    558 SALDTESEAVVQAALDKAREGRTTIVIAHRLSTV-RNADVIAGFDGGVIVEQGNHDEL 614
Cdd:PRK14246  182 SMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEI 239
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
1050-1253 1.18e-22

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 98.76  E-value: 1.18e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD-----PMAGSVFLDGKEIKQLNVQWL--RAHLGIVSQEPILF- 1121
Cdd:PRK14267   19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSPDVDPIevRREVGMVFQYPNPFp 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1122 DCSIAENIAYGD--NSRAVSHEEI---VR-AAKEAnihqfidSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHIL 1195
Cdd:PRK14267   99 HLTIYDNVAIGVklNGLVKSKKELderVEwALKKA-------ALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKIL 171
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6755046   1196 LLDEATSALDTESEKVVQEALDKAREGRTCIVIAHrlSTIQNA---DLIVVIENGKVKEHG 1253
Cdd:PRK14267  172 LMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTH--SPAQAArvsDYVAFLYLGKLIEVG 230
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
409-586 1.19e-22

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: 97.92  E-value: 1.19e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     409 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLreiigVVSQEPVLFA-TTIAENI 487
Cdd:TIGR01184    1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPwLTVRENI 75
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     488 RYG----REDVTMDEIEKAVKEANAydfIMKLPHQFDtlvgERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTE 563
Cdd:TIGR01184   76 ALAvdrvLPDLSKSERRAIVEEHIA---LVGLTEAAD----KRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAL 148
                          170       180
                   ....*....|....*....|....*
gi 6755046     564 SEAVVQAALDKARE--GRTTIVIAH 586
Cdd:TIGR01184  149 TRGNLQEELMQIWEehRVTVLMVTH 173
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
1049-1262 1.56e-22

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: 99.16  E-value: 1.56e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1049 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKeikqlnvqwlrahLGIVSQEPILFDCSIAEN 1128
Cdd:cd03291   51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQFSWIMPGTIKEN 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1129 IAYGDNSRAVSHEEIVRAAKeanIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTES 1208
Cdd:cd03291  118 IIFGVSYDEYRYKSVVKACQ---LEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFT 194
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 6755046  1209 EKVVQEA-LDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQLLAQK 1262
Cdd:cd03291  195 EKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLR 249
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
1050-1249 1.58e-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: 97.73  E-value: 1.58e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMA---GSVFLDGKEIKQlnVQWLRaHLGIVSQEPILFDC-SI 1125
Cdd:cd03234   22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRKP--DQFQK-CVAYVRQDDILLPGlTV 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1126 AENIAYGDNSRavSHEEIVRAAKEANIHQFidSLPDKYNTRVGDKG-TQLSGGQKQRIAIARALVRQPHILLLDEATSAL 1204
Cdd:cd03234   99 RETLTYTAILR--LPRKSSDAIRKKRVEDV--LLRDLALTRIGGNLvKGISGGERRRVSIAVQLLWDPKVLILDEPTSGL 174
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 6755046  1205 DTESE-KVVQEALDKAREGRTCIVIAH--RLSTIQNADLIVVIENGKV 1249
Cdd:cd03234  175 DSFTAlNLVSTLSQLARRNRIVILTIHqpRSDLFRLFDRILLLSSGEI 222
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
388-614 1.64e-22

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 99.11  E-value: 1.64e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    388 MGNLEFKNVHFNYpsRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLRE 467
Cdd:PRK13652    1 MHLIETRDLCYSY--SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    468 IIGVVSQEP--VLFATTIAENIRYGREDVTMDE------IEKAVKEANAYDFIMKLPHqfdtlvgergaQLSGGQKQRIA 539
Cdd:PRK13652   79 FVGLVFQNPddQIFSPTVEQDIAFGPINLGLDEetvahrVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVA 147
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6755046    540 IARALVRNPKILLLDEATSALDTESEAVVQAALDKARE--GRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDEL 614
Cdd:PRK13652  148 IAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEI 225
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
1040-1232 2.12e-22

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


Pssm-ID: 440718 [Multi-domain]  Cd Length: 264  Bit Score: 98.23  E-value: 2.12e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1040 FNYPTRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVqWLRA-HLGIVSQEP 1118
Cdd:COG1101   11 FNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPE-YKRAkYIGRVFQDP 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1119 ILFDC---SIAENIAYGDN---SRAVSheeivRAAKEANIHQFIDS-------LPDKYNTRVGdkgtQLSGGQKQRIAIA 1185
Cdd:COG1101   90 MMGTApsmTIEENLALAYRrgkRRGLR-----RGLTKKRRELFRELlatlglgLENRLDTKVG----LLSGGQRQALSLL 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 6755046  1186 RALVRQPHILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRL 1232
Cdd:COG1101  161 MATLTKPKLLLLDEHTAALDPKTAALVLELTEKivEENNLTTLMVTHNM 209
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
1055-1259 2.13e-22

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


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 101.26  E-value: 2.13e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1055 SLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWL----RAHLGIVSQE-PILFDCSIAENI 1129
Cdd:PRK10070   48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELrevrRKKIAMVFQSfALMPHMTVLDNT 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1130 AYGDNSRAVSHEE----IVRAAKEANIHQFIDSLPDkyntrvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEATSALD 1205
Cdd:PRK10070  128 AFGMELAGINAEErrekALDALRQVGLENYAHSYPD-----------ELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 6755046   1206 TESEKVVQEALDK--AREGRTCIVIAHRL-STIQNADLIVVIENGKVKEHGTHQQLL 1259
Cdd:PRK10070  197 PLIRTEMQDELVKlqAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
86-588 2.39e-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: 104.61  E-value: 2.39e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046      86 LPSITNQSGPNST----------LIISNSSleeemAIYAYY-YTGIGAGVLIVAYIQ---VSLWCLAAGRQIHKirqKFF 151
Cdd:TIGR01271  894 NPSAPNYVDQQHAnasspdvqkpVIITPTS-----AYYIFYiYVGTADSVLALGFFRglpLVHTLLTVSKRLHE---QML 965
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     152 HAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDKIGMFFQSITTFL-AGFIIGFISGWkltlVILAVSPLIGLSSAL 230
Cdd:TIGR01271  966 HSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLgAIFVVSVLQPY----IFIAAIPVAVIFIML 1041
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     231 WAKVL-TSFTNKELQAYAKAGAVAEEV--LAAIRTVIAFGGQQkelerYNKNLeeaknvgIKKAITASISIGIAYL---- 303
Cdd:TIGR01271 1042 RAYFLrTSQQLKQLESEARSPIFSHLItsLKGLWTIRAFGRQS-----YFETL-------FHKALNLHTANWFLYLstlr 1109
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     304 -------LVYASYALAFWY---GTSLVlsNEYSIGEVLTVFFSILlGTFSIGhLAPNIEAFANARGAAfEIFKIID--NE 371
Cdd:TIGR01271 1110 wfqmridIIFVFFFIAVTFiaiGTNQD--GEGEVGIILTLAMNIL-STLQWA-VNSSIDVDGLMRSVS-RVFKFIDlpQE 1184
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     372 PSIDSFSTKGYKPDSIM--------------GNLEFKNVHFNYPSRSEvQILKGLNLKVKSGQTVALVGNSGCGKSTTVQ 437
Cdd:TIGR01271 1185 EPRPSGGGGKYQLSTVLvienphaqkcwpsgGQMDVQGLTAKYTEAGR-AVLQDLSFSVEGGQRVGLLGRTGSGKSTLLS 1263
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     438 LMQRLYDPlEGVVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENI----RYGREdvtmdEIEKAVKEANAYDFIM 513
Cdd:TIGR01271 1264 ALLRLLST-EGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLdpyeQWSDE-----EIWKVAEEVGLKSVIE 1337
                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6755046     514 KLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRL 588
Cdd:TIGR01271 1338 QFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRV 1412
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
402-563 2.78e-22

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


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 96.40  E-value: 2.78e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   402 SRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDP---LEGVVSIDGQDIRTINVrYLREIiGVVSQEPVL 478
Cdd:COG4136   10 TLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPA-EQRRI-GILFQDDLL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   479 FA-TTIAENIRYG-REDVTM----DEIEKAVKEANaydfimkLPHQFDTLVgergAQLSGGQKQRIAIARALVRNPKILL 552
Cdd:COG4136   88 FPhLSVGENLAFAlPPTIGRaqrrARVEQALEEAG-------LAGFADRDP----ATLSGGQRARVALLRALLAEPRALL 156
                        170
                 ....*....|.
gi 6755046   553 LDEATSALDTE 563
Cdd:COG4136  157 LDEPFSKLDAA 167
PTZ00243 PTZ00243
ABC transporter; Provisional
995-1275 3.11e-22

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 104.48  E-value: 3.11e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    995 DYAKAKVSASHIIRiiektPEIDSYSTEGLKPTLLEGNVKFNGVQFnYPTRPNIpVLQGLSLEVKKGQTLALVGSSGCGK 1074
Cdd:PTZ00243  627 DYGSPSSASRHIVE-----GGTGGGHEATPTSERSAKTPKMKTDDF-FELEPKV-LLRDVSVSVPRGKLTVVLGATGSGK 699
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1075 STVVQLLERFYDPMAGSVfldgkeikqlnvqWLRAHLGIVSQEPILFDCSIAENIAYGDNSRAVSHEEIVRAAK-EANIH 1153
Cdd:PTZ00243  700 STLLQSLLSQFEISEGRV-------------WAERSIAYVPQQAWIMNATVRGNILFFDEEDAARLADAVRVSQlEADLA 766
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1154 QfidsLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTE-SEKVVQEALDKAREGRTCIVIAHRL 1232
Cdd:PTZ00243  767 Q----LGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHvGERVVEECFLGALAGKTRVLATHQV 842
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 6755046   1233 STIQNADLIVVIENGKVKEHGTHQQlLAQKGIYFSMVQAGAKR 1275
Cdd:PTZ00243  843 HVVPRADYVVALGDGRVEFSGSSAD-FMRTSLYATLAAELKEN 884
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
391-618 3.14e-22

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 97.53  E-value: 3.14e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    391 LEFKNVHFNYPSRsevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIG 470
Cdd:PRK13548    3 LEARNLSVRLGGR---TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    471 VVSQEPVL-FATTIAENIRYGREDVT--MDEIEKAVKEANAydfIMKLPHqfdtLVGERGAQLSGGQKQRIAIARALVR- 546
Cdd:PRK13548   80 VLPQHSSLsFPFTVEEVVAMGRAPHGlsRAEDDALVAAALA---QVDLAH----LAGRDYPQLSGGEQQRVQLARVLAQl 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    547 -----NPKILLLDEATSALD-TESEAVVQAALDKARE-GRTTIVIAHRLS-TVRNADVIAGFDGGVIVEQGNHDELMREK 618
Cdd:PRK13548  153 wepdgPPRWLLLDEPTSALDlAHQHHVLRLARQLAHErGLAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPAEVLTPE 232
CeuD COG4604
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ...
392-621 3.68e-22

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


Pssm-ID: 443654 [Multi-domain]  Cd Length: 252  Bit Score: 97.08  E-value: 3.68e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   392 EFKNVHFNYpsrSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIGV 471
Cdd:COG4604    3 EIKNVSKRY---GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   472 VSQEPVlFAT--TIAENIRYGR----------EDvtmdeiEKAVKEANAYDFIMKLPHQF-DtlvgergaQLSGGQKQRI 538
Cdd:COG4604   80 LRQENH-INSrlTVRELVAFGRfpyskgrltaED------REIIDEAIAYLDLEDLADRYlD--------ELSGGQRQRA 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   539 AIARALVRNPKILLLDEATSALDTESEAVVQAALDK-ARE-GRTTIVIAHRLstvrN-----ADVIAGFDGGVIVEQGNH 611
Cdd:COG4604  145 FIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRlADElGKTVVIVLHDI----NfascyADHIVAMKDGRVVAQGTP 220
                        250
                 ....*....|...
gi 6755046   612 DELMRE---KGIY 621
Cdd:COG4604  221 EEIITPevlSDIY 233
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
1049-1260 3.88e-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: 96.46  E-value: 3.88e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1049 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVqWLRAHLGI--VSQEPILF-DCSI 1125
Cdd:cd03218   14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPM-HKRARLGIgyLPQEASIFrKLTV 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1126 AENIAYGDNSRAVSHEEIVRAAkEANIHQF-IDSLPDKyntrvgdKGTQLSGGQKQRIAIARALVRQPHILLLDEATSAL 1204
Cdd:cd03218   93 EENILAVLEIRGLSKKEREEKL-EELLEEFhITHLRKS-------KASSLSGGERRRVEIARALATNPKFLLLDEPFAGV 164
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 6755046  1205 DTESEKVVQEALDKAREGRTCIVIA-HRLS-TIQNADLIVVIENGKVKEHGTHQQLLA 1260
Cdd:cd03218  165 DPIAVQDIQKIIKILKDRGIGVLITdHNVReTLSITDRAYIIYEGKVLAEGTPEEIAA 222
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
1042-1261 3.92e-22

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 97.95  E-value: 3.92e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1042 YPTRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGIVSQEP--I 1119
Cdd:PRK13652   11 YSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPddQ 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1120 LFDCSIAENIAYGDNSRAVSHEEIVRAAKEA----NIHQFIDSLPDkyntrvgdkgtQLSGGQKQRIAIARALVRQPHIL 1195
Cdd:PRK13652   91 IFSPTVEQDIAFGPINLGLDEETVAHRVSSAlhmlGLEELRDRVPH-----------HLSGGEKKRVAIAGVIAMEPQVL 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6755046   1196 LLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTI-QNADLIVVIENGKVKEHGTHQQLLAQ 1261
Cdd:PRK13652  160 VLDEPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEIFLQ 228
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
391-609 4.17e-22

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 102.09  E-value: 4.17e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    391 LEFKNVHFNYPSR--------SEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYdPLEGVVSIDGQDIRTINV 462
Cdd:PRK15134  276 LDVEQLQVAFPIRkgilkrtvDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNR 354
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    463 RYL---REIIGVVSQEP---------VLfaTTIAENIRYGREDVTMDEIEKAVKEAnaydfiMKlphqfdtlvgERG--- 527
Cdd:PRK15134  355 RQLlpvRHRIQVVFQDPnsslnprlnVL--QIIEEGLRVHQPTLSAAQREQQVIAV------ME----------EVGldp 416
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    528 -------AQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGR--TTIVIAHRLSTVRNA--DV 596
Cdd:PRK15134  417 etrhrypAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHqlAYLFISHDLHVVRALchQV 496
                         250
                  ....*....|...
gi 6755046    597 IAGFDGGViVEQG 609
Cdd:PRK15134  497 IVLRQGEV-VEQG 508
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
400-595 5.23e-22

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 94.99  E-value: 5.23e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    400 YPSRsevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGqdirTINVRYLREIIGVVSQEPVlf 479
Cdd:NF040873    2 YGGR---PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG----GARVAYVPQRSEVPDSLPL-- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    480 atTIAENI------------RYGREDvtmdeiEKAVKEAnaydfIMKLphQFDTLVGERGAQLSGGQKQRIAIARALVRN 547
Cdd:NF040873   73 --TVRDLVamgrwarrglwrRLTRDD------RAAVDDA-----LERV--GLADLAGRQLGELSGGQRQRALLAQGLAQE 137
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 6755046    548 PKILLLDEATSALDTESEAVVQAAL-DKAREGRTTIVIAHRLSTVRNAD 595
Cdd:NF040873  138 ADLLLLDEPTTGLDAESRERIIALLaEEHARGATVVVVTHDLELVRRAD 186
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
391-614 5.37e-22

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 99.52  E-value: 5.37e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    391 LEFKNVHFNYPSRSEVQilkGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINvRYLREIiG 470
Cdd:PRK11607   20 LEIRNLTKSFDGQHAVD---DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVP-PYQRPI-N 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    471 VVSQEPVLFA-TTIAENIRYG--REDVTMDEIEKAVKE----ANAYDFIMKLPHQfdtlvgergaqLSGGQKQRIAIARA 543
Cdd:PRK11607   95 MMFQSYALFPhMTVEQNIAFGlkQDKLPKAEIASRVNEmlglVHMQEFAKRKPHQ-----------LSGGQRQRVALARS 163
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6755046    544 LVRNPKILLLDEATSALDTESEAVVQAALDK--AREGRTTIVIAH-RLSTVRNADVIAGFDGGVIVEQGNHDEL 614
Cdd:PRK11607  164 LAKRPKLLLLDEPMGALDKKLRDRMQLEVVDilERVGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
1049-1272 6.30e-22

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 97.00  E-value: 6.30e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1049 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEI--KQLNVQWLRAHLGIVSQEP--ILFDCS 1124
Cdd:PRK13638   15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdySKRGLLALRQQVATVFQDPeqQIFYTD 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1125 IAENIAYGDNSRAVSHEEIVRAAKEANihqfidSLPDKYNTRvgDKGTQ-LSGGQKQRIAIARALVRQPHILLLDEATSA 1203
Cdd:PRK13638   95 IDSDIAFSLRNLGVPEAEITRRVDEAL------TLVDAQHFR--HQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAG 166
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6755046   1204 LDTESEKVVQEALDK-AREGRTCIVIAHRLSTI-QNADLIVVIENGKVKEHGTHQQLLAQKGIyfsMVQAG 1272
Cdd:PRK13638  167 LDPAGRTQMIAIIRRiVAQGNHVIISSHDIDLIyEISDAVYVLRQGQILTHGAPGEVFACTEA---MEQAG 234
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
1049-1242 7.01e-22

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 95.55  E-value: 7.01e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1049 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAEN 1128
Cdd:PRK10247   21 KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTVYDN 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1129 IAYGDNSRavsHEEIVRAAKEANIHQFidSLPDKyntrVGDKG-TQLSGGQKQRIAIARALVRQPHILLLDEATSALDTE 1207
Cdd:PRK10247  101 LIFPWQIR---NQQPDPAIFLDDLERF--ALPDT----ILTKNiAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDES 171
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 6755046   1208 SEKVVQEALDK-AREGRTCIV-IAHRLSTIQNADLIV 1242
Cdd:PRK10247  172 NKHNVNEIIHRyVREQNIAVLwVTHDKDEINHADKVI 208
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
1011-1252 7.65e-22

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 100.91  E-value: 7.65e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1011 EKTPEIDSYSTEGLKPTLLEgnvkFNGVQFNYPTRPnipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAG 1090
Cdd:COG0488  298 DKTVEIRFPPPERLGKKVLE----LEGLSKSYGDKT---LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSG 370
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1091 SVFLdGKEIKqlnvqwlrahLGIVSQEPILFDC--SIAENIAygdnsravsheEIVRAAKEANIHQFIDSL---PDKYNT 1165
Cdd:COG0488  371 TVKL-GETVK----------IGYFDQHQEELDPdkTVLDELR-----------DGAPGGTEQEVRGYLGRFlfsGDDAFK 428
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1166 RVGDkgtqLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDkAREGrTCIVIAH-R--LSTIqnADLIV 1242
Cdd:COG0488  429 PVGV----LSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALD-DFPG-TVLLVSHdRyfLDRV--ATRIL 500
                        250
                 ....*....|
gi 6755046  1243 VIENGKVKEH 1252
Cdd:COG0488  501 EFEDGGVREY 510
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
389-588 9.26e-22

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: 96.85  E-value: 9.26e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   389 GNLEFKNVHFNYPSRSEVqILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDpLEGVVSIDGQDIRTINVRYLREI 468
Cdd:cd03289    1 GQMTVKDLTAKYTEGGNA-VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   469 IGVVSQEPVLFATTIAENIR-YGREdvTMDEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRN 547
Cdd:cd03289   79 FGVIPQKVFIFSGTFRKNLDpYGKW--SDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSK 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 6755046   548 PKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRL 588
Cdd:cd03289  157 AKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRI 197
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
391-592 9.84e-22

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 100.49  E-value: 9.84e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   391 LEFKNVHFNYPSrseVQILKGLNLKVKSGQTVALVGNSGCGKSTtvqLMQRL---YDPLEGVVSIDGQDIRtinvrylre 467
Cdd:COG3845    6 LELRGITKRFGG---VVANDDVSLTVRPGEIHALLGENGAGKST---LMKILyglYQPDSGEILIDGKPVR--------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   468 I----------IGVVSQEPVLFAT-TIAENIRYGREDVT-----MDEIEKAVKE-ANAYDFIMKLphqfDTLVGergaQL 530
Cdd:COG3845   71 IrsprdaialgIGMVHQHFMLVPNlTVAENIVLGLEPTKggrldRKAARARIRElSERYGLDVDP----DAKVE----DL 142
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6755046   531 SGGQKQRIAIARALVRNPKILLLDEATSALdTESEAV-VQAALDK-AREGRTTIVIAHRLSTVR 592
Cdd:COG3845  143 SVGEQQRVEILKALYRGARILILDEPTAVL-TPQEADeLFEILRRlAAEGKSIIFITHKLREVM 205
SufC COG0396
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ...
391-617 9.99e-22

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


Pssm-ID: 440165 [Multi-domain]  Cd Length: 245  Bit Score: 95.90  E-value: 9.99e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   391 LEFKNVHFnypSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQ-LMQR-LYDPLEGVVSIDGQDI--RTINVR--- 463
Cdd:COG0396    1 LEIKNLHV---SVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKvLMGHpKYEVTSGSILLDGEDIleLSPDERara 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   464 -------YLREIIGV-VSQepvlFATTIAENIRygREDVTMDEIEKAVKEANAydfIMKLPHQFdtlvGERG--AQLSGG 533
Cdd:COG0396   78 giflafqYPVEIPGVsVSN----FLRTALNARR--GEELSAREFLKLLKEKMK---ELGLDEDF----LDRYvnEGFSGG 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   534 QKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAR-EGRTTIVIAH--RLSTVRNADVIAGFDGGVIVEQGN 610
Cdd:COG0396  145 EKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRsPDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGG 224

                 ....*..
gi 6755046   611 HdELMRE 617
Cdd:COG0396  225 K-ELALE 230
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
1042-1244 1.18e-21

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 93.84  E-value: 1.18e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1042 YPTRPnipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQwlrahlgiVSQEPILF 1121
Cdd:NF040873    2 YGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQ--------RSEVPDSL 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1122 DCSIAENIAYGDNSRAVSHEEIVRAAKEAnihqFIDSLpdkynTRVGDKG------TQLSGGQKQRIAIARALVRQPHIL 1195
Cdd:NF040873   71 PLTVRDLVAMGRWARRGLWRRLTRDDRAA----VDDAL-----ERVGLADlagrqlGELSGGQRQRALLAQGLAQEADLL 141
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 6755046   1196 LLDEATSALDTESEKVVQEAL-DKAREGRTCIVIAHRLSTIQNADLIVVI 1244
Cdd:NF040873  142 LLDEPTTGLDAESRERIIALLaEEHARGATVVVVTHDLELVRRADPCVLL 191
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
1044-1259 1.30e-21

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 98.76  E-value: 1.30e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1044 TRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGIVSQEPIL-FD 1122
Cdd:PRK09536   12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFE 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1123 CSIAENIAYGDN---SRAVSHEEIVRAAKE-----ANIHQFIDSlpdkyntrvgdKGTQLSGGQKQRIAIARALVRQPHI 1194
Cdd:PRK09536   92 FDVRQVVEMGRTphrSRFDTWTETDRAAVEramerTGVAQFADR-----------PVTSLSGGERQRVLLARALAQATPV 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1195 LLLDEATSALDTESE----KVVQEALDkarEGRTCIVIAHRLS-TIQNADLIVVIENGKVKEHGTHQQLL 1259
Cdd:PRK09536  161 LLLDEPTASLDINHQvrtlELVRRLVD---DGKTAVAAIHDLDlAARYCDELVLLADGRVRAAGPPADVL 227
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
1048-1251 1.89e-21

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 94.46  E-value: 1.89e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1048 IPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQW---LRA-HLGIVSQEPILFDC 1123
Cdd:PRK10584   23 LSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEArakLRAkHVGFVFQSFMLIPT 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1124 SIA-ENIAY-----GDNSRAvSHEEIVRAAKEANIHQFIDSLPdkyntrvgdkgTQLSGGQKQRIAIARALVRQPHILLL 1197
Cdd:PRK10584  103 LNAlENVELpallrGESSRQ-SRNGAKALLEQLGLGKRLDHLP-----------AQLSGGEQQRVALARAFNGRPDVLFA 170
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 6755046   1198 DEATSALDTES-EKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIVVIENGKVKE 1251
Cdd:PRK10584  171 DEPTGNLDRQTgDKIADLLFSLNREhGTTLILVTHDLQLAARCDRRLRLVNGQLQE 226
ABC_6TM_TmrA_like cd18544
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ...
100-336 2.07e-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: 2.07e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   100 IISNSSLEEEMAIYAYYYTGIGAGVLIVAYIQVSLWCLAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVS 179
Cdd:cd18544   30 IVPGQGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDRTPVGRLVTRVTNDTE 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   180 KINDGIGDKIGMFFQSITTFLAGFIIGFISGWKLTLVILAVSPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAA 259
Cdd:cd18544  110 ALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATYLFRKKSRKAYREVREKLSRLNAFLQESISG 189
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6755046   260 IRTVIAFGGQQKELERYNKNLEEAKNVGIKKAITASISIGIAYLLVYASYALAFWYGTSLVLSNEYSIGeVLTVFFS 336
Cdd:cd18544  190 MSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELLSSLALALVLWYGGGQVLSGAVTLG-VLYAFIQ 265
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
1026-1248 4.29e-21

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 98.46  E-value: 4.29e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1026 PTLLE--GNVK-FNGVqfnyptrpniPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYdPMA---GSVFLDGKEI 1099
Cdd:PRK13549    3 EYLLEmkNITKtFGGV----------KALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHGtyeGEIIFEGEEL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1100 KQLNVQWL-RAHLGIVSQEPILF-DCSIAENIAYGD---NSRAVSHEEIVRAAKE--ANIHQFIDSlpdkyNTRVGDkgt 1172
Cdd:PRK13549   72 QASNIRDTeRAGIAIIHQELALVkELSVLENIFLGNeitPGGIMDYDAMYLRAQKllAQLKLDINP-----ATPVGN--- 143
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6755046   1173 qLSGGQKQRIAIARALVRQPHILLLDEATSALdTESEKVVQEAL--DKAREGRTCIVIAHRLSTIQN-ADLIVVIENGK 1248
Cdd:PRK13549  144 -LGLGQQQLVEIAKALNKQARLLILDEPTASL-TESETAVLLDIirDLKAHGIACIYISHKLNEVKAiSDTICVIRDGR 220
ABC_6TM_exporter_like cd18564
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
119-343 4.64e-21

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: 95.27  E-value: 4.64e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   119 GIGAGVLIVAYIQVSLWCLAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDKIGMFFQSITT 198
Cdd:cd18564   62 GIALLRGLASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLT 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   199 FLAGFIIGFISGWKLTLVILAVSPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQKELERYNK 278
Cdd:cd18564  142 LVGMLGVMFWLDWQLALIALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFAR 221
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6755046   279 NLEEAKNVGIKKAITASISIGIAYLLVYASYALAFWYGTSLVLSNEYSIGEvLTVFFSILLGTFS 343
Cdd:cd18564  222 ENRKSLRAGLRAARLQALLSPVVDVLVAVGTALVLWFGAWLVLAGRLTPGD-LLVFLAYLKNLYK 285
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
1035-1262 4.69e-21

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 98.60  E-value: 4.69e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1035 FNGVQFNYPTRPnipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGkeikqlnvqwlRAHLGIV 1114
Cdd:COG0488    1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-----------GLRIGYL 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1115 SQEPILFD-CSIAENIAYGDNSR--------------AVSHEEIVRAAK-------------EANIHQFIDSL---PDKY 1163
Cdd:COG0488   67 PQEPPLDDdLTVLDTVLDGDAELraleaeleeleaklAEPDEDLERLAElqeefealggweaEARAEEILSGLgfpEEDL 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1164 NTRVGDkgtqLSGGQKQRIAIARALVRQPHILLLDEATSALDTESekvVQ--EALDKAREGrTCIVIAH-R--LSTIqnA 1238
Cdd:COG0488  147 DRPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES---IEwlEEFLKNYPG-TVLVVSHdRyfLDRV--A 216
                        250       260
                 ....*....|....*....|....*
gi 6755046  1239 DLIVVIENGKVKEH-GTHQQLLAQK 1262
Cdd:COG0488  217 TRILELDRGKLTLYpGNYSAYLEQR 241
ABC_6TM_TAP2 cd18590
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ...
145-334 5.37e-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: 94.71  E-value: 5.37e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   145 KIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDKIGMFFQSI--TTFLAGFIIGFisGWKLTLVILAVSP 222
Cdd:cd18590   70 RLRHQLFSSLVQQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLvkTLGMLGFMLSL--SWQLTLLTLIEMP 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   223 LIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQKELERYNKNLEEAKNVGIKKAITASISIGIAY 302
Cdd:cd18590  148 LTAIAQKVYNTYHQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTVRAVYLLVRR 227
                        170       180       190
                 ....*....|....*....|....*....|..
gi 6755046   303 LLVYASYALAFWYGTSLVLSNEYSIGEVLTVF 334
Cdd:cd18590  228 VLQLGVQVLMLYCGRQLIQSGHLTTGSLVSFI 259
PLN03232 PLN03232
ABC transporter C family member; Provisional
1040-1272 5.38e-21

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 100.44  E-value: 5.38e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1040 FNYPTRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLdgkeikqlnvqwLRAHLGIVSQEPI 1119
Cdd:PLN03232  622 FSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVV------------IRGSVAYVPQVSW 689
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1120 LFDCSIAENIAYGDNSRAvshEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDE 1199
Cdd:PLN03232  690 IFNATVRENILFGSDFES---ERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDD 766
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6755046   1200 ATSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIENGKVKEHGTHQQlLAQKGIYFS--MVQAG 1272
Cdd:PLN03232  767 PLSALDAHvAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAE-LSKSGSLFKklMENAG 841
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
1049-1199 6.72e-21

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


Pssm-ID: 440752 [Multi-domain]  Cd Length: 240  Bit Score: 93.17  E-value: 6.72e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1049 PVLQGLSLEVKKGQTLALVGSSGCGKSTVvqllerFY------DPMAGSVFLDGKEIKQLNVqWLRAHLGI--VSQEPIL 1120
Cdd:COG1137   17 TVVKDVSLEVNQGEIVGLLGPNGAGKTTT------FYmivglvKPDSGRIFLDGEDITHLPM-HKRARLGIgyLPQEASI 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1121 F-DCSIAENIaygdnsRAVSheEIVRAAKEAnIHQFIDSLPDKYN-TRVGD-KGTQLSGGQKQRIAIARALVRQPHILLL 1197
Cdd:COG1137   90 FrKLTVEDNI------LAVL--ELRKLSKKE-REERLEELLEEFGiTHLRKsKAYSLSGGERRRVEIARALATNPKFILL 160

                 ..
gi 6755046  1198 DE 1199
Cdd:COG1137  161 DE 162
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
407-615 9.96e-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: 92.61  E-value: 9.96e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   407 QILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINV-RYLREIIGVVSQEPVLFAT-TIA 484
Cdd:cd03218   14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMhKRARLGIGYLPQEASIFRKlTVE 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   485 ENIRYGREDVTMDEIEKAVK-EANAYDF-IMKLPHQFdtlvgerGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDT 562
Cdd:cd03218   94 ENILAVLEIRGLSKKEREEKlEELLEEFhITHLRKSK-------ASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDP 166
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 6755046   563 ESEAVVQAALDKAREGRTTIVIA-HR----LSTVRNADVIagFDGGVIVEqGNHDELM 615
Cdd:cd03218  167 IAVQDIQKIIKILKDRGIGVLITdHNvretLSITDRAYII--YEGKVLAE-GTPEEIA 221
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
1040-1258 1.34e-20

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 94.00  E-value: 1.34e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1040 FNYPTRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSV---FLDGKEIKQL-------------- 1102
Cdd:PRK13651   12 FNKKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewiFKDEKNKKKTkekekvleklviqk 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1103 -------NVQWLRAHLGIVSQ--EPILFDCSIAENIAYGDNSRAVSHEEIVRAAKEanihqFID--SLPDKYNTRvgdKG 1171
Cdd:PRK13651   92 trfkkikKIKEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSKEEAKKRAAK-----YIElvGLDESYLQR---SP 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1172 TQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKA-REGRTCIVIAHRL-STIQNADLIVVIENGK- 1248
Cdd:PRK13651  164 FELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLdNVLEWTKRTIFFKDGKi 243
                         250
                  ....*....|
gi 6755046   1249 VKEHGTHQQL 1258
Cdd:PRK13651  244 IKDGDTYDIL 253
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
1036-1249 1.47e-20

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 92.82  E-value: 1.47e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1036 NGVQFNYPTRPnipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDP-----MAGSVFL-DGKEIKQLNVQWLRa 1109
Cdd:PRK11247   16 NAVSKRYGERT---VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPsagelLAGTAPLaEAREDTRLMFQDAR- 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1110 hlgivsqepILFDCSIAENIAYGdnsravsheeiVRAAKEANIHQFIDS--LPDkyntRVGDKGTQLSGGQKQRIAIARA 1187
Cdd:PRK11247   92 ---------LLPWKKVIDNVGLG-----------LKGQWRDAALQALAAvgLAD----RANEWPAALSGGQKQRVALARA 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6755046   1188 LVRQPHILLLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVIENGKV 1249
Cdd:PRK11247  148 LIHRPGLLLLDEPLGALDALTRIEMQDLIESlwQQHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
391-587 1.61e-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: 89.91  E-value: 1.61e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   391 LEFKNVHFNYPSRSevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDirtiNVRYLreiig 470
Cdd:cd03223    1 IELENLSLATPDGR--VLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGE----DLLFL----- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   471 vvSQEPVLFATTIAENIRYGREDVtmdeiekavkeanaydfimklphqfdtlvgergaqLSGGQKQRIAIARALVRNPKI 550
Cdd:cd03223   70 --PQRPYLPLGTLREQLIYPWDDV-----------------------------------LSGGEQQRLAFARLLLHKPKF 112
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 6755046   551 LLLDEATSALDTESEAvvqAALDKAREGRTTIV-IAHR 587
Cdd:cd03223  113 VFLDEATSALDEESED---RLYQLLKELGITVIsVGHR 147
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...
406-616 1.63e-20

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: 92.41  E-value: 1.63e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   406 VQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDI--------------RTI-NVRYLRE--- 467
Cdd:COG0411   17 LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDItglpphriarlgiaRTFqNPRLFPEltv 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   468 ----IIGVVSQEPVLFATTIAENIRYGREDvtmDEIEKAVKEANAydfIMKLPHQFDTLVGErgaqLSGGQKQRIAIARA 543
Cdd:COG0411   97 lenvLVAAHARLGRGLLAALLRLPRARREE---REARERAEELLE---RVGLADRADEPAGN----LSYGQQRRLEIARA 166
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6755046   544 LVRNPKILLLDEATSAL-DTESEAVVQAALD-KAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDELMR 616
Cdd:COG0411  167 LATEPKLLLLDEPAAGLnPEETEELAELIRRlRDERGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGTPAEVRA 242
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
1050-1260 1.64e-20

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 93.24  E-value: 1.64e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAG-----SVFLDGKEI-KQLNVQWLRAHLGIVSQEPILFDC 1123
Cdd:PRK14271   36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIfNYRDVLEFRRRVGMLFQRPNPFPM 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1124 SIAENIAYGDNSRAVSHEEIVRAAKEANIHQFidSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSA 1203
Cdd:PRK14271  116 SIMDNVLAGVRAHKLVPRKEFRGVAQARLTEV--GLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSA 193
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 6755046   1204 LDTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLLA 1260
Cdd:PRK14271  194 LDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLFS 251
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
1026-1260 1.97e-20

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 96.70  E-value: 1.97e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1026 PTLLEgnvkFNGVQFNYPTRPNI--------PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYdPMAGSVFLDGK 1097
Cdd:PRK15134  273 SPLLD----VEQLQVAFPIRKGIlkrtvdhnVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQ 347
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1098 EIKQLNVQWL---RAHLGIVSQEP---ILFDCSIAENIAYGdnsRAVSHEEIVRAAKEAnihQFIDSLpdkynTRVG-DK 1170
Cdd:PRK15134  348 PLHNLNRRQLlpvRHRIQVVFQDPnssLNPRLNVLQIIEEG---LRVHQPTLSAAQREQ---QVIAVM-----EEVGlDP 416
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1171 GT------QLSGGQKQRIAIARALVRQPHILLLDEATSALDteseKVVQE---ALDKAREGR---TCIVIAHRLSTIQN- 1237
Cdd:PRK15134  417 ETrhrypaEFSGGQRQRIAIARALILKPSLIILDEPTSSLD----KTVQAqilALLKSLQQKhqlAYLFISHDLHVVRAl 492
                         250       260
                  ....*....|....*....|...
gi 6755046   1238 ADLIVVIENGKVKEHGTHQQLLA 1260
Cdd:PRK15134  493 CHQVIVLRQGEVVEQGDCERVFA 515
cbiO PRK13643
energy-coupling factor transporter ATPase;
391-617 2.14e-20

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 93.26  E-value: 2.14e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    391 LEFKNVHFNYPSRSEV--QILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTIN----VRY 464
Cdd:PRK13643    2 IKFEKVNYTYQPNSPFasRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeIKP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    465 LREIIGVVSQEP--VLFATTIAENIRYGRED--VTMDEIEKAVKE-----ANAYDFIMKLPHQfdtlvgergaqLSGGQK 535
Cdd:PRK13643   82 VRKKVGVVFQFPesQLFEETVLKDVAFGPQNfgIPKEKAEKIAAEklemvGLADEFWEKSPFE-----------LSGGQM 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    536 QRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKARE-GRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDE 613
Cdd:PRK13643  151 RRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSD 230

                  ....
gi 6755046    614 LMRE 617
Cdd:PRK13643  231 VFQE 234
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
1051-1255 3.12e-20

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 90.70  E-value: 3.12e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1051 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLN---VQWLRAHLGIVSQEP-ILFDCSIA 1126
Cdd:PRK10908   18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKnreVPFLRRQIGMIFQDHhLLMDRTVY 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1127 ENIAYgdnsravshEEIVRAAKEANIHQFIDSLPDKyntrVG--DKG----TQLSGGQKQRIAIARALVRQPHILLLDEA 1200
Cdd:PRK10908   98 DNVAI---------PLIIAGASGDDIRRRVSAALDK----VGllDKAknfpIQLSGGEQQRVGIARAVVNKPAVLLADEP 164
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 6755046   1201 TSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQNADL-IVVIENGKVkeHGTH 1255
Cdd:PRK10908  165 TGNLDDAlSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYrMLTLSDGHL--HGGV 219
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
1028-1249 3.31e-20

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 96.72  E-value: 3.31e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1028 LLEgnvkFNGVQFNYPT-RPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQW 1106
Cdd:PRK10535    4 LLE----LKDIRRSYPSgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1107 L----RAHLGIVSQE-PILFDCSIAENIAYgdnsRAVsHEEIVRAAKEANIHQFIDSLpdKYNTRVGDKGTQLSGGQKQR 1181
Cdd:PRK10535   80 LaqlrREHFGFIFQRyHLLSHLTAAQNVEV----PAV-YAGLERKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQR 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6755046   1182 IAIARALVRQPHILLLDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIVVIENGKV 1249
Cdd:PRK10535  153 VSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDrGHTVIIVTHDPQVAAQAERVIEIRDGEI 221
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
1050-1233 4.08e-20

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 90.65  E-value: 4.08e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQW---LRAH-LGIVSQ-EPILFDCS 1124
Cdd:PRK11629   24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeLRNQkLGFIYQfHHLLPDFT 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1125 IAENIAY----GDNSRAVSHEEIVRAAKEANIHQfidslpdkyntRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEA 1200
Cdd:PRK11629  104 ALENVAMplliGKKKPAEINSRALEMLAAVGLEH-----------RANHRPSELSGGERQRVAIARALVNNPRLVLADEP 172
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 6755046   1201 TSALDTESEKVVQEALDK--AREGRTCIVIAHRLS 1233
Cdd:PRK11629  173 TGNLDARNADSIFQLLGElnRLQGTAFLVVTHDLQ 207
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
391-608 4.88e-20

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 95.46  E-value: 4.88e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    391 LEFKNVHFNYPSrseVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREI-I 469
Cdd:PRK10762    5 LQLKGIDKAFPG---VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAgI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    470 GVVSQEPVLFAT-TIAENIRYGREDVT-MDEIE--KAVKEANAYDFIMKLPHQFDTLVGErgaqLSGGQKQRIAIARALV 545
Cdd:PRK10762   82 GIIHQELNLIPQlTIAENIFLGREFVNrFGRIDwkKMYAEADKLLARLNLRFSSDKLVGE----LSIGEQQMVEIAKVLS 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6755046    546 RNPKILLLDEATSAL-DTESEAVVQAALDKAREGRTTIVIAHRLSTVRNA--DVIAGFDGGVIVEQ 608
Cdd:PRK10762  158 FESKVIIMDEPTDALtDTETESLFRVIRELKSQGRGIVYISHRLKEIFEIcdDVTVFRDGQFIAER 223
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
1056-1253 6.86e-20

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 93.17  E-value: 6.86e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1056 LEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKqlNVQWLRAHLGIVSQEPILF-DCSIAENIAYGDN 1134
Cdd:PRK11000   24 LDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMN--DVPPAERGVGMVFQSYALYpHLSVAENMSFGLK 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1135 SRAVSHEEIVRAAKE-ANIHQfIDSLPDKyntrvgdKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEkvVQ 1213
Cdd:PRK11000  102 LAGAKKEEINQRVNQvAEVLQ-LAHLLDR-------KPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALR--VQ 171
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 6755046   1214 EALDKA----REGRTCIVIAH-RLSTIQNADLIVVIENGKVKEHG 1253
Cdd:PRK11000  172 MRIEISrlhkRLGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVG 216
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
1050-1261 8.26e-20

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


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 91.32  E-value: 8.26e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNvqwlRAHLGIVSQEPILF-DCSIAEN 1128
Cdd:COG4152   16 AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED----RRRIGYLPEERGLYpKMKVGEQ 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1129 IAY-----GdnsraVSHEEIVRAAKEanihqFID--SLPDKYNTRVGDkgtqLSGGQKQRIAIARALVRQPHILLLDEAT 1201
Cdd:COG4152   92 LVYlarlkG-----LSKAEAKRRADE-----WLErlGLGDRANKKVEE----LSKGNQQKVQLIAALLHDPELLILDEPF 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6755046  1202 SALDTES-EKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLLAQ 1261
Cdd:COG4152  158 SGLDPVNvELLKDVIRELAAKGTTVIFSSHQMELVEElCDRIVIINKGRKVLSGSVDEIRRQ 219
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
394-616 9.16e-20

Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 90.62  E-value: 9.16e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    394 KNVHFNYPSRSevqILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVR-YLREIIGVV 472
Cdd:PRK10575   15 RNVSFRVPGRT---LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKaFARKVAYLP 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    473 SQEPVLFATTIAENI------------RYGREDvtmdeiEKAVKEANAYDFIMKLPHQfdtLVGergaQLSGGQKQRIAI 540
Cdd:PRK10575   92 QQLPAAEGMTVRELVaigrypwhgalgRFGAAD------REKVEEAISLVGLKPLAHR---LVD----SLSGGERQRAWI 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6755046    541 ARALVRNPKILLLDEATSALDTESEAVVQAALDK-ARE-GRTTIVIAHRLS-TVRNADVIAGFDGGVIVEQGNHDELMR 616
Cdd:PRK10575  159 AMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRlSQErGLTVIAVLHDINmAARYCDYLVALRGGEMIAQGTPAELMR 237
cbiO PRK13646
energy-coupling factor transporter ATPase;
1033-1262 9.75e-20

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 90.99  E-value: 9.75e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1033 VKFNGVQFNYP--TRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEI----KQLNVQW 1106
Cdd:PRK13646    3 IRFDNVSYTYQkgTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktKDKYIRP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1107 LRAHLGIVSQ--EPILFDCSIAENIAYGDNSRAVSHEEIVRAAkeaniHQFIDSLPDKYNTrVGDKGTQLSGGQKQRIAI 1184
Cdd:PRK13646   83 VRKRIGMVFQfpESQLFEDTVEREIIFGPKNFKMNLDEVKNYA-----HRLLMDLGFSRDV-MSQSPFQMSGGQMRKIAI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1185 ARALVRQPHILLLDEATSALDTESEKVVQEALDKAR--EGRTCIVIAHRLSTI-QNADLIVVIENGKVKEHGTHQQLLAQ 1261
Cdd:PRK13646  157 VSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFKD 236

                  .
gi 6755046   1262 K 1262
Cdd:PRK13646  237 K 237
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
1050-1260 1.21e-19

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 91.41  E-value: 1.21e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQlNVQWLRAHLGIVSQ----EPilfDCSI 1125
Cdd:PRK13537   22 VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVGVVPQfdnlDP---DFTV 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1126 AENIAYGDNSRAVSHEEIvrAAKEANIHQFIdSLPDKYNTRVGDkgtqLSGGQKQRIAIARALVRQPHILLLDEATSALD 1205
Cdd:PRK13537   98 RENLLVFGRYFGLSAAAA--RALVPPLLEFA-KLENKADAKVGE----LSGGMKRRLTLARALVNDPDVLVLDEPTTGLD 170
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 6755046   1206 TESEKVVQEALDK--AReGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLLA 1260
Cdd:PRK13537  171 PQARHLMWERLRSllAR-GKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHALIE 227
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
402-609 1.41e-19

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 92.60  E-value: 1.41e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    402 SRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIGVVSQEPVL-FA 480
Cdd:PRK09536   12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFE 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    481 TTIAENIRYGRED-----VTMDE-----IEKAVKEANAYDFIMKlphQFDTlvgergaqLSGGQKQRIAIARALVRNPKI 550
Cdd:PRK09536   92 FDVRQVVEMGRTPhrsrfDTWTEtdraaVERAMERTGVAQFADR---PVTS--------LSGGERQRVLLARALAQATPV 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6755046    551 LLLDEATSALDTESEA-VVQAALDKAREGRTTIVIAHRLS-TVRNADVIAGFDGGVIVEQG 609
Cdd:PRK09536  161 LLLDEPTASLDINHQVrTLELVRRLVDDGKTAVAAIHDLDlAARYCDELVLLADGRVRAAG 221
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
1051-1248 1.52e-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: 1.52e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    1051 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFY--DPMAGSVFLDGKEIKQLNVQWL-RAHLGIVSQEPILF-DCSIA 1126
Cdd:TIGR02633   17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSPLKASNIRDTeRAGIVIIHQELTLVpELSVA 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    1127 ENIAYGD----NSRAVSHEEIVRAAKEAnIHQFidSLPDKYNTR-VGDKGtqlsGGQKQRIAIARALVRQPHILLLDEAT 1201
Cdd:TIGR02633   97 ENIFLGNeitlPGGRMAYNAMYLRAKNL-LREL--QLDADNVTRpVGDYG----GGQQQLVEIAKALNKQARLLILDEPS 169
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 6755046    1202 SAL-DTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIENGK 1248
Cdd:TIGR02633  170 SSLtEKETEILLDIIRDLKAHGVACVYISHKLNEVKAvCDTICVIRDGQ 218
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
403-585 1.95e-19

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 88.01  E-value: 1.95e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    403 RSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVR----YLREIIGVvsqEPVL 478
Cdd:PRK13539   12 RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAeachYLGHRNAM---KPAL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    479 fatTIAENIR-----YGREDVTMDEiekavkeanAYDFiMKLPHQFDTlvgeRGAQLSGGQKQRIAIARALVRNPKILLL 553
Cdd:PRK13539   89 ---TVAENLEfwaafLGGEELDIAA---------ALEA-VGLAPLAHL----PFGYLSAGQKRRVALARLLVSNRPIWIL 151
                         170       180       190
                  ....*....|....*....|....*....|..
gi 6755046    554 DEATSALDTESEAVVqAALDKAREGRTTIVIA 585
Cdd:PRK13539  152 DEPTAALDAAAVALF-AELIRAHLAQGGIVIA 182
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
391-597 2.00e-19

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 93.46  E-value: 2.00e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    391 LEFKNVHFNYPSrseVQILKGLNLKVKSGQTVALVGNSGCGKSTtvqLMQRL-----YDPLEGVVSIDGQDIRTINVRYL 465
Cdd:PRK13549    6 LEMKNITKTFGG---VKALDNVSLKVRAGEIVSLCGENGAGKST---LMKVLsgvypHGTYEGEIIFEGEELQASNIRDT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    466 REI-IGVVSQEPVLFAT-TIAENIRYGREDVTMDEIEKAVKEANAYDFIMKLphQFDTLVGERGAQLSGGQKQRIAIARA 543
Cdd:PRK13549   80 ERAgIAIIHQELALVKElSVLENIFLGNEITPGGIMDYDAMYLRAQKLLAQL--KLDINPATPVGNLGLGQQQLVEIAKA 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 6755046    544 LVRNPKILLLDEATSALdTESEAVVQAAL--DKAREGRTTIVIAHRLSTVRN-ADVI 597
Cdd:PRK13549  158 LNKQARLLILDEPTASL-TESETAVLLDIirDLKAHGIACIYISHKLNEVKAiSDTI 213
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
391-609 2.08e-19

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 94.15  E-value: 2.08e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    391 LEFKNVHFNYPSRS--------EVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTIN- 461
Cdd:PRK10261  314 LQVRNLVTRFPLRSgllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSp 393
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    462 --VRYLREIIGVVSQEPvlFAT---------TIAENIRY--------GREDVTMDEIEKAVKEANAYDFimklPHQFdtl 522
Cdd:PRK10261  394 gkLQALRRDIQFIFQDP--YASldprqtvgdSIMEPLRVhgllpgkaAAARVAWLLERVGLLPEHAWRY----PHEF--- 464
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    523 vgergaqlSGGQKQRIAIARALVRNPKILLLDEATSALDTESEA-VVQAALDKARE-GRTTIVIAHRLSTV-RNADVIAG 599
Cdd:PRK10261  465 --------SGGQRQRICIARALALNPKVIIADEAVSALDVSIRGqIINLLLDLQRDfGIAYLFISHDMAVVeRISHRVAV 536
                         250
                  ....*....|
gi 6755046    600 FDGGVIVEQG 609
Cdd:PRK10261  537 MYLGQIVEIG 546
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
404-586 2.29e-19

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 88.30  E-value: 2.29e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    404 SEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVR---YLR-EIIGVVSQEPVLF 479
Cdd:PRK10584   21 HELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEaraKLRaKHVGFVFQSFMLI 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    480 ATTIAenirygREDVTMDEIEKAVKEANAYDFIMKLPHQFDtlVGER----GAQLSGGQKQRIAIARALVRNPKILLLDE 555
Cdd:PRK10584  101 PTLNA------LENVELPALLRGESSRQSRNGAKALLEQLG--LGKRldhlPAQLSGGEQQRVALARAFNGRPDVLFADE 172
                         170       180       190
                  ....*....|....*....|....*....|...
gi 6755046    556 ATSALDTES-EAVVQAALDKAREGRTT-IVIAH 586
Cdd:PRK10584  173 PTGNLDRQTgDKIADLLFSLNREHGTTlILVTH 205
ABC_6TM_MsbA_like cd18552
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ...
709-979 2.51e-19

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: 89.79  E-value: 2.51e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   709 LLVGVLCAVINGCIQPVFAIVFSRIVGVFSRDDDHETKRqncnLFSLFFLVMGLISFVTYFFQGFTFGKAGEILTKRVRY 788
Cdd:cd18552    1 LALAILGMILVAATTAALAWLLKPLLDDIFVEKDLEALL----LVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRN 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   789 MVFKSMLRQDISWFDdhKNSTGSLTTRLASDASSVKGAMGARLAVVTQNVANLGTGVILSLVYGWQLTLLLVVIIPLIVL 868
Cdd:cd18552   77 DLFDKLLRLPLSFFD--RNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAAL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   869 GGIIEMKLLSGQAlkdKKQLEISGKIAT---EAIENFRTIVSLTREQKFETMYAQSLQVPYRNAMKKAHVFGITFSFTQA 945
Cdd:cd18552  155 PIRRIGKRLRKIS---RRSQESMGDLTSvlqETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMEL 231
                        250       260       270
                 ....*....|....*....|....*....|....
gi 6755046   946 MMYFSYAACFRFGAYLVAQQLMTFENVMLVFSAV 979
Cdd:cd18552  232 LGAIAIALVLWYGGYQVISGELTPGEFISFITAL 265
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
1035-1261 2.68e-19

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 93.05  E-value: 2.68e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1035 FNGVQFNYPtrpNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQ-WLRAHLGI 1113
Cdd:PRK11288    7 FDGIGKTFP---GVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTaALAAGVAI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1114 VSQEPILF-DCSIAENIAYGD--NSRAVSHEEIVRA-AKEANIHQFIDSLPDkynTRVGDkgtqLSGGQKQRIAIARALV 1189
Cdd:PRK11288   84 IYQELHLVpEMTVAENLYLGQlpHKGGIVNRRLLNYeAREQLEHLGVDIDPD---TPLKY----LSIGQRQMVEIAKALA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1190 RQPHILLLDEATSALDT-ESE---KVVQEALDkarEGRTCIVIAHRLSTI-QNADLIVVIENG-KVKEHG-----THQQL 1258
Cdd:PRK11288  157 RNARVIAFDEPTSSLSArEIEqlfRVIRELRA---EGRVILYVSHRMEEIfALCDAITVFKDGrYVATFDdmaqvDRDQL 233

                  ...
gi 6755046   1259 LAQ 1261
Cdd:PRK11288  234 VQA 236
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
1033-1255 3.66e-19

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 90.66  E-value: 3.66e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1033 VKFNGVQFNYPTRPnipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQlNVQWLRAHLG 1112
Cdd:PRK13536   42 IDLAGVSKSYGDKA---VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIG 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1113 IVSQepilFD-----CSIAEN-IAYGDNSRaVSHEEIvraakEANIHQFID--SLPDKYNTRVGDkgtqLSGGQKQRIAI 1184
Cdd:PRK13536  118 VVPQ----FDnldleFTVRENlLVFGRYFG-MSTREI-----EAVIPSLLEfaRLESKADARVSD----LSGGMKRRLTL 183
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6755046   1185 ARALVRQPHILLLDEATSALDTESEKVVQEALDK--AReGRTCIVIAHRLSTIQN-ADLIVVIENG-KVKEHGTH 1255
Cdd:PRK13536  184 ARALINDPQLLILDEPTTGLDPHARHLIWERLRSllAR-GKTILLTTHFMEEAERlCDRLCVLEAGrKIAEGRPH 257
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
395-597 4.33e-19

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: 89.15  E-value: 4.33e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   395 NVHFNYPSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQdirtinvrylreiIGVVSQ 474
Cdd:cd03291   39 NLFFSNLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQ 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   475 EPVLFATTIAENIRYGredVTMDEI--EKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILL 552
Cdd:cd03291  106 FSWIMPGTIKENIIFG---VSYDEYryKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYL 182
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 6755046   553 LDEATSALD--TESEaVVQAALDKAREGRTTIVIAHRLSTVRNADVI 597
Cdd:cd03291  183 LDSPFGYLDvfTEKE-IFESCVCKLMANKTRILVTSKMEHLKKADKI 228
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
1050-1254 5.15e-19

ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 87.83  E-value: 5.15e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKeikqlnVQWLrahLGI-VSQEPILfdcSIAEN 1128
Cdd:COG1134   41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR------VSAL---LELgAGFHPEL---TGREN 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1129 I-----AYGdnsraVSHEEIVRAAKE----ANIHQFIDsLPDKYntrvgdkgtqLSGGQKQRIAIARALVRQPHILLLDE 1199
Cdd:COG1134  109 IylngrLLG-----LSRKEIDEKFDEivefAELGDFID-QPVKT----------YSSGMRARLAFAVATAVDPDILLVDE 172
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 6755046  1200 ATSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGT 1254
Cdd:COG1134  173 VLAVGDAAfQKKCLARIRELRESGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGD 229
SapF COG4167
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
391-615 5.24e-19

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


Pssm-ID: 443328 [Multi-domain]  Cd Length: 265  Bit Score: 88.36  E-value: 5.24e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   391 LEFKNVHFNYPSRS------EVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRY 464
Cdd:COG4167    5 LEVRNLSKTFKYRTglfrrqQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKY 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   465 ----LREI-------------IGVVSQEPVLFATTIAENIRYGRedvtmdeIEKAVKE-------ANAYdfimklPHQfd 520
Cdd:COG4167   85 rckhIRMIfqdpntslnprlnIGQILEEPLRLNTDLTAEEREER-------IFATLRLvgllpehANFY------PHM-- 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   521 tlvgergaqLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEA-VVQAALD-KAREGRTTIVIAHRLSTVRN-ADVI 597
Cdd:COG4167  150 ---------LSSGQKQRVALARALILQPKIIIADEALAALDMSVRSqIINLMLElQEKLGISYIYVSQHLGIVKHiSDKV 220
                        250
                 ....*....|....*...
gi 6755046   598 AGFDGGVIVEQGNHDELM 615
Cdd:COG4167  221 LVMHQGEVVEYGKTAEVF 238
SapF COG4167
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
1039-1261 5.44e-19

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


Pssm-ID: 443328 [Multi-domain]  Cd Length: 265  Bit Score: 88.36  E-value: 5.44e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1039 QFNYPT----RPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGIV 1114
Cdd:COG4167   13 TFKYRTglfrRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKYRCKHIRMI 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1115 SQEPilfdcsiaeNIAYgdNSRAvsheeivraakeaNIHQFIDsLPDKYNT----------------RVG-------DKG 1171
Cdd:COG4167   93 FQDP---------NTSL--NPRL-------------NIGQILE-EPLRLNTdltaeereerifatlrLVGllpehanFYP 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1172 TQLSGGQKQRIAIARALVRQPHILLLDEATSALD--TESEKV-----VQEaldkaREGRTCIVIAHRLSTIQN-ADLIVV 1243
Cdd:COG4167  148 HMLSSGQKQRVALARALILQPKIIIADEALAALDmsVRSQIInlmleLQE-----KLGISYIYVSQHLGIVKHiSDKVLV 222
                        250
                 ....*....|....*...
gi 6755046  1244 IENGKVKEHGTHQQLLAQ 1261
Cdd:COG4167  223 MHQGEVVEYGKTAEVFAN 240
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
398-618 5.94e-19

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 88.99  E-value: 5.94e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    398 FNYPSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTI----------------- 460
Cdd:PRK13651   12 FNKKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKkktkekekvleklviqk 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    461 -------NVRYLREIIGVVSQ--EPVLFATTIAENIRYGREDVTMDEiEKAVKEANAYDFIMKLPHQFDtlvgERGA-QL 530
Cdd:PRK13651   92 trfkkikKIKEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSK-EEAKKRAAKYIELVGLDESYL----QRSPfEL 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    531 SGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKA-REGRTTIVIAHRLSTV--RNADVIAGFDGGVIVE 607
Cdd:PRK13651  167 SGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLDNVleWTKRTIFFKDGKIIKD 246
                         250
                  ....*....|.
gi 6755046    608 QGNHDELMREK 618
Cdd:PRK13651  247 GDTYDILSDNK 257
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
1049-1261 6.39e-19

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 92.08  E-value: 6.39e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1049 PVLQGLSLEVKKGQTLALVGSSGCGKS-TVVQLLERFYDP----MAGSVFLDGKEIKQLNVQWLRAHLG----IVSQEPI 1119
Cdd:PRK15134   23 TVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQTLRGVRGnkiaMIFQEPM 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1120 L-------FDCSIAENIAYgdnSRAVSHE----EIVRAAKEANIHQfidslpdkYNTRVGDKGTQLSGGQKQRIAIARAL 1188
Cdd:PRK15134  103 VslnplhtLEKQLYEVLSL---HRGMRREaargEILNCLDRVGIRQ--------AAKRLTDYPHQLSGGERQRVMIAMAL 171
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6755046   1189 VRQPHILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTI-QNADLIVVIENGKVKEHGTHQQLLAQ 1261
Cdd:PRK15134  172 LTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVrKLADRVAVMQNGRCVEQNRAATLFSA 247
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
391-586 7.59e-19

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 87.83  E-value: 7.59e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    391 LEFKNVHFNYPSRSevqILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYlreiiG 470
Cdd:PRK11248    2 LQISHLYADYGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER-----G 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    471 VVSQ-EPVLFATTIAENIRYGREdvtMDEIEKAVKEANAYDFIMKlphqfdtlVGERGA------QLSGGQKQRIAIARA 543
Cdd:PRK11248   74 VVFQnEGLLPWRNVQDNVAFGLQ---LAGVEKMQRLEIAHQMLKK--------VGLEGAekryiwQLSGGQRQRVGIARA 142
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 6755046    544 LVRNPKILLLDEATSALDTESEAVVQAALDK--AREGRTTIVIAH 586
Cdd:PRK11248  143 LAANPQLLLLDEPFGALDAFTREQMQTLLLKlwQETGKQVLLITH 187
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
413-561 8.16e-19

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 86.94  E-value: 8.16e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    413 NLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRylREIIGVVSQEPVLFA-TTIAENIRYG- 490
Cdd:PRK10771   19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQENNLFShLTVAQNIGLGl 96
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6755046    491 --------REDVTMDEIEKAVkeaNAYDFIMKLPhqfdtlvgergAQLSGGQKQRIAIARALVRNPKILLLDEATSALD 561
Cdd:PRK10771   97 npglklnaAQREKLHAIARQM---GIEDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEPFSALD 161
ABC_6TM_exporter_like cd18563
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
124-336 8.87e-19

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: 88.34  E-value: 8.87e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   124 VLIVAYIQVSLWCLAAGRQ----------IHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDKIGMFF 193
Cdd:cd18563   46 VLGLAGAYVLSALLGILRGrllarlgeriTADLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFL 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   194 QSITTFLAGFIIGFISGWKLTLVILAVSPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQKEL 273
Cdd:cd18563  126 TNILMIIGIGVVLFSLNWKLALLVLIPVPLVVWGSYFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREI 205
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6755046   274 ERYNKNLEEAKNVGIKKAITASISIGIAYLLVYASYALAFWYGTSLVLSNEYSIGeVLTVFFS 336
Cdd:cd18563  206 KRFDEANQELLDANIRAEKLWATFFPLLTFLTSLGTLIVWYFGGRQVLSGTMTLG-TLVAFLS 267
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
391-609 9.19e-19

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: 86.18  E-value: 9.19e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   391 LEFKNVHFNYpsrSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINvrylREIIG 470
Cdd:cd03269    1 LEVENVTKRF---GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIG 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   471 VVSQEPVLF-ATTIAENIRY-GR-EDVTMDEIEKAVKEanaydFIMKL---PHQfdtlvGERGAQLSGGQKQRIAIARAL 544
Cdd:cd03269   74 YLPEERGLYpKMKVIDQLVYlAQlKGLKKEEARRRIDE-----WLERLelsEYA-----NKRVEELSKGNQQKVQFIAAV 143
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6755046   545 VRNPKILLLDEATSALDTES-EAVVQAALDKAREGRTTIVIAHRLSTV-RNADVIAGFDGGVIVEQG 609
Cdd:cd03269  144 IHDPELLILDEPFSGLDPVNvELLKDVIRELARAGKTVILSTHQMELVeELCDRVLLLNKGRAVLYG 210
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
391-617 9.61e-19

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


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 88.24  E-value: 9.61e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   391 LEFKNVHFNYpsrSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVR---YLRE 467
Cdd:COG4152    2 LELKGLTKRF---GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRrigYLPE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   468 iigvvsqEPVLFAT-TIAENIRY-GR-EDVTMDEIEKAVKEAnaydfimklphqFDTL-VGERGA----QLSGGQKQRIA 539
Cdd:COG4152   79 -------ERGLYPKmKVGEQLVYlARlKGLSKAEAKRRADEW------------LERLgLGDRANkkveELSKGNQQKVQ 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   540 IARALVRNPKILLLDEATSALDTES-EAVVQAALDKAREGRTTIVIAHRLSTV-RNADVIAGFDGGVIVEQGNHDELMRE 617
Cdd:COG4152  140 LIAALLHDPELLILDEPFSGLDPVNvELLKDVIRELAAKGTTVIFSSHQMELVeELCDRIVIINKGRKVLSGSVDEIRRQ 219
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
1051-1258 9.74e-19

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: 86.27  E-value: 9.74e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1051 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQlNVQWLRAHLGIVSQEPILFDCSIA-ENI 1129
Cdd:cd03265   16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLSVDDELTGwENL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1130 A-----YGdNSRAVSHEEIVRAAKEANIHQFIDSLPDKYntrvgdkgtqlSGGQKQRIAIARALVRQPHILLLDEATSAL 1204
Cdd:cd03265   95 YiharlYG-VPGAERRERIDELLDFVGLLEAADRLVKTY-----------SGGMRRRLEIARSLVHRPEVLFLDEPTIGL 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 6755046  1205 DTESEKVVQEALDK--AREGRTCIVIAHRLSTI-QNADLIVVIENGKVKEHGTHQQL 1258
Cdd:cd03265  163 DPQTRAHVWEYIEKlkEEFGMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPEEL 219
PvdE COG4615
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...
755-1251 1.24e-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: 91.01  E-value: 1.24e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   755 LFFLVMGLISFVTYFFQGFTFGKAGEILTKRVRYMVFKSMLRQDISWFDDHknSTGSLTTRLASDASSVKGAMGaRLAVV 834
Cdd:COG4615   52 LLFAGLLVLLLLSRLASQLLLTRLGQHAVARLRLRLSRRILAAPLERLERI--GAARLLAALTEDVRTISQAFV-RLPEL 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   835 TQNVANlgtgVILSLVY----GWQLTLLLVVIIPLIVLGGIIEMKLLsgqalkdKKQLEISGKIATEAIENFRTIVSLTR 910
Cdd:COG4615  129 LQSVAL----VLGCLAYlawlSPPLFLLTLVLLGLGVAGYRLLVRRA-------RRHLRRAREAEDRLFKHFRALLEGFK 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   911 EQKF-----ETMYAQSLQVP---YRNAMKKAHV-FGITFSFTQAMMYFSYAACFrfgaYLVAQQLMTFENVMLVFSAVV- 980
Cdd:COG4615  198 ELKLnrrrrRAFFDEDLQPTaerYRDLRIRADTiFALANNWGNLLFFALIGLIL----FLLPALGWADPAVLSGFVLVLl 273
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   981 FGAMAAGNTSSFAPDYAKAKVSASHIIRIIEKTPEIDSYSTEGLKPTLLEG--NVKFNGVQFNYPTRPNIP--VLQGLSL 1056
Cdd:COG4615  274 FLRGPLSQLVGALPTLSRANVALRKIEELELALAAAEPAAADAAAPPAPADfqTLELRGVTYRYPGEDGDEgfTLGPIDL 353
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1057 EVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDcsiaenIAYGdnsr 1136
Cdd:COG4615  354 TIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFD------RLLG---- 423
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1137 avsheeIVRAAKEANIHQFIDSL--PDKynTRVGDKG---TQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKV 1211
Cdd:COG4615  424 ------LDGEADPARARELLERLelDHK--VSVEDGRfstTDLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEFRRV 495
                        490       500       510       520
                 ....*....|....*....|....*....|....*....|...
gi 6755046  1212 VQEAL---DKAReGRTCIVIAHRLSTIQNADLIVVIENGKVKE 1251
Cdd:COG4615  496 FYTELlpeLKAR-GKTVIAISHDDRYFDLADRVLKMDYGKLVE 537
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
1050-1249 1.36e-18

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: 84.79  E-value: 1.36e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNV-QWLRAHLGIVSQEP----ILFDCS 1124
Cdd:cd03215   15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPrDAIRAGIAYVPEDRkregLVLDLS 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1125 IAENIAYGDnsravsheeivraakeanihqfidslpdkyntrvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEATSAL 1204
Cdd:cd03215   95 VAENIALSS---------------------------------------LLSGGNQQKVVLARWLARDPRVLILDEPTRGV 135
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 6755046  1205 DTES-EKVVQEALDKAREGRTCIVIahrlST-----IQNADLIVVIENGKV 1249
Cdd:cd03215  136 DVGAkAEIYRLIRELADAGKAVLLI----SSeldelLGLCDRILVMYEGRI 182
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
1050-1253 1.57e-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: 85.27  E-value: 1.57e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERF--YDPMAGSVFLDGKEIKQLNVQwLRAHLGI--VSQEPILFDcsi 1125
Cdd:cd03217   15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPE-ERARLGIflAFQYPPEIP--- 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1126 aeniaygdnsrAVSHEEIVRaakeanihqfidslpdkyNTRVGdkgtqLSGGQKQRIAIARALVRQPHILLLDEATSALD 1205
Cdd:cd03217   91 -----------GVKNADFLR------------------YVNEG-----FSGGEKKRNEILQLLLLEPDLAILDEPDSGLD 136
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 6755046  1206 TESEKVVQEALDKAR-EGRTCIVIAH--RLSTIQNADLIVVIENGKVKEHG 1253
Cdd:cd03217  137 IDALRLVAEVINKLReEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSG 187
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
407-620 1.77e-18

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 86.98  E-value: 1.77e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    407 QILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQ--DIRTINVRYLREIIGVVSQEP--VLFATT 482
Cdd:PRK13638   15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQVATVFQDPeqQIFYTD 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    483 IAENIRYGRED--VTMDEIEKAVKEANaydfimklphqfdTLVGERGAQ------LSGGQKQRIAIARALVRNPKILLLD 554
Cdd:PRK13638   95 IDSDIAFSLRNlgVPEAEITRRVDEAL-------------TLVDAQHFRhqpiqcLSHGQKKRVAIAGALVLQARYLLLD 161
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6755046    555 EATSALDTESEAVVQAALDK-AREGRTTIVIAHRLSTV----------RNADVIAGFDGGVIVEQGnhdELMREKGI 620
Cdd:PRK13638  162 EPTAGLDPAGRTQMIAIIRRiVAQGNHVIISSHDIDLIyeisdavyvlRQGQILTHGAPGEVFACT---EAMEQAGL 235
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
1050-1259 2.24e-18

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 86.58  E-value: 2.24e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGIVSQEPIL-FDCSIAEN 1128
Cdd:PRK10253   22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTpGDITVQEL 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1129 IAYG--------DNSRAVSHEEIVRAAKEANIHQFIDSLPDkyntrvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEA 1200
Cdd:PRK10253  102 VARGryphqplfTRWRKEDEEAVTKAMQATGITHLADQSVD-----------TLSGGQRQRAWIAMVLAQETAIMLLDEP 170
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6755046   1201 TSALDTESEKVVQEALDK--AREGRTCIVIAHRLS-TIQNADLIVVIENGKVKEHGTHQQLL 1259
Cdd:PRK10253  171 TTWLDISHQIDLLELLSElnREKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIV 232
ABC_6TM_Tm288_like cd18547
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ...
48-336 2.27e-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: 87.07  E-value: 2.27e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    48 LCMILGTLAAIIhgtlLPLLMlvfGNMTDSFTKAEASILPSITNQSGPNSTLIIsnssleeemAIYAyyytgIGAgvlIV 127
Cdd:cd18547    6 ILAIISTLLSVL----GPYLL---GKAIDLIIEGLGGGGGVDFSGLLRILLLLL---------GLYL-----LSA---LF 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   128 AYIQVslWCLA--AGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDKIGMFFQSITTFLAGFII 205
Cdd:cd18547   62 SYLQN--RLMArvSQRTVYDLRKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIM 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   206 GFISGWKLTLVILAVSPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQKELERYNKNLEEAKN 285
Cdd:cd18547  140 MLYISPLLTLIVLVTVPLSLLVTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYK 219
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 6755046   286 VGIKKAITASISIGIAYLLVYASYALAFWYGTSLVLSNEYSIGeVLTVFFS 336
Cdd:cd18547  220 ASFKAQFYSGLLMPIMNFINNLGYVLVAVVGGLLVINGALTVG-VIQAFLQ 269
cbiO PRK13645
energy-coupling factor transporter ATPase;
1031-1261 2.50e-18

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 86.99  E-value: 2.50e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1031 GNVKFNGVQFNYPTRP--NIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDG-------KEIKQ 1101
Cdd:PRK13645    5 KDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipanlKKIKE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1102 lnVQWLRAHLGIVSQEP--ILFDCSIAENIAYGDNSRAVSHEEIVRaakeaNIHQFID--SLPDKYNTRvgdKGTQLSGG 1177
Cdd:PRK13645   85 --VKRLRKEIGLVFQFPeyQLFQETIEKDIAFGPVNLGENKQEAYK-----KVPELLKlvQLPEDYVKR---SPFELSGG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1178 QKQRIAIARALVRQPHILLLDEATSALDTESEK---VVQEALDKaREGRTCIVIAHRLSTI-QNADLIVVIENGKVKEHG 1253
Cdd:PRK13645  155 QKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEdfiNLFERLNK-EYKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIG 233
                         250
                  ....*....|....
gi 6755046   1254 ------THQQLLAQ 1261
Cdd:PRK13645  234 spfeifSNQELLTK 247
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
1033-1231 2.60e-18

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: 83.36  E-value: 2.60e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1033 VKFNGVQFNYPTrpNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEikqlnvqwlraHLG 1112
Cdd:cd03223    1 IELENLSLATPD--GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGE-----------DLL 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1113 IVSQEPILFDCSIAENIAYgdnsravsheeivraakeanihqfidslPdkyntrvgdKGTQLSGGQKQRIAIARALVRQP 1192
Cdd:cd03223   68 FLPQRPYLPLGTLREQLIY----------------------------P---------WDDVLSGGEQQRLAFARLLLHKP 110
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 6755046  1193 HILLLDEATSALDTESEKVVQEALDKarEGRTCIVIAHR 1231
Cdd:cd03223  111 KFVFLDEATSALDEESEDRLYQLLKE--LGITVISVGHR 147
cbiO PRK13645
energy-coupling factor transporter ATPase;
386-636 2.99e-18

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 86.60  E-value: 2.99e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    386 SIMGNLEFKNVHFNYPSRS--EVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLydplegVVSIDGQDI------ 457
Cdd:PRK13645    2 DFSKDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGL------IISETGQTIvgdyai 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    458 -----RTINVRYLREIIGVVSQEP--VLFATTIAENIRYGREDVTMDEiEKAVKEANAYDFIMKLPHQFdtlVGERGAQL 530
Cdd:PRK13645   76 panlkKIKEVKRLRKEIGLVFQFPeyQLFQETIEKDIAFGPVNLGENK-QEAYKKVPELLKLVQLPEDY---VKRSPFEL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    531 SGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDK--AREGRTTIVIAHRLSTV-RNADVIAGFDGGVIVE 607
Cdd:PRK13645  152 SGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERlnKEYKKRIIMVTHNMDQVlRIADEVIVMHEGKVIS 231
                         250       260
                  ....*....|....*....|....*....
gi 6755046    608 QGNHDELMREKGIYFKLvmtqtrgnEIEP 636
Cdd:PRK13645  232 IGSPFEIFSNQELLTKI--------EIDP 252
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
391-613 3.15e-18

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 89.74  E-value: 3.15e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   391 LEFKNVHFNYPSRsevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIdGQdirtiNVRylreiIG 470
Cdd:COG0488  316 LELEGLSKSYGDK---TLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GE-----TVK-----IG 381
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   471 VVSQEPVLFAT--TIAENIRYGREDVTmdeiekavkEANAYDFIMKL---PHQFDTLVGErgaqLSGGQKQRIAIARALV 545
Cdd:COG0488  382 YFDQHQEELDPdkTVLDELRDGAPGGT---------EQEVRGYLGRFlfsGDDAFKPVGV----LSGGEKARLALAKLLL 448
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6755046   546 RNPKILLLDEATSALDTESEAVVQAALDkAREGrTTIVIAH-R--LSTVrnADVIAGFDGGVIVE-QGNHDE 613
Cdd:COG0488  449 SPPNVLLLDEPTNHLDIETLEALEEALD-DFPG-TVLLVSHdRyfLDRV--ATRILEFEDGGVREyPGGYDD 516
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
388-555 3.50e-18

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


Pssm-ID: 440752 [Multi-domain]  Cd Length: 240  Bit Score: 85.47  E-value: 3.50e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   388 MGNLEFKNVHFNYPSRsevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVrYLRE 467
Cdd:COG1137    1 MMTLEAENLVKSYGKR---TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPM-HKRA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   468 I--IGVVSQEPVLFAT-TIAENIRYGREDVTMDEIEKAvKEANAY--DF-IMKLPHQfdtlvgeRGAQLSGGQKQRIAIA 541
Cdd:COG1137   77 RlgIGYLPQEASIFRKlTVEDNILAVLELRKLSKKERE-ERLEELleEFgITHLRKS-------KAYSLSGGERRRVEIA 148
                        170
                 ....*....|....
gi 6755046   542 RALVRNPKILLLDE 555
Cdd:COG1137  149 RALATNPKFILLDE 162
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
391-561 4.23e-18

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 85.50  E-value: 4.23e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    391 LEFKNVHFNYPSRsevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTInvrylREIIG 470
Cdd:PRK11247   13 LLLNAVSKRYGER---TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEA-----REDTR 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    471 VVSQEPVLFA-TTIAENIRYGREDVTMDEIEKAVKEANAYDfimklphqfdtLVGERGAQLSGGQKQRIAIARALVRNPK 549
Cdd:PRK11247   85 LMFQDARLLPwKKVIDNVGLGLKGQWRDAALQALAAVGLAD-----------RANEWPAALSGGQKQRVALARALIHRPG 153
                         170
                  ....*....|..
gi 6755046    550 ILLLDEATSALD 561
Cdd:PRK11247  154 LLLLDEPLGALD 165
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
1053-1258 4.57e-18

leucine/isoleucine/valine transporter ATP-binding subunit; Provisional


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 85.43  E-value: 4.57e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1053 GLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLrAHLGIVS--QEPILF-DCSIAENI 1129
Cdd:PRK11300   23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQI-ARMGVVRtfQHVRLFrEMTVIENL 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1130 --------------------AYgdnsRAVSHEEIVRAAkeanihQFID--SLPDKYNTRVGDkgtqLSGGQKQRIAIARA 1187
Cdd:PRK11300  102 lvaqhqqlktglfsgllktpAF----RRAESEALDRAA------TWLErvGLLEHANRQAGN----LAYGQQRRLEIARC 167
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6755046   1188 LVRQPHILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQL 1258
Cdd:PRK11300  168 MVTQPEILMLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEI 241
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
1051-1258 5.08e-18

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 85.45  E-value: 5.08e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1051 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFY--DPMAGS-VFLDGKEIKQL-----NVQWLRAHLGIVSQEPILFD 1122
Cdd:PRK09984   20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgDKSAGShIELLGRTVQREgrlarDIRKSRANTGYIFQQFNLVN 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1123 -CSIAENIAYGDNSRAVSHEEIVRAAKEANIHQFIDSLpdkynTRVG------DKGTQLSGGQKQRIAIARALVRQPHIL 1195
Cdd:PRK09984  100 rLSVLENVLIGALGSTPFWRTCFSWFTREQKQRALQAL-----TRVGmvhfahQRVSTLSGGQQQRVAIARALMQQAKVI 174
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6755046   1196 LLDEATSALDTESEKVVQEALD--KAREGRTCIVIAHRLS-TIQNADLIVVIENGKVKEHGTHQQL 1258
Cdd:PRK09984  175 LADEPIASLDPESARIVMDTLRdiNQNDGITVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQF 240
ABC_6TM_YknU_like cd18542
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ...
709-1006 5.28e-18

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: 85.95  E-value: 5.28e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   709 LLVGVLCAVINGCIQPVFAIVFSRIVgvfsrdDD--HETKRQNCNLFSLFFLVMGLISFVTYFFQGFTFGKAGEILTKRV 786
Cdd:cd18542    1 YLLAILALLLATALNLLIPLLIRRII------DSviGGGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   787 RYMVFKSMLRQDISWFDdhKNSTGSLTTRLASDASSVKGAMGARLAVVTQNVANLGTGVILSLVYGWQLTLLLVVIIPLI 866
Cdd:cd18542   75 RNDLYDHLQRLSFSFHD--KARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFI 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   867 VLGGIIEMKLLSGQALKDKKQLEISGKIATEAIENFRTIVSLTRE----QKFETMYAQslqvpYRNA-MKKAHVFGITFS 941
Cdd:cd18542  153 ALFSYVFFKKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREdyeiEKFDKENEE-----YRDLnIKLAKLLAKYWP 227
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6755046   942 FTQAMMYFSYAACFRFGAYLVAQQLMTFENvMLVFSA----VVFGAMAAGNTSSfapDYAKAKVSASHI 1006
Cdd:cd18542  228 LMDFLSGLQIVLVLWVGGYLVINGEITLGE-LVAFISylwmLIWPVRQLGRLIN---DMSRASASAERI 292
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
391-617 5.52e-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: 89.09  E-value: 5.52e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     391 LEFKNVHFNYPS--RSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVS-------IDGQDIRTIN 461
Cdd:TIGR03269  280 IKVRNVSKRYISvdRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrvgdewVDMTKPGPDG 359
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     462 VRYLREIIGVVSQEPVLFA-TTIAENIRygrEDVTM---DEI--EKAV--------KEANAYDFIMKLPHQfdtlvgerg 527
Cdd:TIGR03269  360 RGRAKRYIGILHQEYDLYPhRTVLDNLT---EAIGLelpDELarMKAVitlkmvgfDEEKAEEILDKYPDE--------- 427
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     528 aqLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKARE--GRTTIVIAHRLSTVRN-ADVIAGFDGGV 604
Cdd:TIGR03269  428 --LSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDvCDRAALMRDGK 505
                          250
                   ....*....|...
gi 6755046     605 IVEQGNHDELMRE 617
Cdd:TIGR03269  506 IVKIGDPEEIVEE 518
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
412-609 5.63e-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: 5.63e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     412 LNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTiNVRYLREIIGVVSQEPVLFA-TTIAENIRYG 490
Cdd:TIGR01257  949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFHhLTVAEHILFY 1027
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     491 REdVTMDEIEKAVKEANAYDFIMKLPHQFDtlvgERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQA 570
Cdd:TIGR01257 1028 AQ-LKGRSWEEAQLEMEAMLEDTGLHHKRN----EEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWD 1102
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 6755046     571 ALDKAREGRTTIVIAHRLStvrNADVIAgfDGGVIVEQG 609
Cdd:TIGR01257 1103 LLLKYRSGRTIIMSTHHMD---EADLLG--DRIAIISQG 1136
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
402-585 5.95e-18

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: 83.56  E-value: 5.95e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     402 SRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIGVVSQEPVLFAT 481
Cdd:TIGR01189    9 SRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPEL 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     482 TIAENIRYGREDV--TMDEIEKAVKEANaydfimkLPHQFDTLVgergAQLSGGQKQRIAIARALVRNPKILLLDEATSA 559
Cdd:TIGR01189   89 SALENLHFWAAIHggAQRTIEDALAAVG-------LTGFEDLPA----AQLSAGQQRRLALARLWLSRRPLWILDEPTTA 157
                          170       180
                   ....*....|....*....|....*.
gi 6755046     560 LDTESEAVVQAALDkAREGRTTIVIA 585
Cdd:TIGR01189  158 LDKAGVALLAGLLR-AHLARGGIVLL 182
ABC_6TM_PCAT1_LagD_like cd18570
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ...
145-342 6.77e-18

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: 85.58  E-value: 6.77e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   145 KIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDdVSKINDGIGDKIGMFFQSITTFLAGFIIGFISGWKLTLVILAVSPLI 224
Cdd:cd18570   76 RLILGYFKHLLKLPLSFFETRKTGEIISRFND-ANKIREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPLY 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   225 GLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQKELERYNKNLEEAKNVGIKKAITASISIGIAYLL 304
Cdd:cd18570  155 ILIILLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLI 234
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 6755046   305 VYASYALAFWYGTSLVLSNEYSIGEVLTvfFSILLGTF 342
Cdd:cd18570  235 SLIGSLLILWIGSYLVIKGQLSLGQLIA--FNALLGYF 270
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
1040-1253 6.96e-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: 6.96e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1040 FNYPTRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKeikqlnVQW-LRAHLGIVSQ-- 1116
Cdd:cd03220   27 GRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR------VSSlLGLGGGFNPElt 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1117 --EPILFDCSIaeniaYGdnsraVSHEEIvrAAKEANIHQFIDsLPDKYNTRVGdkgtQLSGGQKQRIAIARALVRQPHI 1194
Cdd:cd03220  101 grENIYLNGRL-----LG-----LSRKEI--DEKIDEIIEFSE-LGDFIDLPVK----TYSSGMKARLAFAIATALEPDI 163
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6755046  1195 LLLDEATSALDTE-SEKVVQEALDKAREGRTCIVIAHRLSTI-QNADLIVVIENGKVKEHG 1253
Cdd:cd03220  164 LLIDEVLAVGDAAfQEKCQRRLRELLKQGKTVILVSHDPSSIkRLCDRALVLEKGKIRFDG 224
ABC_6TM_LmrA_like cd18551
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ...
755-1006 7.03e-18

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: 85.56  E-value: 7.03e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   755 LFFLVMGLISFVTYFFQGFTFGKAGEILTKRVRYMVFKSMLRQDISWFDdhKNSTGSLTTRLASDASSVKgamgarlAVV 834
Cdd:cd18551   40 ALLVALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWRRLLRLPVSFFD--RRRSGDLVSRVTNDTTLLR-------ELI 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   835 TQNVANLGTGVIL---SLV----YGWQLTLLLVVIIPLIVLGGIIEMKLLSGQALKDKKQL-EISGKIaTEAIENFRTIV 906
Cdd:cd18551  111 TSGLPQLVTGVLTvvgAVVlmflLDWVLTLVTLAVVPLAFLIILPLGRRIRKASKRAQDALgELSAAL-ERALSAIRTVK 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   907 SLTREQKFETMYAQSLQVPYRNAMKKAHVFGITFSFTQAMMYFSYAACFRFGAYLVAQ------QLMTFenVMLVFSAVv 980
Cdd:cd18551  190 ASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQLALLVVLGVGGARVASgaltvgTLVAF--LLYLFQLI- 266
                        250       260
                 ....*....|....*....|....*.
gi 6755046   981 fgaMAAGNTSSFAPDYAKAKVSASHI 1006
Cdd:cd18551  267 ---TPLSQLSSFFTQLQKALGALERI 289
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
1025-1258 7.50e-18

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 86.30  E-value: 7.50e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1025 KPTLLEgnVKFNGVQFN------YPTRP--NIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDG 1096
Cdd:PRK15079    5 KKVLLE--VADLKVHFDikdgkqWFWQPpkTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1097 KEI-KQLNVQWL--RAHLGIVSQEPILF---DCSIAENIA------YGDNSRAVSHEEiVRA--AKEANIHQFIDSLPDK 1162
Cdd:PRK15079   83 KDLlGMKDDEWRavRSDIQMIFQDPLASlnpRMTIGEIIAeplrtyHPKLSRQEVKDR-VKAmmLKVGLLPNLINRYPHE 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1163 YntrvgdkgtqlSGGQKQRIAIARALVRQPHILLLDEATSALDTESE-KVVQEALDKARE-GRTCIVIAHRLSTIQN-AD 1239
Cdd:PRK15079  162 F-----------SGGQCQRIGIARALILEPKLIICDEPVSALDVSIQaQVVNLLQQLQREmGLSLIFIAHDLAVVKHiSD 230
                         250
                  ....*....|....*....
gi 6755046   1240 LIVVIENGKVKEHGTHQQL 1258
Cdd:PRK15079  231 RVLVMYLGHAVELGTYDEV 249
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
391-617 7.68e-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: 83.35  E-value: 7.68e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   391 LEFKNVHFnypSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTtvqLMQRL-----YDPLEGVVSIDGQDIR--TINVR 463
Cdd:cd03217    1 LEIKDLHV---SVGGKEILKGVNLTIKKGEVHALMGPNGSGKST---LAKTImghpkYEVTEGEILFKGEDITdlPPEER 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   464 yLREIIGVVSQEPVLFA-TTIAENIRYgredvtmdeiekavkeanaydfimklphqfdtlVGErgaQLSGGQKQRIAIAR 542
Cdd:cd03217   75 -ARLGIFLAFQYPPEIPgVKNADFLRY---------------------------------VNE---GFSGGEKKRNEILQ 117
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6755046   543 ALVRNPKILLLDEATSALDTESEAVVQAALDKAR-EGRTTIVIAH--RLSTVRNADVIAGFDGGVIVEQGNhDELMRE 617
Cdd:cd03217  118 LLLLEPDLAILDEPDSGLDIDALRLVAEVINKLReEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGD-KELALE 194
ABC_6TM_ABCB9_like cd18784
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ...
753-971 7.90e-18

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: 85.44  E-value: 7.90e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   753 FSLFFLVMGLISFVTYFFQG-----FTFGKAGeiLTKRVRYMVFKSMLRQDISWFDdhKNSTGSLTTRLASDASSVKGAM 827
Cdd:cd18784   35 FSRAIIIMGLLAIASSVAAGirgglFTLAMAR--LNIRIRNLLFRSIVSQEIGFFD--TVKTGDITSRLTSDTTTMSDTV 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   828 GARLAVVTQNVANLGTGVILSLVYGWQLTLLLVVIIPLIVLGGIIEMKLLSGQALKDKKQLEISGKIATEAIENFRTIVS 907
Cdd:cd18784  111 SLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYYKKLSKAVQDSLAKANEVAEETISSIRTVRS 190
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6755046   908 LTREQKFETMYAQSLQVPYRNAMKKAHVFGiTFSFTQAMMYFS-YAACFRFGAYLVAQQLMTFEN 971
Cdd:cd18784  191 FANEDGEANRYSEKLKDTYKLKIKEALAYG-GYVWSNELTELAlTVSTLYYGGHLVITGQISGGN 254
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
391-617 8.96e-18

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 88.04  E-value: 8.96e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    391 LEFKNVHFNYPSrseVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVR-YLREII 469
Cdd:PRK11288    5 LSFDGIGKTFPG---VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTaALAAGV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    470 GVVSQE----PVLfatTIAENIRYGREDVTMDEIEKAVKEANAYDFIMKLPHQFD--TLVGErgaqLSGGQKQRIAIARA 543
Cdd:PRK11288   82 AIIYQElhlvPEM---TVAENLYLGQLPHKGGIVNRRLLNYEAREQLEHLGVDIDpdTPLKY----LSIGQRQMVEIAKA 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    544 LVRNPKILLLDEATSALDTESEAVVQAALDKAR-EGRTTIVIAHRLSTV-RNADVIAGF-DGGVI-----VEQGNHDELM 615
Cdd:PRK11288  155 LARNARVIAFDEPTSSLSAREIEQLFRVIRELRaEGRVILYVSHRMEEIfALCDAITVFkDGRYVatfddMAQVDRDQLV 234

                  ..
gi 6755046    616 RE 617
Cdd:PRK11288  235 QA 236
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
1045-1261 9.60e-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: 88.32  E-value: 9.60e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    1045 RPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSV-------FLDGKEIKQLNVQWLRAHLGIVSQE 1117
Cdd:TIGR03269  294 RGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdeWVDMTKPGPDGRGRAKRYIGILHQE 373
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    1118 PILF-DCSIAENIaygdnSRAVSHEEIVRAAKEANIHQF-IDSLPDKYNTRVGDKGT-QLSGGQKQRIAIARALVRQPHI 1194
Cdd:TIGR03269  374 YDLYpHRTVLDNL-----TEAIGLELPDELARMKAVITLkMVGFDEEKAEEILDKYPdELSEGERHRVALAQVLIKEPRI 448
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    1195 LLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLLAQ 1261
Cdd:TIGR03269  449 VILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIVEE 518
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
1049-1254 1.07e-17

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: 89.69  E-value: 1.07e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    1049 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIkQLNVQWLRAHLGIVSQEPILFD-CSIAE 1127
Cdd:TIGR01257  944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHhLTVAE 1022
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    1128 NIAYGDNSRAVSHEEiVRAAKEANIHQfiDSLPDKYNTRVGDkgtqLSGGQKQRIAIARALVRQPHILLLDEATSALDTE 1207
Cdd:TIGR01257 1023 HILFYAQLKGRSWEE-AQLEMEAMLED--TGLHHKRNEEAQD----LSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPY 1095
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 6755046    1208 SEKVVQEALDKAREGRTCIVIAHRLStiqNADL----IVVIENGKVKEHGT 1254
Cdd:TIGR01257 1096 SRRSIWDLLLKYRSGRTIIMSTHHMD---EADLlgdrIAIISQGRLYCSGT 1143
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
1033-1248 1.47e-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: 80.57  E-value: 1.47e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1033 VKFNGVQFNYPTRPnipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLErfydpmagsvfldGKeikqlnvqwLRAHLG 1112
Cdd:cd03221    1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIA-------------GE---------LEPDEG 55
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1113 IVSQEPILfdcsiaeNIAYgdnsravsheeivraakeanihqfidsLPdkyntrvgdkgtQLSGGQKQRIAIARALVRQP 1192
Cdd:cd03221   56 IVTWGSTV-------KIGY---------------------------FE------------QLSGGEKMRLALAKLLLENP 89
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 6755046  1193 HILLLDEATSALDTESEKVVQEALdKAREGrTCIVIAHRLSTIQN-ADLIVVIENGK 1248
Cdd:cd03221   90 NLLLLDEPTNHLDLESIEALEEAL-KEYPG-TVILVSHDRYFLDQvATKIIELEDGK 144
ABC_6TM_TmrA_like cd18544
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ...
709-969 1.81e-17

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: 84.36  E-value: 1.81e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   709 LLVGVLCAVINGCIQPVFAIVFSRIVgvfsrdDDHETKRQNC----NLFSLFFLVMGLISFVTYFFQGFTFGKAGEILTK 784
Cdd:cd18544    1 FILALLLLLLATALELLGPLLIKRAI------DDYIVPGQGDlqglLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   785 RVRYMVFKSMLRQDISWFDdhKNSTGSLTTRLASDASSVKGAMGARLAVVTQNVANLGTGVILSLVYGWQLTLLLVVIIP 864
Cdd:cd18544   75 DLRRDLFSHIQRLPLSFFD--RTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLP 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   865 LIVLGGIIEMKLLSGQALKDKKQL-EISGKIAtEAIENFRTIVSLTREQKFETMYAQSLQVPYRNAMKKAHVFGITFSFT 943
Cdd:cd18544  153 LLLLATYLFRKKSRKAYREVREKLsRLNAFLQ-ESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLV 231
                        250       260
                 ....*....|....*....|....*.
gi 6755046   944 QAMMYFSYAACFRFGAYLVAQQLMTF 969
Cdd:cd18544  232 ELLSSLALALVLWYGGGQVLSGAVTL 257
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
391-618 2.08e-17

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 85.27  E-value: 2.08e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    391 LEFKNVHFNYPSRSevqILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTiNVRYLREIIG 470
Cdd:PRK13536   42 IDLAGVSKSYGDKA---VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIG 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    471 VVSQEPVL-FATTIAEN-IRYGRE-DVTMDEIEKAVkeANAYDFiMKLPHQFDTLVgergAQLSGGQKQRIAIARALVRN 547
Cdd:PRK13536  118 VVPQFDNLdLEFTVRENlLVFGRYfGMSTREIEAVI--PSLLEF-ARLESKADARV----SDLSGGMKRRLTLARALIND 190
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6755046    548 PKILLLDEATSALDTESEAVVQAALDK--AReGRTTIVIAHRLSTV-RNADVIAGFDGGVIVEQGNHDELMREK 618
Cdd:PRK13536  191 PQLLILDEPTTGLDPHARHLIWERLRSllAR-GKTILLTTHFMEEAeRLCDRLCVLEAGRKIAEGRPHALIDEH 263
ABC_6TM_TAP2 cd18590
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ...
732-968 2.45e-17

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: 83.93  E-value: 2.45e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   732 RIVGVFSRDDDHetkrqncNLFSLFFLVMGLISFVTYFFQG-----FTFgkAGEILTKRVRYMVFKSMLRQDISWFDdhK 806
Cdd:cd18590   21 RVIDILGGEYQH-------NAFTSAIGLMCLFSLGSSLSAGlrgglFMC--TLSRLNLRLRHQLFSSLVQQDIGFFE--K 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   807 NSTGSLTTRLASDASSVKGAMGARLAVVTQN-VANLGT-GVILSLvyGWQLTLLLVVIIPLIVLggIIEMKLLSGQALKD 884
Cdd:cd18590   90 TKTGDLTSRLSTDTTLMSRSVALNANVLLRSlVKTLGMlGFMLSL--SWQLTLLTLIEMPLTAI--AQKVYNTYHQKLSQ 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   885 KKQLEI--SGKIATEAIENFRTIVSLTREQKFETMYAQSLQVPYRNAMKKAHVFGITFSFTQAMMYFSYAACFRFGAYLV 962
Cdd:cd18590  166 AVQDSIakAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTVRAVYLLVRRVLQLGVQVLMLYCGRQLI 245

                 ....*.
gi 6755046   963 AQQLMT 968
Cdd:cd18590  246 QSGHLT 251
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
402-566 2.54e-17

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: 81.77  E-value: 2.54e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   402 SRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIGVVSQEPVLFAT 481
Cdd:cd03231    9 ERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   482 TIAENIRYGREDVTMDEIEKAVKEANAYDFimklphqFDTLVgergAQLSGGQKQRIAIARALVRNPKILLLDEATSALD 561
Cdd:cd03231   89 SVLENLRFWHADHSDEQVEEALARVGLNGF-------EDRPV----AQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157

                 ....*
gi 6755046   562 TESEA 566
Cdd:cd03231  158 KAGVA 162
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
391-615 2.86e-17

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 84.09  E-value: 2.86e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    391 LEFKNVHFNYpsrSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTiNVRYLREIIG 470
Cdd:PRK13537    8 IDFRNVEKRY---GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    471 VVSQ----EPVLfatTIAENIR-YGRE-DVTMDEIEKAVkeANAYDFiMKLPHQFDTLVGErgaqLSGGQKQRIAIARAL 544
Cdd:PRK13537   84 VVPQfdnlDPDF---TVRENLLvFGRYfGLSAAAARALV--PPLLEF-AKLENKADAKVGE----LSGGMKRRLTLARAL 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6755046    545 VRNPKILLLDEATSALDTESEAVVQAALDK--AReGRTTIVIAHRLSTV-RNADVIAGFDGGVIVEQGNHDELM 615
Cdd:PRK13537  154 VNDPDVLVLDEPTTGLDPQARHLMWERLRSllAR-GKTILLTTHFMEEAeRLCDRLCVIEEGRKIAEGAPHALI 226
ABC_6TM_bac_exporter_ABCB8_10_like cd18575
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ...
752-992 3.76e-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: 83.30  E-value: 3.76e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   752 LFSLFFLVMGLISFVTYFFqgftFGKAGEILTKRVRYMVFKSMLRQDISWFDdhKNSTGSLTTRLASDASSVKGAMGARL 831
Cdd:cd18575   41 LLLAVALVLALASALRFYL----VSWLGERVVADLRKAVFAHLLRLSPSFFE--TTRTGEVLSRLTTDTTLIQTVVGSSL 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   832 AVVTQNVANLGTGVILSLVYGWQLTLLLVVIIPLIVLGGII---EMKLLSGQAlKDKkqLEISGKIATEAIENFRTIVSL 908
Cdd:cd18575  115 SIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILfgrRVRRLSRAS-QDR--LADLSAFAEETLSAIKTVQAF 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   909 TREQKFETMYAQSLQVPYRNAMKKAHvfgitfsftqammyfsyaacfrfgaylvAQQLMTFENVMLVFSAVVF------- 981
Cdd:cd18575  192 TREDAERQRFATAVEAAFAAALRRIR----------------------------ARALLTALVIFLVFGAIVFvlwlgah 243
                        250
                 ....*....|....*
gi 6755046   982 ----GAMAAGNTSSF 992
Cdd:cd18575  244 dvlaGRMSAGELSQF 258
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
397-584 3.84e-17

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: 82.38  E-value: 3.84e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   397 HFNYPSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIiGVV--SQ 474
Cdd:cd03267   25 SLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRI-GVVfgQK 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   475 EPVLFATTIAENIRYGRE--DVTMDEIEKAVKEANAydfIMKLPHQFDTLVgergAQLSGGQKQRIAIARALVRNPKILL 552
Cdd:cd03267  104 TQLWWDLPVIDSFYLLAAiyDLPPARFKKRLDELSE---LLDLEELLDTPV----RQLSLGQRMRAEIAAALLHEPEILF 176
                        170       180       190
                 ....*....|....*....|....*....|...
gi 6755046   553 LDEATSALDTESEAVVQAALDKA-REGRTTIVI 584
Cdd:cd03267  177 LDEPTIGLDVVAQENIRNFLKEYnRERGTTVLL 209
ABC_6TM_ABCB8_like cd18574
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ...
765-973 4.27e-17

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: 83.36  E-value: 4.27e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   765 FVTYFFQG-FTF------GKAGEILTKRVRYMVFKSMLRQDISWFDDHKnsTGSLTTRLASDASSVKGAMGarlAVVTQN 837
Cdd:cd18574   49 LGLYLLQSlLTFayisllSVVGERVAARLRNDLFSSLLRQDIAFFDTHR--TGELVNRLTADVQEFKSSFK---QCVSQG 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   838 VANLG--TGVILSLVY-GWQLTLLLVVIIPLIVLGGII---EMKLLSGQAlkdKKQLEISGKIATEAIENFRTIVSLTRE 911
Cdd:cd18574  124 LRSVTqtVGCVVSLYLiSPKLTLLLLVIVPVVVLVGTLygsFLRKLSRRA---QAQVAKATGVADEALGNIRTVRAFAME 200
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6755046   912 QKFETMYAQSLQvpyrNAMKKAHVFGITFSFTQAMMYFS---------YaacfrFGAYLVAQQLMTFENVM 973
Cdd:cd18574  201 DRELELYEEEVE----KAAKLNEKLGLGIGIFQGLSNLAlngivlgvlY-----YGGSLVSRGELTAGDLM 262
GguA NF040905
sugar ABC transporter ATP-binding protein;
1044-1251 4.45e-17

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 86.00  E-value: 4.45e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1044 TRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYdP---MAGSVFLDGKE-----IKQlnvqwlRAHLGIV- 1114
Cdd:NF040905   10 TFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PhgsYEGEILFDGEVcrfkdIRD------SEALGIVi 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1115 -SQE----PILfdcSIAENIAYGdNSRA----VSHEEIVRAAKE--ANIhqfidSLPDKYNTRVGDKGTqlsgGQKQRIA 1183
Cdd:NF040905   83 iHQElaliPYL---SIAENIFLG-NERAkrgvIDWNETNRRAREllAKV-----GLDESPDTLVTDIGV----GKQQLVE 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1184 IARALVRQPHILLLDEATSAL-DTESEKVVQEALDKAREGRTCIVIAHRLSTI-QNADLIVVIENGKVKE 1251
Cdd:NF040905  150 IAKALSKDVKLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIrRVADSITVLRDGRTIE 219
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
1049-1249 4.84e-17

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 85.84  E-value: 4.84e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1049 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNV-QWLRAHLGIVS----QEPILFDC 1123
Cdd:COG1129  266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPrDAIRAGIAYVPedrkGEGLVLDL 345
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1124 SIAENIAYGdNSRAVSHEEIVRAAKEANI-HQFIDSLpdkyNTRVGDKGT---QLSGGQKQRIAIARALVRQPHILLLDE 1199
Cdd:COG1129  346 SIRENITLA-SLDRLSRGGLLDRRRERALaEEYIKRL----RIKTPSPEQpvgNLSGGNQQKVVLAKWLATDPKVLILDE 420
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 6755046  1200 ATSALD--TESE--KVVQEAldkAREGRTCIVIahrlST-----IQNADLIVVIENGKV 1249
Cdd:COG1129  421 PTRGIDvgAKAEiyRLIREL---AAEGKAVIVI----SSelpelLGLSDRILVMREGRI 472
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
1033-1264 5.24e-17

high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 81.85  E-value: 5.24e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1033 VKFNGVQFNYPtrpNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLerFYDPMA--GSVFLDGKEIKQL-NVQWLRA 1109
Cdd:PRK11614    6 LSFDKVSAHYG---KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTL--CGDPRAtsGRIVFDGKDITDWqTAKIMRE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1110 HLGIVSQEPILFD-CSIAENIAYGD--NSRAVSHEEIVRAakeanihqfIDSLPDKYNTRVGDKGTqLSGGQKQRIAIAR 1186
Cdd:PRK11614   81 AVAIVPEGRRVFSrMTVEENLAMGGffAERDQFQERIKWV---------YELFPRLHERRIQRAGT-MSGGEQQMLAIGR 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1187 ALVRQPHILLLDEATSALdteSEKVVQEALDKAR----EGRTCIVIAHRLS-TIQNADLIVVIENGKVKEHGTHQQLLAQ 1261
Cdd:PRK11614  151 ALMSQPRLLLLDEPSLGL---APIIIQQIFDTIEqlreQGMTIFLVEQNANqALKLADRGYVLENGHVVLEDTGDALLAN 227

                  ...
gi 6755046   1262 KGI 1264
Cdd:PRK11614  228 EAV 230
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
391-586 8.33e-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: 78.64  E-value: 8.33e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   391 LEFKNVHFNYPSRsevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDgqdiRTINVRYLreiig 470
Cdd:cd03221    1 IELENLSKTYGGK---LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG----STVKIGYF----- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   471 vvsqepvlfattiaenirygredvtmdeiekavkeanaydfimklphqfdtlvgergAQLSGGQKQRIAIARALVRNPKI 550
Cdd:cd03221   69 ---------------------------------------------------------EQLSGGEKMRLALAKLLLENPNL 91
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 6755046   551 LLLDEATSALDTESEAVVQAALdKAREGrTTIVIAH 586
Cdd:cd03221   92 LLLDEPTNHLDLESIEALEEAL-KEYPG-TVILVSH 125
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
407-614 9.13e-17

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 85.14  E-value: 9.13e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    407 QILKGLNLKVKSGQTVALVGNSGCGKS-TTVQLMQRLYDP----LEGVVSIDGQDIRTINVRYLREI----IGVVSQEPV 477
Cdd:PRK15134   23 TVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQTLRGVrgnkIAMIFQEPM 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    478 LFAT---TIAENI-------RYGREDVTMDE---------IEKAVKEANAYdfimklPHQfdtlvgergaqLSGGQKQRI 538
Cdd:PRK15134  103 VSLNplhTLEKQLyevlslhRGMRREAARGEilncldrvgIRQAAKRLTDY------PHQ-----------LSGGERQRV 165
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6755046    539 AIARALVRNPKILLLDEATSALDTESEAVVQAALDKARE--GRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDEL 614
Cdd:PRK15134  166 MIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKlADRVAVMQNGRCVEQNRAATL 244
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
403-614 9.18e-17

The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 85.48  E-value: 9.18e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     403 RSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQ-LMQRLYDPLE--GVVSIDGqdiRTINVRYLREIIGVVSQEPVLF 479
Cdd:TIGR00955   35 RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNaLAFRSPKGVKgsGSVLLNG---MPIDAKEMRAISAYVQQDDLFI 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     480 AT-TIAENI------RYGReDVTMDEIEKAVKEanaydFI--MKLPHQFDTLVGERGAQ--LSGGQKQRIAIARALVRNP 548
Cdd:TIGR00955  112 PTlTVREHLmfqahlRMPR-RVTKKEKRERVDE-----VLqaLGLRKCANTRIGVPGRVkgLSGGERKRLAFASELLTDP 185
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6755046     549 KILLLDEATSALDTESEA-VVQAALDKAREGRTTIVIAHRLST--VRNADVIAGFDGGVIVEQGNHDEL 614
Cdd:TIGR00955  186 PLLFCDEPTSGLDSFMAYsVVQVLKGLAQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQA 254
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
391-614 9.79e-17

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 85.10  E-value: 9.79e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    391 LEFKNVHFNYpsrSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREI-I 469
Cdd:PRK15439   12 LCARSISKQY---SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLgI 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    470 GVVSQEPVLFAT-TIAENIRYG--REDVTMDEIEKAVKEANAYdfiMKLPHQFDTL-VGERgaqlsggqkQRIAIARALV 545
Cdd:PRK15439   89 YLVPQEPLLFPNlSVKENILFGlpKRQASMQKMKQLLAALGCQ---LDLDSSAGSLeVADR---------QIVEILRGLM 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6755046    546 RNPKILLLDEATSALD-TESEAV---VQAALDKareGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDEL 614
Cdd:PRK15439  157 RDSRILILDEPTASLTpAETERLfsrIRELLAQ---GVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADL 227
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
1048-1249 1.04e-16

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 84.72  E-value: 1.04e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1048 IPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKeiKQLNVQWLRAH-LGI--VSQEPILF-DC 1123
Cdd:PRK15439   24 VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGN--PCARLTPAKAHqLGIylVPQEPLLFpNL 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1124 SIAENIAYGDNSRAVSHEEIVRAAKEANIHQFIDSlpdkyntrvgdKGTQLSGGQKQRIAIARALVRQPHILLLDEATSA 1203
Cdd:PRK15439  102 SVKENILFGLPKRQASMQKMKQLLAALGCQLDLDS-----------SAGSLEVADRQIVEILRGLMRDSRILILDEPTAS 170
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 6755046   1204 LD-TESEKV---VQEALDKareGRTCIVIAHRLSTI-QNADLIVVIENGKV 1249
Cdd:PRK15439  171 LTpAETERLfsrIRELLAQ---GVGIVFISHKLPEIrQLADRISVMRDGTI 218
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
1033-1258 1.20e-16

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 81.74  E-value: 1.20e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1033 VKFNGVQFnypTRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWL---RA 1109
Cdd:PRK11831    8 VDMRGVSF---TRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRK 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1110 HLGIVSQEPILF-DCSIAENIAYGDNSRAVSHEEIVRAAKEANIHQfidslpdkyntrVGDKG------TQLSGGQKQRI 1182
Cdd:PRK11831   85 RMSMLFQSGALFtDMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEA------------VGLRGaaklmpSELSGGMARRA 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6755046   1183 AIARALVRQPHILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQL 1258
Cdd:PRK11831  153 ALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSalGVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQAL 231
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
1044-1229 1.62e-16

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 79.53  E-value: 1.62e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1044 TRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGIVSQ-EPILfd 1122
Cdd:PRK13539   11 VRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLGHRNAmKPAL-- 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1123 cSIAENIAYGDNSRAVSHEEIVRAAKEANIHQFIDsLPDKYntrvgdkgtqLSGGQKQRIAIARALVRQPHILLLDEATS 1202
Cdd:PRK13539   89 -TVAENLEFWAAFLGGEELDIAAALEAVGLAPLAH-LPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPTA 156
                         170       180
                  ....*....|....*....|....*..
gi 6755046   1203 ALDTESEKVVQEALdKAREGRTCIVIA 1229
Cdd:PRK13539  157 ALDAAAVALFAELI-RAHLAQGGIVIA 182
ABC_6TM_ABCB8_like cd18574
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ...
145-329 1.95e-16

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: 81.44  E-value: 1.95e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   145 KIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVskindgiGDKIGMFFQSITTFLAGF--IIG------FISGwKLTLV 216
Cdd:cd18574   76 RLRNDLFSSLLRQDIAFFDTHRTGELVNRLTADV-------QEFKSSFKQCVSQGLRSVtqTVGcvvslyLISP-KLTLL 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   217 ILAVSPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQKELERYNKNLEEAKN--------VGI 288
Cdd:cd18574  148 LLVIVPVVVLVGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYEEEVEKAAKlneklglgIGI 227
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 6755046   289 KKAITaSISIGIAYLLVYasyalafWYGTSLVLSNEYSIGE 329
Cdd:cd18574  228 FQGLS-NLALNGIVLGVL-------YYGGSLVSRGELTAGD 260
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
408-615 2.27e-16

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 80.80  E-value: 2.27e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    408 ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIGVVSQEPVLFA-TTIAEN 486
Cdd:PRK10253   22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGdITVQEL 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    487 IRYGREDVT------MDEIEKAVKEANAYDFIMKLPHQ-FDTlvgergaqLSGGQKQRIAIARALVRNPKILLLDEATSA 559
Cdd:PRK10253  102 VARGRYPHQplftrwRKEDEEAVTKAMQATGITHLADQsVDT--------LSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 6755046    560 LDTESEA-VVQAALDKARE-GRTTIVIAHRLS-TVRNADVIAGFDGGVIVEQGNHDELM 615
Cdd:PRK10253  174 LDISHQIdLLELLSELNREkGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIV 232
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
1045-1259 3.16e-16

The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 83.94  E-value: 3.16e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    1045 RPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLErFYDP----MAGSVFLDGKEIkqlNVQWLRAHLGIVSQEPIL 1120
Cdd:TIGR00955   35 RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPkgvkGSGSVLLNGMPI---DAKEMRAISAYVQQDDLF 110
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    1121 FDCSIA-ENIAYgdNSRAVSHEEIVRAAKEANIHQFID--SLPDKYNTRVGDKGTQ--LSGGQKQRIAIARALVRQPHIL 1195
Cdd:TIGR00955  111 IPTLTVrEHLMF--QAHLRMPRRVTKKEKRERVDEVLQalGLRKCANTRIGVPGRVkgLSGGERKRLAFASELLTDPPLL 188
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6755046    1196 LLDEATSALDTES-EKVVQEALDKAREGRTCIVIAHRLST--IQNADLIVVIENGKVKEHGTHQQLL 1259
Cdd:TIGR00955  189 FCDEPTSGLDSFMaYSVVQVLKGLAQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQAV 255
CeuD COG4604
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ...
1049-1254 3.53e-16

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


Pssm-ID: 443654 [Multi-domain]  Cd Length: 252  Bit Score: 79.74  E-value: 3.53e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1049 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGIVSQEP-ILFDCSIAE 1127
Cdd:COG4604   15 VVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILRQENhINSRLTVRE 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1128 NIAYG------------DnsravshEEIVRAAkeanIHQF-IDSLPDKYNTrvgdkgtQLSGGQKQRIAIARALVRQPHI 1194
Cdd:COG4604   95 LVAFGrfpyskgrltaeD-------REIIDEA----IAYLdLEDLADRYLD-------ELSGGQRQRAFIAMVLAQDTDY 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1195 LLLDEATSALD----TESEKVVQEAldkARE-GRTCIVIAHRLstiqN-----ADLIVVIENGKVKEHGT 1254
Cdd:COG4604  157 VLLDEPLNNLDmkhsVQMMKLLRRL---ADElGKTVVIVLHDI----NfascyADHIVAMKDGRVVAQGT 219
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
408-589 4.30e-16

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 79.09  E-value: 4.30e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    408 ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREI----IGVVSQEPVLFATTI 483
Cdd:PRK11629   24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELrnqkLGFIYQFHHLLPDFT 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    484 AenirygREDVTMDEI--EKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALD 561
Cdd:PRK11629  104 A------LENVAMPLLigKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLD 177
                         170       180       190
                  ....*....|....*....|....*....|
gi 6755046    562 TESEAVVQAALDK--AREGRTTIVIAHRLS 589
Cdd:PRK11629  178 ARNADSIFQLLGElnRLQGTAFLVVTHDLQ 207
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
1045-1258 4.31e-16

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 83.37  E-value: 4.31e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1045 RPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDG-------------KEIKQLNVQWLR-AH 1110
Cdd:PRK10261   26 QQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqvielSEQSAAQMRHVRgAD 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1111 LGIVSQEPI-----LFDC--SIAENIAYgdnSRAVSHEEIVRAAKeanihQFIDS--LPDKyNTRVGDKGTQLSGGQKQR 1181
Cdd:PRK10261  106 MAMIFQEPMtslnpVFTVgeQIAESIRL---HQGASREEAMVEAK-----RMLDQvrIPEA-QTILSRYPHQLSGGMRQR 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1182 IAIARALVRQPHILLLDEATSALDTESE-------KVVQEALDKAregrtCIVIAHRLSTIQN-ADLIVVIENGKVKEHG 1253
Cdd:PRK10261  177 VMIAMALSCRPAVLIADEPTTALDVTIQaqilqliKVLQKEMSMG-----VIFITHDMGVVAEiADRVLVMYQGEAVETG 251

                  ....*
gi 6755046   1254 THQQL 1258
Cdd:PRK10261  252 SVEQI 256
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
407-602 4.53e-16

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 78.76  E-value: 4.53e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    407 QILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDI---RTINVRYLREIIGVVSQE-------- 475
Cdd:PRK10908   16 QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlKNREVPFLRRQIGMIFQDhhllmdrt 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    476 -------PVLFATTIAENIRYgREDVTMDEIEKAVKEANaydfimkLPhqfdtlvgergAQLSGGQKQRIAIARALVRNP 548
Cdd:PRK10908   96 vydnvaiPLIIAGASGDDIRR-RVSAALDKVGLLDKAKN-------FP-----------IQLSGGEQQRVGIARAVVNKP 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 6755046    549 KILLLDEATSALDTE-SEAVVQAALDKAREGRTTIVIAHRLSTV--RNADVIAGFDG 602
Cdd:PRK10908  157 AVLLADEPTGNLDDAlSEGILRLFEEFNRVGVTVLMATHDIGLIsrRSYRMLTLSDG 213
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
388-610 5.48e-16

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 78.78  E-value: 5.48e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    388 MGNLEFKNVHFNYPSRsevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVR-YLR 466
Cdd:PRK10895    1 MATLTAKNLAKAYKGR---RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHaRAR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    467 EIIGVVSQEPVLFAT-TIAENIRYG---REDVTMDEIEKAVKEANAyDFimKLPHQFDTLvgerGAQLSGGQKQRIAIAR 542
Cdd:PRK10895   78 RGIGYLPQEASIFRRlSVYDNLMAVlqiRDDLSAEQREDRANELME-EF--HIEHLRDSM----GQSLSGGERRRVEIAR 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6755046    543 ALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRlsTVRnaDVIAGFDGGVIVEQGN 610
Cdd:PRK10895  151 ALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDH--NVR--ETLAVCERAYIVSQGH 214
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
1050-1216 7.70e-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: 77.53  E-value: 7.70e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAENI 1129
Cdd:cd03231   15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1130 AY--GDNSRavshEEIVRAAKEANIHQFIDsLPdkyntrvgdkGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTE 1207
Cdd:cd03231   95 RFwhADHSD----EQVEEALARVGLNGFED-RP----------VAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKA 159

                 ....*....
gi 6755046  1208 SEKVVQEAL 1216
Cdd:cd03231  160 GVARFAEAM 168
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
406-592 8.13e-16

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 82.14  E-value: 8.13e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    406 VQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREI-IGVVSQE-PVLFATTI 483
Cdd:PRK09700   18 VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLgIGIIYQElSVIDELTV 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    484 AENIRYGRE------DVTMDEIEKAVKEANAYDFIMKLPHQFDTLVGErgaqLSGGQKQRIAIARALVRNPKILLLDEAT 557
Cdd:PRK09700   98 LENLYIGRHltkkvcGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVAN----LSISHKQMLEIAKTLMLDAKVIIMDEPT 173
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 6755046    558 SALDTESEAVVQAALDKAR-EGRTTIVIAHRLSTVR 592
Cdd:PRK09700  174 SSLTNKEVDYLFLIMNQLRkEGTAIVYISHKLAEIR 209
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
1046-1248 9.43e-16

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 81.97  E-value: 9.43e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1046 PNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIK-------QlnvqwlRAHLGIVSQEP 1118
Cdd:PRK10762   15 PGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfngpkssQ------EAGIGIIHQEL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1119 ILFD-CSIAENIAYGdnsravshEEIVRAAKEAN---IHQFIDSLPDKYN------TRVGDkgtqLSGGQKQRIAIARAL 1188
Cdd:PRK10762   89 NLIPqLTIAENIFLG--------REFVNRFGRIDwkkMYAEADKLLARLNlrfssdKLVGE----LSIGEQQMVEIAKVL 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6755046   1189 VRQPHILLLDEATSAL-DTESE---KVVQEALDkarEGRTCIVIAHRLSTI-QNADLIVVIENGK 1248
Cdd:PRK10762  157 SFESKVIIMDEPTDALtDTETEslfRVIRELKS---QGRGIVYISHRLKEIfEICDDVTVFRDGQ 218
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
1049-1229 1.43e-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: 76.63  E-value: 1.43e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    1049 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAEN 1128
Cdd:TIGR01189   14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELSALEN 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    1129 IAYgdnsravsheeivraakEANIHQFIDSLPDKYNTRVGDKG------TQLSGGQKQRIAIARALVRQPHILLLDEATS 1202
Cdd:TIGR01189   94 LHF-----------------WAAIHGGAQRTIEDALAAVGLTGfedlpaAQLSAGQQRRLALARLWLSRRPLWILDEPTT 156
                          170       180
                   ....*....|....*....|....*..
gi 6755046    1203 ALDTESEKVVQEALDkAREGRTCIVIA 1229
Cdd:TIGR01189  157 ALDKAGVALLAGLLR-AHLARGGIVLL 182
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
395-616 1.54e-15

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 81.44  E-value: 1.54e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    395 NVHFNYpSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTIN--VRYLREI---- 468
Cdd:PRK10261   19 NIAFMQ-EQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSrqVIELSEQsaaq 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    469 --------IGVVSQEPV-----LFAT--TIAENIR----YGREDvtmdeiekAVKEANAYDFIMKLPhQFDTLVGERGAQ 529
Cdd:PRK10261   98 mrhvrgadMAMIFQEPMtslnpVFTVgeQIAESIRlhqgASREE--------AMVEAKRMLDQVRIP-EAQTILSRYPHQ 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    530 LSGGQKQRIAIARALVRNPKILLLDEATSALDTESEA-------VVQAALDKAregrtTIVIAHRLSTVRN-ADVIAGFD 601
Cdd:PRK10261  169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAqilqlikVLQKEMSMG-----VIFITHDMGVVAEiADRVLVMY 243
                         250
                  ....*....|....*
gi 6755046    602 GGVIVEQGNHDELMR 616
Cdd:PRK10261  244 QGEAVETGSVEQIFH 258
ABCG_PDR_domain2 cd03232
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...
391-609 2.05e-15

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: 76.13  E-value: 2.05e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   391 LEFKNVHFNYPS-RSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQ-LMQRLYDPL-EGVVSIDGQDIRtinvRYLRE 467
Cdd:cd03232    4 LTWKNLNYTVPVkGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDvLAGRKTAGViTGEILINGRPLD----KNFQR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   468 IIGVVSQEPVLFAT-TIAENIRygredvtmdeiekavkeanaydFIMKLphqfdtlvgeRGaqLSGGQKQRIAIARALVR 546
Cdd:cd03232   80 STGYVEQQDVHSPNlTVREALR----------------------FSALL----------RG--LSVEQRKRLTIGVELAA 125
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6755046   547 NPKILLLDEATSALDTESEAVVQAALDK-AREGRTTIVIAHRLStvrnADVIAGFDGGVIVEQG 609
Cdd:cd03232  126 KPSILFLDEPTSGLDSQAAYNIVRFLKKlADSGQAILCTIHQPS----ASIFEKFDRLLLLKRG 185
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
391-560 2.49e-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: 2.49e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    391 LEFKNVHFNYpsrSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTI-NVRYLREII 469
Cdd:PRK11614    6 LSFDKVSAHY---GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWqTAKIMREAV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    470 GVVSQEPVLFA-TTIAENIRYGREDVTMDEIEKAVKEAnaYDFimkLPHQFDTLVgERGAQLSGGQKQRIAIARALVRNP 548
Cdd:PRK11614   83 AIVPEGRRVFSrMTVEENLAMGGFFAERDQFQERIKWV--YEL---FPRLHERRI-QRAGTMSGGEQQMLAIGRALMSQP 156
                         170
                  ....*....|..
gi 6755046    549 KILLLDEATSAL 560
Cdd:PRK11614  157 RLLLLDEPSLGL 168
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
392-601 2.85e-15

Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 81.69  E-value: 2.85e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     392 EFKNVHFNYPSRSEV-QILKGLNLKVKSGQTVALVGNSGCGKSTtvqLMQRLYDPLEGVVSIDGqdIRTINVRYLRE--- 467
Cdd:TIGR00956  761 HWRNLTYEVKIKKEKrVILNNVDGWVKPGTLTALMGASGAGKTT---LLNVLAERVTTGVITGG--DRLVNGRPLDSsfq 835
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     468 -IIGVVSQEPVLFAT-TIAENIRYGREDVTMDEIEKavKEANAY-DFIMKL---PHQFDTLVGERGAQLSGGQKQRIAIA 541
Cdd:TIGR00956  836 rSIGYVQQQDLHLPTsTVRESLRFSAYLRQPKSVSK--SEKMEYvEEVIKLlemESYADAVVGVPGEGLNVEQRKRLTIG 913
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6755046     542 RALVRNPKILL-LDEATSALDTESEAVVQAALDK-AREGRTTIVIAHRLStvrnADVIAGFD 601
Cdd:TIGR00956  914 VELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKlADHGQAILCTIHQPS----AILFEEFD 971
ABC_6TM_exporter_like cd18565
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
50-344 3.42e-15

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: 77.99  E-value: 3.42e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    50 MILGTLAAIIhGTLLPLL-MLVFGNMTDSFTKAEASILPSITNQSGPNSTliisnsslEEEMAIYAYYYTGIGAGVLIVA 128
Cdd:cd18565    1 LVLGLLASIL-NRLFDLApPLLIGVAIDAVFNGEASFLPLVPASLGPADP--------RGQLWLLGGLTVAAFLLESLFQ 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   129 YIQVSLWCLAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDKIGMFFQSITTFLAGFIIGFI 208
Cdd:cd18565   72 YLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFY 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   209 SGWKLTLVILAVSPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQKELERYNKNLEE--AKNV 286
Cdd:cd18565  152 LNWQLALVALLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAEDFERERVADASEEyrDANW 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 6755046   287 GikkAITASIS-IGIAYLLVYASYALAFWYGTSLVLSNEYSIGEVLTVffsillGTFSI 344
Cdd:cd18565  232 R---AIRLRAAfFPVIRLVAGAGFVATFVVGGYWVLDGPPLFTGTLTV------GTLVT 281
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
399-617 4.93e-15

ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 76.27  E-value: 4.93e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   399 NYPSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGqdirtiNVRYLREIIGVVSQEpvl 478
Cdd:COG1134   32 RRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG------RVSALLELGAGFHPE--- 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   479 faTTIAENIR-----YGredVTMDEIEKAVKEANAY----DFImklphqfDTLVGergaQLSGGQKQRIAIARALVRNPK 549
Cdd:COG1134  103 --LTGRENIYlngrlLG---LSRKEIDEKFDEIVEFaelgDFI-------DQPVK----TYSSGMRARLAFAVATAVDPD 166
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6755046   550 ILLLDEATSALDTE----SEAVVQaalDKAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDELMRE 617
Cdd:COG1134  167 ILLVDEVLAVGDAAfqkkCLARIR---ELRESGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGDPEEVIAA 236
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
1047-1249 5.67e-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: 5.67e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1047 NIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL--ERfyDPMAGSVFLDGKEIKQLNVQWLRAH-LGIVSQEP----- 1118
Cdd:COG3845  270 GVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALagLR--PPASGSIRLDGEDITGLSPRERRRLgVAYIPEDRlgrgl 347
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1119 ILfDCSIAENIAYGD-NSRAVSHEEIVRAAKeanIHQFIDSLPDKYNTRVGDKGT---QLSGGQKQRIAIARALVRQPHI 1194
Cdd:COG3845  348 VP-DMSVAENLILGRyRRPPFSRGGFLDRKA---IRAFAEELIEEFDVRTPGPDTparSLSGGNQQKVILARELSRDPKL 423
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 6755046  1195 LLLDEATSALDTESEKVVQEALDKAR-EGRTCIVIAHRLSTIQN-ADLIVVIENGKV 1249
Cdd:COG3845  424 LIAAQPTRGLDVGAIEFIHQRLLELRdAGAAVLLISEDLDEILAlSDRIAVMYEGRI 480
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
1050-1270 5.74e-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: 79.46  E-value: 5.74e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERF--YDPMAGSVFLDGKEIKQLNVQWLRAHLG---------IVSQEP 1118
Cdd:TIGR03269   15 VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHVALCEKCGYVERPSKVGepcpvcggtLEPEEV 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    1119 ILFDCS------IAENIA---------YGDNSRAV----SHEEIVRAAKEAnIHQFIDSLPD-KYNTRVGDKGTQLSGGQ 1178
Cdd:TIGR03269   95 DFWNLSdklrrrIRKRIAimlqrtfalYGDDTVLDnvleALEEIGYEGKEA-VGRAVDLIEMvQLSHRITHIARDLSGGE 173
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    1179 KQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKA--REGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTH 1255
Cdd:TIGR03269  174 KQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvkASGISMVLTSHWPEVIEDlSDKAIWLENGEIKEEGTP 253
                          250
                   ....*....|....*
gi 6755046    1256 QQLLAQKGIYFSMVQ 1270
Cdd:TIGR03269  254 DEVVAVFMEGVSEVE 268
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
1027-1260 5.99e-15

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 76.37  E-value: 5.99e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1027 TLLEgnVKFNGVQFNYPT----RPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQL 1102
Cdd:PRK15112    3 TLLE--VRNLSKTFRYRTgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1103 NVQWLRAHLGIVSQEPI-----------LFDCSIAENIAYGDNSRAvshEEIVRAAKEANIhqfidsLPDKYNTRvgdkG 1171
Cdd:PRK15112   81 DYSYRSQRIRMIFQDPStslnprqrisqILDFPLRLNTDLEPEQRE---KQIIETLRQVGL------LPDHASYY----P 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1172 TQLSGGQKQRIAIARALVRQPHILLLDEATSALD-TESEKVVQEALD-KAREGRTCIVIAHRLSTIQN-ADLIVVIENGK 1248
Cdd:PRK15112  148 HMLAPGQKQRLGLARALILRPKVIIADEALASLDmSMRSQLINLMLElQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGE 227
                         250
                  ....*....|..
gi 6755046   1249 VKEHGTHQQLLA 1260
Cdd:PRK15112  228 VVERGSTADVLA 239
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
408-614 7.73e-15

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 76.29  E-value: 7.73e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    408 ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGV-----VSIDGQDIRTI-NVRYLREIIGVVSQEPVLFAT 481
Cdd:PRK14271   36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYrysgdVLLGGRSIFNYrDVLEFRRRVGMLFQRPNPFPM 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    482 TIAENIRYGREDVTMDEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALD 561
Cdd:PRK14271  116 SIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALD 195
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 6755046    562 TESEAVVQAALDKAREGRTTIVIAHRLS-TVRNADVIAGFDGGVIVEQGNHDEL 614
Cdd:PRK14271  196 PTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQL 249
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
391-606 8.34e-15

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 77.07  E-value: 8.34e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    391 LEFKN--VHFNYPSrSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTV-QLMQRLYDP--LEGVVSIDGQDIRTINVRYL 465
Cdd:PRK09473   13 LDVKDlrVTFSTPD-GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAfALMGLLAANgrIGGSATFNGREILNLPEKEL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    466 REI----IGVVSQEPVlfaTTIAENIRYG-------------------REDVTMDEiekAVKEANAYDFIMKLPHQFdtl 522
Cdd:PRK09473   92 NKLraeqISMIFQDPM---TSLNPYMRVGeqlmevlmlhkgmskaeafEESVRMLD---AVKMPEARKRMKMYPHEF--- 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    523 vgergaqlSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDK-AREGRTTIV-IAHRLStvrnadVIAGF 600
Cdd:PRK09473  163 --------SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNElKREFNTAIImITHDLG------VVAGI 228

                  ....*.
gi 6755046    601 DGGVIV 606
Cdd:PRK09473  229 CDKVLV 234
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
1040-1253 8.56e-15

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 79.13  E-value: 8.56e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1040 FNYPTRpNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLN---VQWLRAHLGIVSQ 1116
Cdd:PRK10261  330 LNRVTR-EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQ 408
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1117 EPIlfdCSIAENIAYGDnsravSHEEIVRaakeanIHQFIDSLPDKYNT-----RVGDKGT-------QLSGGQKQRIAI 1184
Cdd:PRK10261  409 DPY---ASLDPRQTVGD-----SIMEPLR------VHGLLPGKAAAARVawlleRVGLLPEhawryphEFSGGQRQRICI 474
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6755046   1185 ARALVRQPHILLLDEATSALDTE-SEKVVQEALDKARE-GRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHG 1253
Cdd:PRK10261  475 ARALALNPKVIIADEAVSALDVSiRGQIINLLLDLQRDfGIAYLFISHDMAVVERiSHRVAVMYLGQIVEIG 546
ABC_6TM_Tm288_like cd18547
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ...
709-969 1.03e-14

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: 76.29  E-value: 1.03e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   709 LLVGVLCAVINGCIQPVFAIVFSRIVGVFSRDDDHETKRQNCNLFS--LFFLVMGLISFVTYFFQGFTFGKAGEILTKRV 786
Cdd:cd18547    1 LILVIILAIISTLLSVLGPYLLGKAIDLIIEGLGGGGGVDFSGLLRilLLLLGLYLLSALFSYLQNRLMARVSQRTVYDL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   787 RYMVFKSMLRQDISWFDdhKNSTGSLTTRLASDASSVKGAMGARLAVVTQNVANLGTGVILSLVYGWQLTLLLVVIIPLI 866
Cdd:cd18547   81 RKDLFEKLQRLPLSYFD--THSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLS 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   867 VLGgiieMKLLSGQALKD-KKQLEISGKI---ATEAIENFRTIVSLTRE----QKFETMYAQslqvpYRNAMKKAHVF-G 937
Cdd:cd18547  159 LLV----TKFIAKRSQKYfRKQQKALGELngyIEEMISGQKVVKAFNREeeaiEEFDEINEE-----LYKASFKAQFYsG 229
                        250       260       270
                 ....*....|....*....|....*....|..
gi 6755046   938 ITFSFTQAMMYFSYAACFRFGAYLVAQQLMTF 969
Cdd:cd18547  230 LLMPIMNFINNLGYVLVAVVGGLLVINGALTV 261
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
407-561 1.11e-14

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 77.22  E-value: 1.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    407 QILKGLNLKVK-----SGQTvALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQ---DI-RTINVRYLREIIGVVSQEPV 477
Cdd:PRK11144    8 QQLGDLCLTVNltlpaQGIT-AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAeKGICLPPEKRRIGYVFQDAR 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    478 LFA-TTIAENIRYGredvtMDEIEKAvkeanaydfimklphQFDTLVGERG---------AQLSGGQKQRIAIARALVRN 547
Cdd:PRK11144   87 LFPhYKVRGNLRYG-----MAKSMVA---------------QFDKIVALLGieplldrypGSLSGGEKQRVAIGRALLTA 146
                         170
                  ....*....|....
gi 6755046    548 PKILLLDEATSALD 561
Cdd:PRK11144  147 PELLLMDEPLASLD 160
GguA NF040905
sugar ABC transporter ATP-binding protein;
406-597 1.11e-14

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 78.29  E-value: 1.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    406 VQILKGLNLKVKSGQTVALVGNSGCGKSTtvqLMQRL-----YDPLEGVVSIDGQ-----DIRTinvrylREIIGVV--S 473
Cdd:NF040905   14 VKALDDVNLSVREGEIHALCGENGAGKST---LMKVLsgvypHGSYEGEILFDGEvcrfkDIRD------SEALGIViiH 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    474 QE----PVLfatTIAENIRYGREDVTMDEI--EKAVKEANAYDFIMKLPHQFDTLVGERGAqlsgGQKQRIAIARALVRN 547
Cdd:NF040905   85 QElaliPYL---SIAENIFLGNERAKRGVIdwNETNRRARELLAKVGLDESPDTLVTDIGV----GKQQLVEIAKALSKD 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 6755046    548 PKILLLDEATSAL-DTESEAVVQAALDKAREGRTTIVIAHRLSTVRN-ADVI 597
Cdd:NF040905  158 VKLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIRRvADSI 209
PvdE COG4615
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...
114-555 1.49e-14

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: 78.30  E-value: 1.49e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   114 AYYYTGIGAGVLIVAYIQvslwclaagRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDkIGMFF 193
Cdd:COG4615   60 LLLLSRLASQLLLTRLGQ---------HAVARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQAFVR-LPELL 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   194 QSITTFLAGFI-IGFISgWKLTLVILAVSPLIGLSSALwakvLTSFTNKELQayaKAGAVAEEVLAAIRTVIafGGQqKE 272
Cdd:COG4615  130 QSVALVLGCLAyLAWLS-PPLFLLTLVLLGLGVAGYRL----LVRRARRHLR---RAREAEDRLFKHFRALL--EGF-KE 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   273 L------------ERYNKNLEEAKNVGIKKAITASISIGIAYLLVYASYALAFWYGTSLVLSNeysiGEVLTVFFSILLg 340
Cdd:COG4615  199 LklnrrrrraffdEDLQPTAERYRDLRIRADTIFALANNWGNLLFFALIGLILFLLPALGWAD----PAVLSGFVLVLL- 273
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   341 tFSIGHLAP---NIEAFANARgAAFEifKI------IDNEPSIDSFSTKGyKPDSIMGNLEFKNVHFNYPSRSEVQ--IL 409
Cdd:COG4615  274 -FLRGPLSQlvgALPTLSRAN-VALR--KIeelelaLAAAEPAAADAAAP-PAPADFQTLELRGVTYRYPGEDGDEgfTL 348
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   410 KGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTiaenirY 489
Cdd:COG4615  349 GPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFDRL------L 422
                        410       420       430       440       450       460       470
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6755046   490 GREDVTMDEiekavkEANAYDFIMKLPH-------QFDTLvgergaQLSGGQKQRIAIARALVRNPKILLLDE 555
Cdd:COG4615  423 GLDGEADPA------RARELLERLELDHkvsvedgRFSTT------DLSQGQRKRLALLVALLEDRPILVFDE 483
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
376-609 1.56e-14

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: 74.11  E-value: 1.56e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   376 SFSTKGYKPDSIMgnleFKNVHFNYPSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQ 455
Cdd:cd03220    9 SYPTYKGGSSSLK----KLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   456 dirtinVRYLREI-IGVvsqEPVLfatTIAENIR-----YGREDVTMDEIEKAVKE-ANAYDFImklphqfDTLVGErga 528
Cdd:cd03220   85 ------VSSLLGLgGGF---NPEL---TGRENIYlngrlLGLSRKEIDEKIDEIIEfSELGDFI-------DLPVKT--- 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   529 qLSGGQKQRIAIARALVRNPKILLLDEATSALDtesEAVVQAALDKARE----GRTTIVIAHRLSTVRN-ADVIAGFDGG 603
Cdd:cd03220  143 -YSSGMKARLAFAIATALEPDILLIDEVLAVGD---AAFQEKCQRRLREllkqGKTVILVSHDPSSIKRlCDRALVLEKG 218

                 ....*.
gi 6755046   604 VIVEQG 609
Cdd:cd03220  219 KIRFDG 224
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
1051-1247 1.63e-14

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 77.90  E-value: 1.63e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1051 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQwLRAHLG--IVSQEPILFD-CSIAE 1127
Cdd:PRK09700   21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHK-LAAQLGigIIYQELSVIDeLTVLE 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1128 NIAYGDN-SRAVSHEEIVRAAK---EANIHQFIDSLPDKYNTRVGDkgtqLSGGQKQRIAIARALVRQPHILLLDEATSA 1203
Cdd:PRK09700  100 NLYIGRHlTKKVCGVNIIDWREmrvRAAMMLLRVGLKVDLDEKVAN----LSISHKQMLEIAKTLMLDAKVIIMDEPTSS 175
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 6755046   1204 L-DTESEKVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIENG 1247
Cdd:PRK09700  176 LtNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRiCDRYTVMKDG 221
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
391-615 1.71e-14

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 75.21  E-value: 1.71e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    391 LEFKNVH--FNYPS----RSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRY 464
Cdd:PRK15112    5 LEVRNLSktFRYRTgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSY 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    465 LREIIGVVSQEPvlfATTIAENIRYGR---------EDVTMDEIEKAVKE-----------ANAYdfimklPHQfdtlvg 524
Cdd:PRK15112   85 RSQRIRMIFQDP---STSLNPRQRISQildfplrlnTDLEPEQREKQIIEtlrqvgllpdhASYY------PHM------ 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    525 ergaqLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEA-VVQAALD-KAREGRTTIVIAHRLSTVRN-ADVIAGFD 601
Cdd:PRK15112  150 -----LAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSqLINLMLElQEKQGISYIYVTQHLGMMKHiSDQVLVMH 224
                         250
                  ....*....|....
gi 6755046    602 GGVIVEQGNHDELM 615
Cdd:PRK15112  225 QGEVVERGSTADVL 238
PRK10522 PRK10522
multidrug transporter membrane component/ATP-binding component; Provisional
1035-1261 2.00e-14

multidrug transporter membrane component/ATP-binding component; Provisional


Pssm-ID: 236707 [Multi-domain]  Cd Length: 547  Bit Score: 77.70  E-value: 2.00e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1035 FNGVQFNYPTrPNIPVlQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGIV 1114
Cdd:PRK10522  325 LRNVTFAYQD-NGFSV-GPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAV 402
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1115 SQEPILFDcsiaeniaygdnsRAVSHEEivRAAKEANIHQFIDSLPDKYNTRVGD---KGTQLSGGQKQRIAIARALVRQ 1191
Cdd:PRK10522  403 FTDFHLFD-------------QLLGPEG--KPANPALVEKWLERLKMAHKLELEDgriSNLKLSKGQKKRLALLLALAEE 467
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6755046   1192 PHILLLDEATSALDTESEKVV-QEALDKARE-GRTCIVIAHRLSTIQNADLIVVIENGKVKE-HGTHQQLLAQ 1261
Cdd:PRK10522  468 RDILLLDEWAADQDPHFRREFyQVLLPLLQEmGKTIFAISHDDHYFIHADRLLEMRNGQLSElTGEERDAASR 540
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
1051-1259 2.11e-14

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 74.58  E-value: 2.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1051 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWL----RAHL-----GIVSQEP--- 1118
Cdd:PRK11701   22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseaeRRRLlrtewGFVHQHPrdg 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1119 ILFDCSIAENI-----AYGDNsravsHEEIVRAAKEANIHQF-IDSlpdkynTRVGDKGTQLSGGQKQRIAIARALVRQP 1192
Cdd:PRK11701  102 LRMQVSAGGNIgerlmAVGAR-----HYGDIRATAGDWLERVeIDA------ARIDDLPTTFSGGMQQRLQIARNLVTHP 170
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6755046   1193 HILLLDEATSALDTEsekvVQ-EALDKARE-----GRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLL 1259
Cdd:PRK11701  171 RLVFMDEPTGGLDVS----VQaRLLDLLRGlvrelGLAVVIVTHDLAVARLlAHRLLVMKQGRVVESGLTDQVL 240
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
406-634 2.28e-14

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: 77.56  E-value: 2.28e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     406 VQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLY--DPLEGVVSIDGQDIRTINVRYL-REIIGVVSQEPVLFAT- 481
Cdd:TIGR02633   14 VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSPLKASNIRDTeRAGIVIIHQELTLVPEl 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     482 TIAENIRYGRE----DVTMDEIEkAVKEANAYDFIMKLPHQFDTL-VGERGaqlsGGQKQRIAIARALVRNPKILLLDEA 556
Cdd:TIGR02633   94 SVAENIFLGNEitlpGGRMAYNA-MYLRAKNLLRELQLDADNVTRpVGDYG----GGQQQLVEIAKALNKQARLLILDEP 168
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6755046     557 TSAL-DTESEAVVQAALDKAREGRTTIVIAHRLSTVRnadviAGFDGGVIVEQGNHDELMREKGIYFKLVMTQTRGNEI 634
Cdd:TIGR02633  169 SSSLtEKETEILLDIIRDLKAHGVACVYISHKLNEVK-----AVCDTICVIRDGQHVATKDMSTMSEDDIITMMVGREI 242
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
406-638 2.35e-14

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: 77.54  E-value: 2.35e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     406 VQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRL--YDPLEGVV----------------SIDGQ------------ 455
Cdd:TIGR03269   13 KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgyverpSKVGEpcpvcggtlepe 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     456 --DIRTINVRYLREIIGVVSqepVLFATTIAeniRYGREDV------TMDEIEKAVKEA--NAYDFI--MKLPHQFDTLV 523
Cdd:TIGR03269   93 evDFWNLSDKLRRRIRKRIA---IMLQRTFA---LYGDDTVldnvleALEEIGYEGKEAvgRAVDLIemVQLSHRITHIA 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     524 GErgaqLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKA--REGRTTIVIAHRLSTVRN-ADVIAGF 600
Cdd:TIGR03269  167 RD----LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvkASGISMVLTSHWPEVIEDlSDKAIWL 242
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 6755046     601 DGGVIVEQGNHDELMrekGIYFKLVMTQTRGNEIEPGN 638
Cdd:TIGR03269  243 ENGEIKEEGTPDEVV---AVFMEGVSEVEKECEVEVGE 277
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
1025-1259 3.30e-14

Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 74.05  E-value: 3.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1025 KPTLLEGNVKFNGVQFNYPTRPnipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNV 1104
Cdd:PRK10575    4 YTNHSDTTFALRNVSFRVPGRT---LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1105 QWLRAHLGIVSQE-PILFDCSIAENIA------------YGDNSRAVSHEEIVRAAKEANIHQFIDSlpdkyntrvgdkg 1171
Cdd:PRK10575   81 KAFARKVAYLPQQlPAAEGMTVRELVAigrypwhgalgrFGAADREKVEEAISLVGLKPLAHRLVDS------------- 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1172 tqLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAhRLSTIQNA----DLIVVIENG 1247
Cdd:PRK10575  148 --LSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIA-VLHDINMAarycDYLVALRGG 224
                         250
                  ....*....|..
gi 6755046   1248 KVKEHGTHQQLL 1259
Cdd:PRK10575  225 EMIAQGTPAELM 236
ABC_6TM_TAP1 cd18589
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ...
109-332 3.94e-14

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: 74.43  E-value: 3.94e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   109 EMAIYayYYTG--------------IGAGVLIVAYIQVS----------LWCLAAGRQIHKIRQKFFHAIMNQEIGWFDV 164
Cdd:cd18589   12 EMAIP--YYTGrmtdwimnkdapeaFTAAITVMSLLTIAsavsefvcdlIYNITMSRIHSRLQGLVFAAVLRQEIAFFDS 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   165 HDVGELNTRLTDDVSKINDGIGDKIGMFFQSITTFLAGFIIGFISGWKLTLVILAVSPLIGLSSALWAKVLTSFTNKELQ 244
Cdd:cd18589   90 NQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQQSLAVQVQK 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   245 AYAKAGAVAEEVLAAIRTVIAFGGQQKELERYNKNLEEAKNVGIKKAITASISIGIAYLLVYASYALAFWYGTSLVLSNE 324
Cdd:cd18589  170 SLARANQVAVETFSAMKTVRSFANEEGEAQRYRQRLQKTYRLNKKEAAAYAVSMWTSSFSGLALKVGILYYGGQLVTAGT 249

                 ....*...
gi 6755046   325 YSIGEVLT 332
Cdd:cd18589  250 VSSGDLVT 257
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
1048-1249 4.06e-14

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: 73.52  E-value: 4.06e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1048 IPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGkeikqlNVQW-----LRAHLGIV--SQEPIL 1120
Cdd:cd03267   34 VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG------LVPWkrrkkFLRRIGVVfgQKTQLW 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1121 FDCSIAENIAYgdnsravsHEEIVRAaKEANIHQFIDSLPDKYN-TRVGDKGT-QLSGGQKQRIAIARALVRQPHILLLD 1198
Cdd:cd03267  108 WDLPVIDSFYL--------LAAIYDL-PPARFKKRLDELSELLDlEELLDTPVrQLSLGQRMRAEIAAALLHEPEILFLD 178
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 6755046  1199 EATSALDTESEKVVQEALDKAREGR--TCIVIAHRLSTIQN-ADLIVVIENGKV 1249
Cdd:cd03267  179 EPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEAlARRVLVIDKGRL 232
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
418-610 5.14e-14

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: 70.87  E-value: 5.14e-14
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046      418 SGQTVALVGNSGCGKSTTVQ-LMQRLYDPLEGVVSIDGQDIRTINVRYLREIIgvvsqepvlfattiaenirygredvtm 496
Cdd:smart00382    1 PGEVILIVGPPGSGKTTLARaLARELGPPGGGVIYIDGEDILEEVLDQLLLII--------------------------- 53
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046      497 deiekavkeanaydfimklphqfdtlVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALD--- 573
Cdd:smart00382   54 --------------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrl 107
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|.
gi 6755046      574 ----KAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGN 610
Cdd:smart00382  108 llllKSEKNLTVILTTNDEKDLGPALLRRRFDRRIVLLLIL 148
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
397-587 6.35e-14

ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 72.30  E-value: 6.35e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   397 HFNYPSRS-EVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLY--DPLEGVVSIDGQDIrtinvrylreiigvvS 473
Cdd:COG2401   33 AFGVELRVvERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQF---------------G 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   474 QEpvlfaTTIAENIryGREDVTMDEIE--KAVKEANAYDFIMKLPHqfdtlvgergaqLSGGQKQRIAIARALVRNPKIL 551
Cdd:COG2401   98 RE-----ASLIDAI--GRKGDFKDAVEllNAVGLSDAVLWLRRFKE------------LSTGQKFRFRLALLLAERPKLL 158
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 6755046   552 LLDEATSALDTESEAVVQAALDK-AREGRTTIVIA-HR 587
Cdd:COG2401  159 VIDEFCSHLDRQTAKRVARNLQKlARRAGITLVVAtHH 196
ABC_6TM_Tm287_like cd18548
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ...
146-342 7.79e-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: 73.59  E-value: 7.79e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   146 IRQKFFHAIMNqeigwFDVHDVGE-----LNTRLTDDVSKINDGIGDKIGMFFQSITTFLAGFIIGFISGWKLTLVILAV 220
Cdd:cd18548   74 LRKDLFEKIQS-----FSFAEIDKfgtssLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVA 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   221 SPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQKELERYNKNLEEAKNVGIKKAITASISIGI 300
Cdd:cd18548  149 IPILALVVFLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPL 228
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 6755046   301 AYLLVYASYALAFWYGTSLVLSNEYSIGEV-------LTVFFSILLGTF 342
Cdd:cd18548  229 MMLIMNLAIVAILWFGGHLINAGSLQVGDLvafinylMQILMSLMMLSM 277
ycf16 CHL00131
sulfate ABC transporter protein; Validated
1047-1254 7.85e-14

sulfate ABC transporter protein; Validated


Pssm-ID: 214372 [Multi-domain]  Cd Length: 252  Bit Score: 72.75  E-value: 7.85e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1047 NIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERF--YDPMAGSVFLDGKEIKQLNVQwLRAHLGI--VSQEPIlfd 1122
Cdd:CHL00131   19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEPE-ERAHLGIflAFQYPI--- 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1123 cSIAeniaygdnsrAVSHEEIVRAA----------KEANIHQFIDSLPDKYNTrVGDKGTQL--------SGGQKQRIAI 1184
Cdd:CHL00131   95 -EIP----------GVSNADFLRLAynskrkfqglPELDPLEFLEIINEKLKL-VGMDPSFLsrnvnegfSGGEKKRNEI 162
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6755046   1185 ARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIV-IAH--RLSTIQNADLIVVIENGKVKEHGT 1254
Cdd:CHL00131  163 LQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIIlITHyqRLLDYIKPDYVHVMQNGKIIKTGD 235
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
1054-1253 8.60e-14

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 74.53  E-value: 8.60e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1054 LSLEVK-----KGQTlALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEI----KQLNVQWLRAHLGIVSQEPILF-DC 1123
Cdd:PRK11144   13 LCLTVNltlpaQGIT-AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLfdaeKGICLPPEKRRIGYVFQDARLFpHY 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1124 SIAENIAYG-DNSRAVSHEEIVRAAKeanihqfIDSLPDKYNTRvgdkgtqLSGGQKQRIAIARALVRQPHILLLDEATS 1202
Cdd:PRK11144   92 KVRGNLRYGmAKSMVAQFDKIVALLG-------IEPLLDRYPGS-------LSGGEKQRVAIGRALLTAPELLLMDEPLA 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 6755046   1203 ALDTESEKVVQEALDK-AREGRTCIV-IAHRLSTI-QNADLIVVIENGKVKEHG 1253
Cdd:PRK11144  158 SLDLPRKRELLPYLERlAREINIPILyVSHSLDEIlRLADRVVVLEQGKVKAFG 211
ABC_6TM_exporter_like cd18550
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
143-340 9.60e-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: 73.29  E-value: 9.60e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   143 IHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDKIGMFFQSITTFLAGFIIGFISGWKLTLVILAVSP 222
Cdd:cd18550   71 MYDLRVQLYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLP 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   223 LIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAA--IRTVIAFGGQQKELERYNKNLEEAKNVGIKKAITASISIGI 300
Cdd:cd18550  151 LFVLPTRRVGRRRRKLTREQQEKLAELNSIMQETLSVsgALLVKLFGREDDEAARFARRSRELRDLGVRQALAGRWFFAA 230
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 6755046   301 AYLLVYASYALAFWYGTSLVLSNEYSIGEVltVFFSILLG 340
Cdd:cd18550  231 LGLFTAIGPALVYWVGGLLVIGGGLTIGTL--VAFTALLG 268
3a01203 TIGR00954
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...
1014-1233 1.01e-13

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: 75.94  E-value: 1.01e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    1014 PEIDSYSTEGLKPTLLEGN----VKFNGVQF-NYP--TRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD 1086
Cdd:TIGR00954  424 EEIESGREGGRNSNLVPGRgiveYQDNGIKFeNIPlvTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWP 503
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    1087 PMAGSVFLDGKeikqlnvqwlrAHLGIVSQEPILFDCSIAENIAYGDNS-----RAVSHEEIVRAAKEANIHQFIdslpd 1161
Cdd:TIGR00954  504 VYGGRLTKPAK-----------GKLFYVPQRPYMTLGTLRDQIIYPDSSedmkrRGLSDKDLEQILDNVQLTHIL----- 567
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6755046    1162 kynTR------VGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAreGRTCIVIAHRLS 1233
Cdd:TIGR00954  568 ---EReggwsaVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREF--GITLFSVSHRKS 640
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
393-585 1.02e-13

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: 71.14  E-value: 1.02e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   393 FKNVHFNYP-SRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTtvqLMQRL------YDPLEGVVSIDGQDIRTINVRYL 465
Cdd:cd03233    6 WRNISFTTGkGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCST---LLKALanrtegNVSVEGDIHYNGIPYKEFAEKYP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   466 REIIgVVSQEPVLFAT-TIAEnirygredvTMDeiekAVKEANAYDFImklphqfdtlvgeRGaqLSGGQKQRIAIARAL 544
Cdd:cd03233   83 GEII-YVSEEDVHFPTlTVRE---------TLD----FALRCKGNEFV-------------RG--ISGGERKRVSIAEAL 133
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 6755046   545 VRNPKILLLDEATSALDTESeavvqaALD-------KAREGRTTIVIA 585
Cdd:cd03233  134 VSRASVLCWDNSTRGLDSST------ALEilkcirtMADVLKTTTFVS 175
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
1050-1264 1.37e-13

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 71.85  E-value: 1.37e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQwLRAHLGI--VSQEPilfdcSIAE 1127
Cdd:PRK10895   18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLH-ARARRGIgyLPQEA-----SIFR 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1128 NIAYGDNSRAV--------SHEEIVRAAK---EANIHQFIDSLpdkyntrvgdkGTQLSGGQKQRIAIARALVRQPHILL 1196
Cdd:PRK10895   92 RLSVYDNLMAVlqirddlsAEQREDRANElmeEFHIEHLRDSM-----------GQSLSGGERRRVEIARALAANPKFIL 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1197 LDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRL-STIQNADLIVVIENGKVKEHGTHQQLLAQKGI 1264
Cdd:PRK10895  161 LDEPFAGVDPISVIDIKRIIEHLRDsGLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQDEHV 230
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
409-603 1.42e-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: 70.15  E-value: 1.42e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   409 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREI-IGVVSQEPV---LFAT-TI 483
Cdd:cd03215   16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVPEDRKregLVLDlSV 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   484 AENIrygredvtmdeiekavkeanaydfimklphqfdTLvgerGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTE 563
Cdd:cd03215   96 AENI---------------------------------AL----SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVG 138
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 6755046   564 SEAVVQAALDK-AREGRTTIVIAHRLSTV-RNADVIAGFDGG 603
Cdd:cd03215  139 AKAEIYRLIRElADAGKAVLLISSELDELlGLCDRILVMYEG 180
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
1044-1249 1.59e-13

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 74.77  E-value: 1.59e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1044 TRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLN-----------VQWLRAHLG 1112
Cdd:PRK10982  257 TSLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNaneainhgfalVTEERRSTG 336
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1113 IVSQEPILFDCSIAENIAYGDNSRAVSHEEIvraakEANIHQFIDSLPDK---YNTRVGdkgtQLSGGQKQRIAIARALV 1189
Cdd:PRK10982  337 IYAYLDIGFNSLISNIRNYKNKVGLLDNSRM-----KSDTQWVIDSMRVKtpgHRTQIG----SLSGGNQQKVIIGRWLL 407
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6755046   1190 RQPHILLLDEATSALDTESE-KVVQEALDKAREGRTCIVIAHRLSTIQN-ADLIVVIENGKV 1249
Cdd:PRK10982  408 TQPEILMLDEPTRGIDVGAKfEIYQLIAELAKKDKGIIIISSEMPELLGiTDRILVMSNGLV 469
hmuV PRK13547
heme ABC transporter ATP-binding protein;
397-616 1.86e-13

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 72.17  E-value: 1.86e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    397 HFNYPSRSEVqILKGLNLKVKSGQTVALVGNSGCGKSTTVQ-LMQRLYDP-------LEGVVSIDGQDIRTINVRYLREI 468
Cdd:PRK13547    6 HLHVARRHRA-ILRDLSLRIEPGRVTALLGRNGAGKSTLLKaLAGDLTGGgaprgarVTGDVTLNGEPLAAIDAPRLARL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    469 IGVVSQ--EPVlFATTIAENIRYGR----------EDVTMDEIEKAVKEANAydfimklphqfDTLVGERGAQLSGGQKQ 536
Cdd:PRK13547   85 RAVLPQaaQPA-FAFSAREIVLLGRypharragalTHRDGEIAWQALALAGA-----------TALVGRDVTTLSGGELA 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    537 RIAIARAL---------VRNPKILLLDEATSALDTESE----AVVQAALDKAREGRTTIVIAHRLSTvRNADVIAGFDGG 603
Cdd:PRK13547  153 RVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQhrllDTVRRLARDWNLGVLAIVHDPNLAA-RHADRIAMLADG 231
                         250
                  ....*....|...
gi 6755046    604 VIVEQGNHDELMR 616
Cdd:PRK13547  232 AIVAHGAPADVLT 244
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
412-617 2.16e-13

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 71.50  E-value: 2.16e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    412 LNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYdPLEGVVSIDGQDIRTINVRYLREIIGVVSQE-PVLFATTIAENI-RY 489
Cdd:PRK03695   15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRAYLSQQqTPPFAMPVFQYLtLH 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    490 GREDVTMDEIEKAVKE-ANAYDFIMKLPhqfdTLVGergaQLSGGQKQRIAIARALVR-----NP--KILLLDEATSALD 561
Cdd:PRK03695   94 QPDKTRTEAVASALNEvAEALGLDDKLG----RSVN----QLSGGEWQRVRLAAVVLQvwpdiNPagQLLLLDEPMNSLD 165
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6755046    562 TESeavvQAALDK-----AREGRTTIVIAHRLS-TVRNADVIAGFDGGVIVEQGNHDELMRE 617
Cdd:PRK03695  166 VAQ----QAALDRllselCQQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVLTP 223
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
408-616 2.33e-13

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 71.65  E-value: 2.33e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    408 ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDP----LEGVVSIDGQDIRTINVRylREIIGVVSQEP------- 476
Cdd:PRK10418   18 LVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPCALR--GRKIATIMQNPrsafnpl 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    477 VLFATTIAENIR-YGRE--DVTMDEIEKAVKEANAyDFIMKLpHQFdtlvgergaQLSGGQKQRIAIARALVRNPKILLL 553
Cdd:PRK10418   96 HTMHTHARETCLaLGKPadDATLTAALEAVGLENA-ARVLKL-YPF---------EMSGGMLQRMMIALALLCEAPFIIA 164
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    554 DEATSALDteseAVVQA-ALD-----KAREGRTTIVIAHRLSTV-RNADVIAGFDGGVIVEQGNHDELMR 616
Cdd:PRK10418  165 DEPTTDLD----VVAQArILDllesiVQKRALGMLLVTHDMGVVaRLADDVAVMSHGRIVEQGDVETLFN 230
ABC_6TM_YknV_like cd18545
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ...
117-334 2.72e-13

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: 72.12  E-value: 2.72e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   117 YTGIGAGVLIVAYIQVSLWCLAAGRQ----------IHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIG 186
Cdd:cd18545   36 LSGLLIIALLFLALNLVNWVASRLRIylmakvgqriLYDLRQDLFSHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLS 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   187 DKIGMFFQSITTFLAGFIIGFISGWKLTLVILAVSPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAF 266
Cdd:cd18545  116 NGLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVVFLLRRRARKAWQRVRKKISNLNAYLHESISGIRVIQSF 195
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6755046   267 GGQQKELERYNKNLEEAKNVGIKKAITASI---SIGIAYLLvyaSYALAFWYGTSLVLSNEYSIGeVLTVF 334
Cdd:cd18545  196 AREDENEEIFDELNRENRKANMRAVRLNALfwpLVELISAL---GTALVYWYGGKLVLGGAITVG-VLVAF 262
sufC PRK09580
cysteine desulfurase ATPase component; Reviewed
391-611 4.08e-13

cysteine desulfurase ATPase component; Reviewed


Pssm-ID: 181965 [Multi-domain]  Cd Length: 248  Bit Score: 70.59  E-value: 4.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    391 LEFKNVHFnypSRSEVQILKGLNLKVKSGQTVALVGNSGCGKST-TVQLMQRL-YDPLEGVVSIDGQDIRTIN------- 461
Cdd:PRK09580    2 LSIKDLHV---SVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTlSATLAGREdYEVTGGTVEFKGKDLLELSpedrage 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    462 -----VRYLREIIGVVSQepvLFATTIAENIRYGREDVTMDEIEKAvkeanayDFI------MKLPHqfDTLVGERGAQL 530
Cdd:PRK09580   79 gifmaFQYPVEIPGVSNQ---FFLQTALNAVRSYRGQEPLDRFDFQ-------DLMeekialLKMPE--DLLTRSVNVGF 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    531 SGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREG-RTTIVIAH--RLSTVRNADVIAGFDGGVIVE 607
Cdd:PRK09580  147 SGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGkRSFIIVTHyqRILDYIKPDYVHVLYQGRIVK 226

                  ....
gi 6755046    608 QGNH 611
Cdd:PRK09580  227 SGDF 230
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
1049-1231 4.67e-13

ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 69.99  E-value: 4.67e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1049 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFY--DPMAGSVFLDGKEIKQlnvqwlrahlgivsqepilfDCSIA 1126
Cdd:COG2401   44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQFGR--------------------EASLI 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1127 ENIA-YGDNSRAVsheEIVRAAKeanihqfidsLPDKYNTRVgdKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALD 1205
Cdd:COG2401  104 DAIGrKGDFKDAV---ELLNAVG----------LSDAVLWLR--RFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLD 168
                        170       180
                 ....*....|....*....|....*...
gi 6755046  1206 TESEKVVQEALDKA--REGRTCIVIAHR 1231
Cdd:COG2401  169 RQTAKRVARNLQKLarRAGITLVVATHH 196
ABC_6TM_Tm287_like cd18548
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ...
755-1006 4.68e-13

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: 71.28  E-value: 4.68e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   755 LFFLVMGLISFVTYFFQGFTFGKAGEILTKRVRYMVFKSMLRQDISWFDdhKNSTGSLTTRLASDASSVKGA--MGARLA 832
Cdd:cd18548   43 LLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFEKIQSFSFAEID--KFGTSSLITRLTNDVTQVQNFvmMLLRML 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   833 VVTqnVANLGTGVILSLVYGWQLTLLLVVIIPLIVLGGIIEMKLLSGQALKDKKQLEISGKIATEAIENFRTIVSLTRE- 911
Cdd:cd18548  121 VRA--PIMLIGAIIMAFRINPKLALILLVAIPILALVVFLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREd 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   912 ---QKFETMYAQslqvpYRNAMKKA-HVFGITFSFTQAMMYFSYAACFRFGAYLVAQQLMTFENVMLVFS---AVVFGAM 984
Cdd:cd18548  199 yeeERFDKANDD-----LTDTSLKAgRLMALLNPLMMLIMNLAIVAILWFGGHLINAGSLQVGDLVAFINylmQILMSLM 273
                        250       260
                 ....*....|....*....|..
gi 6755046   985 AAGNTSSFAPdyaKAKVSASHI 1006
Cdd:cd18548  274 MLSMVFVMLP---RASASAKRI 292
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
1049-1253 8.23e-13

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 69.73  E-value: 8.23e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1049 PVLQGLSLEVKKGQTLALVGSSGCGKS----TVVQLLERFYDPMAGSVFLDGKEIKQlnvQWLRA-HLGIVSQEP----- 1118
Cdd:PRK10418   17 PLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVAP---CALRGrKIATIMQNPrsafn 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1119 ---ILFDCSIAENIAYGDNSRAVSHEEIVRAAKEANIHQFIDSLPdkyntrvgdkgTQLSGGQKQRIAIARALVRQPHIL 1195
Cdd:PRK10418   94 plhTMHTHARETCLALGKPADDATLTAALEAVGLENAARVLKLYP-----------FEMSGGMLQRMMIALALLCEAPFI 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6755046   1196 LLDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHG 1253
Cdd:PRK10418  163 IADEPTTDLDVVAQARILDLLESivQKRALGMLLVTHDMGVVARlADDVAVMSHGRIVEQG 223
ABC_6TM_Rv0194_D1_like cd18543
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ...
118-339 1.18e-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: 70.20  E-value: 1.18e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   118 TGIGAGVLIVAYIQvslWCLAAGRQI----------HKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGd 187
Cdd:cd18543   39 WPLVLLLLALGVAE---AVLSFLRRYlagrlslgveHDLRTDLFAHLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLA- 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   188 KIGMFFQSITTFLAGFIIGFISGWKLTLVILAVSPLIGLSSALWAKVLTSFTnkeLQAYAKAGAVA---EEVLAAIRTVI 264
Cdd:cd18543  115 FGPFLLGNLLTLVVGLVVMLVLSPPLALVALASLPPLVLVARRFRRRYFPAS---RRAQDQAGDLAtvvEESVTGIRVVK 191
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6755046   265 AFGGQQKELERYNKNLEEAKNVGIKKA-ITASISIGIAyLLVYASYALAFWYGTSLVLSNEYSIGEvLTVFFSILL 339
Cdd:cd18543  192 AFGRERRELDRFEAAARRLRATRLRAArLRARFWPLLE-ALPELGLAAVLALGGWLVANGSLTLGT-LVAFSAYLT 265
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
391-614 1.21e-12

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 69.79  E-value: 1.21e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    391 LEFKNVHFnypSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYL---RE 467
Cdd:PRK11831    8 VDMRGVSF---TRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRK 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    468 IIGVVSQEPVLFA-TTIAENIRYG-REDVTMDE--IEKAVkeanaydfIMKLphqfdTLVGERGA------QLSGGQKQR 537
Cdd:PRK11831   85 RMSMLFQSGALFTdMNVFDNVAYPlREHTQLPAplLHSTV--------MMKL-----EAVGLRGAaklmpsELSGGMARR 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    538 IAIARALVRNPKILLLDEATSALDTESEAVVQAALDKARE--GRTTIVIAHR----LSTVRNADVIAGFDggvIVEQGNH 611
Cdd:PRK11831  152 AALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSalGVTCVVVSHDvpevLSIADHAYIVADKK---IVAHGSA 228

                  ...
gi 6755046    612 DEL 614
Cdd:PRK11831  229 QAL 231
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
391-618 1.25e-12

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 71.98  E-value: 1.25e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   391 LEFKNVHfnYPSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREI-I 469
Cdd:COG3845  258 LEVENLS--VRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgV 335
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   470 GVVSQEPVLFAT----TIAENI---RYGREDVT------MDEIEKAVKEA-NAYDfiMKLPHQfDTLVGergaQLSGGQK 535
Cdd:COG3845  336 AYIPEDRLGRGLvpdmSVAENLilgRYRRPPFSrggfldRKAIRAFAEELiEEFD--VRTPGP-DTPAR----SLSGGNQ 408
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   536 QRIAIARALVRNPKILLLDEATSALDTES-EAVVQAALDKAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDE 613
Cdd:COG3845  409 QKVILARELSRDPKLLIAAQPTRGLDVGAiEFIHQRLLELRDAGAAVLLISEDLDEILAlSDRIAVMYEGRIVGEVPAAE 488

                 ....*
gi 6755046   614 LMREK 618
Cdd:COG3845  489 ATREE 493
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
388-591 1.35e-12

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 68.99  E-value: 1.35e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    388 MGNL-EFKNVHFNYPSRsevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQdirtinvryLR 466
Cdd:PRK09544    1 MTSLvSLENVSVSFGQR---RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK---------LR 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    467 eiIGVVSQEPVLFAT---TIAENIRYgREDVTMDEIEKAVKEANAYDFImKLPHQfdtlvgergaQLSGGQKQRIAIARA 543
Cdd:PRK09544   69 --IGYVPQKLYLDTTlplTVNRFLRL-RPGTKKEDILPALKRVQAGHLI-DAPMQ----------KLSGGETQRVLLARA 134
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 6755046    544 LVRNPKILLLDEATSALDTESEAVVQAALDKARE--GRTTIVIAHRLSTV 591
Cdd:PRK09544  135 LLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRelDCAVLMVSHDLHLV 184
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
1043-1260 1.39e-12

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: 71.78  E-value: 1.39e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    1043 PTRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYD-PMAGSVFLDGKEIKQLN-VQWLRAHLGIVSQEP-- 1118
Cdd:TIGR02633  268 VINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGKPVDIRNpAQAIRAGIAMVPEDRkr 347
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    1119 --ILFDCSIAENIAYGDNSRAVSHEEIVRAAKEANIHQFIDSLpdKYNTRVGDKG-TQLSGGQKQRIAIARALVRQPHIL 1195
Cdd:TIGR02633  348 hgIVPILGVGKNITLSVLKSFCFKMRIDAAAELQIIGSAIQRL--KVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVL 425
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6755046    1196 LLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVIENGKVK----EHG-THQQLLA 1260
Cdd:TIGR02633  426 ILDEPTRGVDVGAKYEIYKLINQlAQEGVAIIVVSSELAEVLGlSDRVLVIGEGKLKgdfvNHAlTQEQVLA 497
ABC_6TM_TmrB_like cd18541
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ...
709-968 1.42e-12

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: 69.75  E-value: 1.42e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   709 LLVGVLCAVINGCIQPVFAIVFSRIV-GVFSRDDDHETKRQNCnlfsLFFLVMGLISFVTYFFQGFTFGKAGEILTKRVR 787
Cdd:cd18541    1 YLLGILFLILVDLLQLLIPRIIGRAIdALTAGTLTASQLLRYA----LLILLLALLIGIFRFLWRYLIFGASRRIEYDLR 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   788 YMVFKSMLRQDISWFddHKNSTGSLTTRLASDASSVKGAMGARLAVVTQNVANLGTGVILSLVYGWQLTLLLVVIIPLIV 867
Cdd:cd18541   77 NDLFAHLLTLSPSFY--QKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLA 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   868 LGGIIEMKLLSGQALKDKKQLeisGKIATEAIENF---RTIVSLTREQKFETMYAQSLQVPYRNAMKKAHVFGITFSFTQ 944
Cdd:cd18541  155 LLVYRLGKKIHKRFRKVQEAF---SDLSDRVQESFsgiRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIG 231
                        250       260
                 ....*....|....*....|....
gi 6755046   945 AMMYFSYAACFRFGAYLVAQQLMT 968
Cdd:cd18541  232 LLIGLSFLIVLWYGGRLVIRGTIT 255
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
1043-1260 1.55e-12

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 71.50  E-value: 1.55e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1043 PTRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPM-AGSVFLDGKEIKQLN-VQWLRAHLGIVSQEP-- 1118
Cdd:PRK13549  270 PVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRwEGEIFIDGKPVKIRNpQQAIAQGIAMVPEDRkr 349
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1119 --ILFDCSIAENIAYGDNSRAVSHEEIVRAAKEANIHQFIDSLPDKYNT---RVGdkgtQLSGGQKQRIAIARALVRQPH 1193
Cdd:PRK13549  350 dgIVPVMGVGKNITLAALDRFTGGSRIDDAAELKTILESIQRLKVKTASpelAIA----RLSGGNQQKAVLAKCLLLNPK 425
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6755046   1194 ILLLDEATSALDT----ESEKVVQEAldkAREGRTCIVIAHRLSTIQN-ADLIVVIENGKVK-----EHGTHQQLLA 1260
Cdd:PRK13549  426 ILILDEPTRGIDVgakyEIYKLINQL---VQQGVAIIVISSELPEVLGlSDRVLVMHEGKLKgdlinHNLTQEQVME 499
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
411-586 1.68e-12

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 67.91  E-value: 1.68e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    411 GLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREII------GVvsqEPVLfatTIA 484
Cdd:PRK13538   19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLylghqpGI---KTEL---TAL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    485 ENIRY-------GREDVTMDEIEKavkeanaydfimklphqfdtlVGERG------AQLSGGQKQRIAIARALVRNPKIL 551
Cdd:PRK13538   93 ENLRFyqrlhgpGDDEALWEALAQ---------------------VGLAGfedvpvRQLSAGQQRRVALARLWLTRAPLW 151
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 6755046    552 LLDEATSALDTESEAVVQAALDK-AREGRTTIVIAH 586
Cdd:PRK13538  152 ILDEPFTAIDKQGVARLEALLAQhAEQGGMVILTTH 187
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
407-603 2.26e-12

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 68.89  E-value: 2.26e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    407 QILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRL----------YDPLEGVVSIDGQDIRtiNVRYLREIIGVVSQEP 476
Cdd:PRK09984   18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgdksagshIELLGRTVQREGRLAR--DIRKSRANTGYIFQQF 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    477 VLF-ATTIAENIRYGREDVT------MDEIEKAVKEaNAYDFIMK--LPHqfdtLVGERGAQLSGGQKQRIAIARALVRN 547
Cdd:PRK09984   96 NLVnRLSVLENVLIGALGSTpfwrtcFSWFTREQKQ-RALQALTRvgMVH----FAHQRVSTLSGGQQQRVAIARALMQQ 170
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6755046    548 PKILLLDEATSALDTESEAVVQAALD--KAREGRTTIVIAH----------RLSTVRNADVIagFDGG 603
Cdd:PRK09984  171 AKVILADEPIASLDPESARIVMDTLRdiNQNDGITVVVTLHqvdyalryceRIVALRQGHVF--YDGS 236
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
390-617 2.30e-12

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 69.77  E-value: 2.30e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    390 NLEFKNVHF---NYPSRSEVQIlkglNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDpLEGVVS-----IDGQDIRTIN 461
Cdd:PRK11022    5 NVDKLSVHFgdeSAPFRAVDRI----SYSVKQGEVVGIVGESGSGKSVSSLAIMGLID-YPGRVMaekleFNGQDLQRIS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    462 VRYLREIIG----VVSQEPVlfaTTIAENIRYGREdvTMDEIE------KAVKEANAYDFImklphqfdTLVG-----ER 526
Cdd:PRK11022   80 EKERRNLVGaevaMIFQDPM---TSLNPCYTVGFQ--IMEAIKvhqggnKKTRRQRAIDLL--------NQVGipdpaSR 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    527 ----GAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEA-VVQAALD-KAREGRTTIVIAHRLSTV-RNADVIAG 599
Cdd:PRK11022  147 ldvyPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAqIIELLLElQQKENMALVLITHDLALVaEAAHKIIV 226
                         250
                  ....*....|....*...
gi 6755046    600 FDGGVIVEQGNHDELMRE 617
Cdd:PRK11022  227 MYAGQVVETGKAHDIFRA 244
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
1032-1261 3.32e-12

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 69.37  E-value: 3.32e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1032 NVKFNGVQFNYPTrPNIPVLQGLSLEVKKGQTLALVGSSGCGKS-TVVQLLERFYDP--MAGSVFLDGKEI-----KQLN 1103
Cdd:PRK09473   14 DVKDLRVTFSTPD-GDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANgrIGGSATFNGREIlnlpeKELN 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1104 VqwLRA-HLGIVSQEPIlfdCSIAENIAYGDN-----------SRAVSHEEIVR---AAKEANIHQFIDSLPDKYntrvg 1168
Cdd:PRK09473   93 K--LRAeQISMIFQDPM---TSLNPYMRVGEQlmevlmlhkgmSKAEAFEESVRmldAVKMPEARKRMKMYPHEF----- 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1169 dkgtqlSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDK-AREGRTCIV-IAHRLSTIQN-ADLIVVIE 1245
Cdd:PRK09473  163 ------SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNElKREFNTAIImITHDLGVVAGiCDKVLVMY 236
                         250
                  ....*....|....*.
gi 6755046   1246 NGKVKEHGTHQQLLAQ 1261
Cdd:PRK09473  237 AGRTMEYGNARDVFYQ 252
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
409-591 3.72e-12

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 68.37  E-value: 3.72e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    409 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRtinvRYLRE-IIGVVSQE-------PVLFA 480
Cdd:PRK15056   23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR----QALQKnLVAYVPQSeevdwsfPVLVE 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    481 TTIAENiRYG-----REDVTMDEieKAVKEANAYDFIMKLPHQfdtLVGErgaqLSGGQKQRIAIARALVRNPKILLLDE 555
Cdd:PRK15056   99 DVVMMG-RYGhmgwlRRAKKRDR--QIVTAALARVDMVEFRHR---QIGE----LSGGQKKRVFLARAIAQQGQVILLDE 168
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 6755046    556 ATSALDTESEAVVQAALDKAR-EGRTTIVIAHRLSTV 591
Cdd:PRK15056  169 PFTGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSV 205
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
407-586 4.10e-12

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: 70.35  E-value: 4.10e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     407 QILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDgqdiRTINVRYLreiigvvSQEPVLFAT-TIAE 485
Cdd:TIGR03719   19 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQ----PGIKVGYL-------PQEPQLDPTkTVRE 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     486 NI-------------------RYGREDVTMD-------EIEKAVKEANAYDFIMKLPHQFDTLVGERG----AQLSGGQK 535
Cdd:TIGR03719   88 NVeegvaeikdaldrfneisaKYAEPDADFDklaaeqaELQEIIDAADAWDLDSQLEIAMDALRCPPWdadvTKLSGGER 167
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 6755046     536 QRIAIARALVRNPKILLLDEATSALDTESEAVVQAALdKAREGrTTIVIAH 586
Cdd:TIGR03719  168 RRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHL-QEYPG-TVVAVTH 216
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
1054-1259 6.10e-12

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 67.27  E-value: 6.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1054 LSLEVKKGQTLALVGSSGCGKSTvvqLLERfydpMAG------SVFLDGKEIKQLNVQWL---RAHLgiVSQEPILF--- 1121
Cdd:PRK03695   15 LSAEVRAGEILHLVGPNGAGKST---LLAR----MAGllpgsgSIQFAGQPLEAWSAAELarhRAYL--SQQQTPPFamp 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1122 -----DCSIAENIAYGDNSRAVshEEIVRAAKeanihqfidsLPDKYNTRVGdkgtQLSGGQKQRIAIARALVR-----Q 1191
Cdd:PRK03695   86 vfqylTLHQPDKTRTEAVASAL--NEVAEALG----------LDDKLGRSVN----QLSGGEWQRVRLAAVVLQvwpdiN 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6755046   1192 PH--ILLLDEATSALDtesekVVQE-ALDK-----AREGRTCIVIAHRLS-TIQNADLIVVIENGKVKEHGTHQQLL 1259
Cdd:PRK03695  150 PAgqLLLLDEPMNSLD-----VAQQaALDRllselCQQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVL 221
ABCG_PDR_domain2 cd03232
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...
1051-1247 6.84e-12

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: 65.73  E-value: 6.84e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1051 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLL-ERFYD-PMAGSVFLDGKEIKQLnvqwLRAHLGIVSQEPILFDCS-IAE 1127
Cdd:cd03232   23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLaGRKTAgVITGEILINGRPLDKN----FQRSTGYVEQQDVHSPNLtVRE 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1128 NIAYGDNSRAVSHEeivraakeanihqfidslpdkyntrvgdkgtqlsggQKQRIAIARALVRQPHILLLDEATSALDTE 1207
Cdd:cd03232   99 ALRFSALLRGLSVE------------------------------------QRKRLTIGVELAAKPSILFLDEPTSGLDSQ 142
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 6755046  1208 SEKVVQEALDK-AREGRTCIVIAHRLS--TIQNADLIVVIENG 1247
Cdd:cd03232  143 AAYNIVRFLKKlADSGQAILCTIHQPSasIFEKFDRLLLLKRG 185
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
419-609 9.22e-12

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 66.87  E-value: 9.22e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    419 GQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINV---------RYLREIIGVVSQEP-------VLFATT 482
Cdd:PRK11701   32 GEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLyalseaerrRLLRTEWGFVHQHPrdglrmqVSAGGN 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    483 IAE-----------NIRYGREDvTMDEIEKAVkeanayDFIMKLPHQFdtlvgergaqlSGGQKQRIAIARALVRNPKIL 551
Cdd:PRK11701  112 IGErlmavgarhygDIRATAGD-WLERVEIDA------ARIDDLPTTF-----------SGGMQQRLQIARNLVTHPRLV 173
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6755046    552 LLDEATSALDTEseavVQAA-LDKARE-----GRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQG 609
Cdd:PRK11701  174 FMDEPTGGLDVS----VQARlLDLLRGlvrelGLAVVIVTHDLAVARLlAHRLLVMKQGRVVESG 234
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
1060-1241 1.60e-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: 63.55  E-value: 1.60e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     1060 KGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVfldgkeikqlnvqwlrahlgivsqepILFDCSIAENIAYGDNSravs 1139
Cdd:smart00382    1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV--------------------------IYIDGEDILEEVLDQLL---- 50
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     1140 heeivraakeanihqfidslpdkyNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALD-- 1217
Cdd:smart00382   51 ------------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElr 106
                           170       180
                    ....*....|....*....|....*....
gi 6755046     1218 -----KAREGRTCIVIAHRLSTIQNADLI 1241
Cdd:smart00382  107 lllllKSEKNLTVILTTNDEKDLGPALLR 135
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
1052-1230 1.81e-11

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 64.83  E-value: 1.81e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1052 QGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQL------NVQWLRAHLGIVS----QEPILF 1121
Cdd:PRK13538   18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQrdeyhqDLLYLGHQPGIKTeltaLENLRF 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1122 DCSIAeniaygdnsRAVSHEEIVRAAKEANIHQFIDsLPDKyntrvgdkgtQLSGGQKQRIAIARALVRQPHILLLDEAT 1201
Cdd:PRK13538   98 YQRLH---------GPGDDEALWEALAQVGLAGFED-VPVR----------QLSAGQQRRVALARLWLTRAPLWILDEPF 157
                         170       180       190
                  ....*....|....*....|....*....|
gi 6755046   1202 SALDTESEKVVQEALDK-AREGRTCIVIAH 1230
Cdd:PRK13538  158 TAIDKQGVARLEALLAQhAEQGGMVILTTH 187
ABC_6TM_exporter_like cd18778
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
122-361 3.82e-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: 3.82e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   122 AGVLIVAYI-QVSLWCL-------AAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDKIGMFF 193
Cdd:cd18778   43 ALLLLGAYLlRALLNFLriylnhvAEQKVVADLRSDLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGI 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   194 QSITTFLAGFIIGFISGWKLTLVILAVSPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQKEL 273
Cdd:cd18778  123 TNVLTLVGVAIILFSINPKLALLTLIPIPFLALGAWLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEA 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   274 ERYNKNLEEAKNVGIKKAITASISIGIAYLLVYASYALAFWYGTSLVLSNEYSIGEVltVFFSILLGTF--SIGHLAPNI 351
Cdd:cd18778  203 KRFEALSRRYRKAQLRAMKLWAIFHPLMEFLTSLGTVLVLGFGGRLVLAGELTIGDL--VAFLLYLGLFyePITSLHGLN 280
                        250
                 ....*....|
gi 6755046   352 EAFANARGAA 361
Cdd:cd18778  281 EMLQRALAGA 290
ABC_6TM_TAP1 cd18589
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ...
758-933 3.89e-11

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: 65.57  E-value: 3.89e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   758 LVMGLI---SFVTYFFQGFTFGKAGEILTKRVRYMVFKSMLRQDISWFDdhKNSTGSLTTRLASDASSVKGAMGARLAVV 834
Cdd:cd18589   40 TVMSLLtiaSAVSEFVCDLIYNITMSRIHSRLQGLVFAAVLRQEIAFFD--SNQTGDIVSRVTTDTEDMSESLSENLSLL 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   835 TQNVANLGTGVILSLVYGWQLTLLLVVIIPLIVLGGIIEMKLLSGQALKDKKQLEISGKIATEAIENFRTIVSLTREQKF 914
Cdd:cd18589  118 MWYLARGLFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEEGE 197
                        170
                 ....*....|....*....
gi 6755046   915 ETMYAQSLQVPYRNAMKKA 933
Cdd:cd18589  198 AQRYRQRLQKTYRLNKKEA 216
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
1049-1249 4.37e-11

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 67.28  E-value: 4.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1049 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLerfydpmAGSVFLD-GKEIKQLNVqwlrahlgIVS---QEP------ 1118
Cdd:PRK11147   17 PLLDNAELHIEDNERVCLVGRNGAGKSTLMKIL-------NGEVLLDdGRIIYEQDL--------IVArlqQDPprnveg 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1119 ILFDcSIAENIA--------YGDNSRAVSHEE----IVRAAK-------------EANIHQFIDSL---PDKyntrvgdK 1170
Cdd:PRK11147   82 TVYD-FVAEGIEeqaeylkrYHDISHLVETDPseknLNELAKlqeqldhhnlwqlENRINEVLAQLgldPDA-------A 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1171 GTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALdKAREGrTCIVIAHRLSTIQN-ADLIVVIENGKV 1249
Cdd:PRK11147  154 LSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFL-KTFQG-SIIFISHDRSFIRNmATRIVDLDRGKL 231
3a01203 TIGR00954
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...
412-602 5.21e-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: 5.21e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     412 LNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDgqdiRTINVRYlreiigvVSQEPVLFATTIAENIRYgr 491
Cdd:TIGR00954  471 LSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKP----AKGKLFY-------VPQRPYMTLGTLRDQIIY-- 537
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     492 EDVTMDEIEKAVKEANAYDFIMKLphQFDTLVGERGA---------QLSGGQKQRIAIARALVRNPKILLLDEATSALDT 562
Cdd:TIGR00954  538 PDSSEDMKRRGLSDKDLEQILDNV--QLTHILEREGGwsavqdwmdVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSV 615
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 6755046     563 ESEavvQAALDKARE-GRTTIVIAHRLSTVRNADVIAGFDG 602
Cdd:TIGR00954  616 DVE---GYMYRLCREfGITLFSVSHRKSLWKYHEYLLYMDG 653
PRK10522 PRK10522
multidrug transporter membrane component/ATP-binding component; Provisional
374-607 5.59e-11

multidrug transporter membrane component/ATP-binding component; Provisional


Pssm-ID: 236707 [Multi-domain]  Cd Length: 547  Bit Score: 66.92  E-value: 5.59e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    374 IDSFSTKGYKPDSIMGN-------LEFKNVHFNYPSRSEVqiLKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPL 446
Cdd:PRK10522  299 LNKLALAPYKAEFPRPQafpdwqtLELRNVTFAYQDNGFS--VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQ 376
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    447 EGVVSIDGQDIRTINVRYLREIIGVVSQEPVLFattiaenirygreDVTMDEIEKAVKEANAYDFI--MKLPHQFdTLVG 524
Cdd:PRK10522  377 SGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLF-------------DQLLGPEGKPANPALVEKWLerLKMAHKL-ELED 442
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    525 ERGA--QLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVV-QAALDKARE-GRTTIVIAHRLSTVRNADVIAGF 600
Cdd:PRK10522  443 GRISnlKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFyQVLLPLLQEmGKTIFAISHDDHYFIHADRLLEM 522

                  ....*..
gi 6755046    601 DGGVIVE 607
Cdd:PRK10522  523 RNGQLSE 529
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
1046-1248 5.65e-11

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 66.68  E-value: 5.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1046 PNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIK-QLNVQWLRAHLGIVSQE-PILFDC 1123
Cdd:PRK10982    9 PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQElNLVLQR 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1124 SIAENIAYGDNSRA---VSHEEIVRAAKeanihQFIDSLPDKYNTRvgDKGTQLSGGQKQRIAIARALVRQPHILLLDEA 1200
Cdd:PRK10982   89 SVMDNMWLGRYPTKgmfVDQDKMYRDTK-----AIFDELDIDIDPR--AKVATLSVSQMQMIEIAKAFSYNAKIVIMDEP 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 6755046   1201 TSALdteSEKVVQ---EALDKAREgRTC--IVIAHRLSTI-QNADLIVVIENGK 1248
Cdd:PRK10982  162 TSSL---TEKEVNhlfTIIRKLKE-RGCgiVYISHKMEEIfQLCDEITILRDGQ 211
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
401-583 6.09e-11

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


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 65.11  E-value: 6.09e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   401 PSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIiGVV----SQ-- 474
Cdd:COG4586   30 REYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFARRI-GVVfgqrSQlw 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   475 --EPVLfattiaENIRYGRE--DVTMDEIEKAVKEanaYDFIMKLPHQFDTLVgeRgaQLSGGQKQRIAIARALVRNPKI 550
Cdd:COG4586  109 wdLPAI------DSFRLLKAiyRIPDAEYKKRLDE---LVELLDLGELLDTPV--R--QLSLGQRMRCELAAALLHRPKI 175
                        170       180       190
                 ....*....|....*....|....*....|....
gi 6755046   551 LLLDEATSALDTESEAVVQAALDKA-REGRTTIV 583
Cdd:COG4586  176 LFLDEPTIGLDVVSKEAIREFLKEYnRERGTTIL 209
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
1050-1232 6.58e-11

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 63.98  E-value: 6.58e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKeikqlnvqwLRahLGIVSQEpILFDCSIAENI 1129
Cdd:PRK09544   19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK---------LR--IGYVPQK-LYLDTTLPLTV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1130 AYGDNSR-AVSHEEIVRAAKEANIHQFIDSLPDKyntrvgdkgtqLSGGQKQRIAIARALVRQPHILLLDEATSALDTES 1208
Cdd:PRK09544   87 NRFLRLRpGTKKEDILPALKRVQAGHLIDAPMQK-----------LSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNG 155
                         170       180
                  ....*....|....*....|....*.
gi 6755046   1209 EKVVQEALDKAREGRTCIV--IAHRL 1232
Cdd:PRK09544  156 QVALYDLIDQLRRELDCAVlmVSHDL 181
hmuV PRK13547
heme ABC transporter ATP-binding protein;
1050-1254 6.85e-11

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 64.46  E-value: 6.85e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLE-RFYDPMA-------GSVFLDGKEIKQLNVQWL---RAHLGIVSQEP 1118
Cdd:PRK13547   16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGGAprgarvtGDVTLNGEPLAAIDAPRLarlRAVLPQAAQPA 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1119 ILFdcSIAENIAYG-----DNSRAVSHE--EIVRAAKEanihqfidsLPDKyNTRVGDKGTQLSGGQKQRIAIARAL--- 1188
Cdd:PRK13547   96 FAF--SAREIVLLGryphaRRAGALTHRdgEIAWQALA---------LAGA-TALVGRDVTTLSGGELARVQFARVLaql 163
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6755046   1189 ------VRQPHILLLDEATSALD-TESEKVVQEALDKAREGRT-CIVIAHRLS-TIQNADLIVVIENGKVKEHGT 1254
Cdd:PRK13547  164 wpphdaAQPPRYLLLDEPTAALDlAHQHRLLDTVRRLARDWNLgVLAIVHDPNlAARHADRIAMLADGAIVAHGA 238
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
1051-1235 8.37e-11

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 64.13  E-value: 8.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1051 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGiVSQE-----PILFDcSI 1125
Cdd:PRK15056   23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYVP-QSEEvdwsfPVLVE-DV 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1126 AENIAYGDNS---RAVSHE-EIVRAAKEAnihqfIDSLPDKYNtRVGdkgtQLSGGQKQRIAIARALVRQPHILLLDEAT 1201
Cdd:PRK15056  101 VMMGRYGHMGwlrRAKKRDrQIVTAALAR-----VDMVEFRHR-QIG----ELSGGQKKRVFLARAIAQQGQVILLDEPF 170
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 6755046   1202 SALDTESEKVVQEALDKAR-EGRTCIVIAHRLSTI 1235
Cdd:PRK15056  171 TGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSV 205
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
1049-1239 1.01e-10

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127 [Multi-domain]  Cd Length: 200  Bit Score: 62.66  E-value: 1.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1049 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAEN 1128
Cdd:PRK13540   15 PLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSGINPYLTLREN 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1129 IAYG--DNSRAVSHEEIVRAAKEANIHQFIDSLpdkyntrvgdkgtqLSGGQKQRIAIARALVRQPHILLLDEATSALDT 1206
Cdd:PRK13540   95 CLYDihFSPGAVGITELCRLFSLEHLIDYPCGL--------------LSSGQKRQVALLRLWMSKAKLWLLDEPLVALDE 160
                         170       180       190
                  ....*....|....*....|....*....|....
gi 6755046   1207 ESEKVVQEALDKAR-EGRTCIVIAHRLSTIQNAD 1239
Cdd:PRK13540  161 LSLLTIITKIQEHRaKGGAVLLTSHQDLPLNKAD 194
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
391-595 1.01e-10

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127 [Multi-domain]  Cd Length: 200  Bit Score: 62.66  E-value: 1.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    391 LEFKNVHFNYPSRSevqILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLREIIG 470
Cdd:PRK13540    2 LDVIELDFDYHDQP---LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    471 VVSQEPVLFATTIAENIRYG-REDVTMDEIEKAVKeanaydfIMKLPHQFDTLVGergaQLSGGQKQRIAIARALVRNPK 549
Cdd:PRK13540   79 VGHRSGINPYLTLRENCLYDiHFSPGAVGITELCR-------LFSLEHLIDYPCG----LLSSGQKRQVALLRLWMSKAK 147
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 6755046    550 ILLLDEATSALDTESEAVVQAALDKAR-EGRTTIVIAHRLSTVRNAD 595
Cdd:PRK13540  148 LWLLDEPLVALDELSLLTIITKIQEHRaKGGAVLLTSHQDLPLNKAD 194
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
1054-1254 1.01e-10

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 64.76  E-value: 1.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1054 LSLEVKKGQTLALVGSSGCGKS----TVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLR----AHLGIVSQEPI--LFDC 1123
Cdd:PRK11022   26 ISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISEKERRnlvgAEVAMIFQDPMtsLNPC 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1124 -----SIAENI-AYGDNSRAVSHEEIVRAAKEANIhqfidslPDKyNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLL 1197
Cdd:PRK11022  106 ytvgfQIMEAIkVHQGGNKKTRRQRAIDLLNQVGI-------PDP-ASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIA 177
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1198 DEATSALD-TESEKVVQEALD-KAREGRTCIVIAHRLSTI-QNADLIVVIENGKVKEHGT 1254
Cdd:PRK11022  178 DEPTTALDvTIQAQIIELLLElQQKENMALVLITHDLALVaEAAHKIIVMYAGQVVETGK 237
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
416-589 1.08e-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: 63.54  E-value: 1.08e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   416 VKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSiDGQDIRTInVRYLReiiGVVSQEpvLFATTIAENIRYGREDVT 495
Cdd:cd03236   23 PREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFD-DPPDWDEI-LDEFR---GSELQN--YFTKLLEGDVKVIVKPQY 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   496 MDEIEKAVKeANAYDFIMKLP--HQFDTLVG--------ERG-AQLSGGQKQRIAIARALVRNPKILLLDEATSALDTES 564
Cdd:cd03236   96 VDLIPKAVK-GKVGELLKKKDerGKLDELVDqlelrhvlDRNiDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQ 174
                        170       180
                 ....*....|....*....|....*.
gi 6755046   565 EAVVQAALDK-AREGRTTIVIAHRLS 589
Cdd:cd03236  175 RLNAARLIRElAEDDNYVLVVEHDLA 200
ycf16 CHL00131
sulfate ABC transporter protein; Validated
391-610 1.37e-10

sulfate ABC transporter protein; Validated


Pssm-ID: 214372 [Multi-domain]  Cd Length: 252  Bit Score: 63.12  E-value: 1.37e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    391 LEFKNVHfnyPSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLM--QRLYDPLEGVVSIDGQDIRTIN------- 461
Cdd:CHL00131    8 LEIKNLH---ASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIagHPAYKILEGDILFKGESILDLEpeerahl 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    462 -----VRYLREIIGVVSQEpvlFATTIAENIRYGREDVTMDEIEkavkeanAYDFIM-KLPhqfdtLVGERGAQL----- 530
Cdd:CHL00131   85 giflaFQYPIEIPGVSNAD---FLRLAYNSKRKFQGLPELDPLE-------FLEIINeKLK-----LVGMDPSFLsrnvn 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    531 ---SGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDK-AREGRTTIVIAH--RLSTVRNADVIAGFDGGV 604
Cdd:CHL00131  150 egfSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKlMTSENSIILITHyqRLLDYIKPDYVHVMQNGK 229

                  ....*.
gi 6755046    605 IVEQGN 610
Cdd:CHL00131  230 IIKTGD 235
PLN03211 PLN03211
ABC transporter G-25; Provisional
1050-1269 1.63e-10

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 65.29  E-value: 1.63e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLE-RFY-DPMAGSVFLDGKEIKQlnvQWLRaHLGIVSQEPILF-DCSIA 1126
Cdd:PLN03211   83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgRIQgNNFTGTILANNRKPTK---QILK-RTGFVTQDDILYpHLTVR 158
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1127 ENIAYGDNSR---AVSHEEIVRAAkEANIHQFidSLPDKYNTRVGDKGTQ-LSGGQKQRIAIARALVRQPHILLLDEATS 1202
Cdd:PLN03211  159 ETLVFCSLLRlpkSLTKQEKILVA-ESVISEL--GLTKCENTIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDEPTS 235
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1203 ALD-TESEKVVQEALDKAREGRTCIVIAHRLST--IQNADLIVVIENGKVKEHGTHQQLLAqkgiYFSMV 1269
Cdd:PLN03211  236 GLDaTAAYRLVLTLGSLAQKGKTIVTSMHQPSSrvYQMFDSVLVLSEGRCLFFGKGSDAMA----YFESV 301
sufC PRK09580
cysteine desulfurase ATPase component; Reviewed
1049-1261 1.71e-10

cysteine desulfurase ATPase component; Reviewed


Pssm-ID: 181965 [Multi-domain]  Cd Length: 248  Bit Score: 62.89  E-value: 1.71e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1049 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL--ERFYDPMAGSVFLDGKEIKQLNVQwLRAHLGI--VSQEPI----- 1119
Cdd:PRK09580   15 AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSPE-DRAGEGIfmAFQYPVeipgv 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1120 ----LFDCSIAENIAYGDnsravsHEEIVRAAKEANIHQFIDSL--PDKYNTRVGDKGtqLSGGQKQRIAIARALVRQPH 1193
Cdd:PRK09580   94 snqfFLQTALNAVRSYRG------QEPLDRFDFQDLMEEKIALLkmPEDLLTRSVNVG--FSGGEKKRNDILQMAVLEPE 165
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6755046   1194 ILLLDEATSALDTESEKVVQEALDKAREG-RTCIVIAH--RLSTIQNADLIVVIENGKVKEHGTH---QQLLAQ 1261
Cdd:PRK09580  166 LCILDESDSGLDIDALKIVADGVNSLRDGkRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDFtlvKQLEEQ 239
ABC_6TM_exporter_like cd18540
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
115-342 1.87e-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: 349984 [Multi-domain]  Cd Length: 295  Bit Score: 63.27  E-value: 1.87e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   115 YYYTGIGAGVLIVAYIQVSLWCLAAGRQ----IHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKIND----GIG 186
Cdd:cd18540   42 TGFILLYLGLILIQALSVFLFIRLAGKIemgvSYDLRKKAFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEiiswGLV 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   187 DkigmFFQSITTFLAGFIIGFISGWKLTLVILAVSPLIGLSSALwakvltsFTNKELQAYAKAGAVAEEVLAA------- 259
Cdd:cd18540  122 D----LVWGITYMIGILIVMLILNWKLALIVLAVVPVLAVVSIY-------FQKKILKAYRKVRKINSRITGAfnegitg 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   260 IRTVIAFGGQQKELERYNKNLEEAKNVGIKKAITASISIGIAYLLVYASYALAFWYGTSLVLSNEYSIGeVLTVFFSILL 339
Cdd:cd18540  191 AKTTKTLVREEKNLREFKELTEEMRRASVRAARLSALFLPIVLFLGSIATALVLWYGGILVLAGAITIG-TLVAFISYAT 269

                 ...
gi 6755046   340 GTF 342
Cdd:cd18540  270 QFF 272
ABC_6TM_YwjA_like cd18549
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ...
146-342 1.99e-10

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: 63.24  E-value: 1.99e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   146 IRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKIND----GIGDkigmFFQSITTFLAGFIIGFISGWKLTLVILAVS 221
Cdd:cd18549   77 MRRDLFEHLQKLSFSFFDNNKTGQLMSRITNDLFDISElahhGPED----LFISIITIIGSFIILLTINVPLTLIVFALL 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   222 PLIGlssalwakVLTSFTNKEL-----QAYAKAG---AVAEEVLAAIRTVIAFGGQQKELERY---NKNLEEAKnvgiKK 290
Cdd:cd18549  153 PLMI--------IFTIYFNKKMkkafrRVREKIGeinAQLEDSLSGIRVVKAFANEEYEIEKFdegNDRFLESK----KK 220
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 6755046   291 AITA-SISIGIAYLLVYASYALAFWYGTSLVLSNEYSIGEVLTvfFSILLGTF 342
Cdd:cd18549  221 AYKAmAYFFSGMNFFTNLLNLVVLVAGGYFIIKGEITLGDLVA--FLLYVNVF 271
ABC_6TM_HetC_like cd18568
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ...
150-342 2.30e-10

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: 63.35  E-value: 2.30e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   150 FFHAIMNQEIGWFDVHDVGELNTRLTDdvskiNDGI-----GDKIGMFFQSITTFLAGFIIGFISgWKLTLVILAVSPLI 224
Cdd:cd18568   81 FYKHLLSLPLSFFASRKVGDIITRFQE-----NQKIrrfltRSALTTILDLLMVFIYLGLMFYYN-LQLTLIVLAFIPLY 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   225 GLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQ----KELERYNKNLeeakNVGIKKAITASISIGI 300
Cdd:cd18568  155 VLLTLLSSPKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAERpirwRWENKFAKAL----NTRFRGQKLSIVLQLI 230
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 6755046   301 AYLLVYASYALAFWYGTSLVLSNEYSIGEVltVFFSILLGTF 342
Cdd:cd18568  231 SSLINHLGTIAVLWYGAYLVISGQLTIGQL--VAFNMLFGSV 270
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
409-610 2.49e-10

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: 62.63  E-value: 2.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   409 LKGLNLKVKSGQTVALVGNSGCGKSTTVQ------LMQRL---------YDPLEG------VVSID----GQDIRTINVR 463
Cdd:cd03271   11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINdtlypaLARRLhlkkeqpgnHDRIEGlehidkVIVIDqspiGRTPRSNPAT 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   464 YlreiIGVVSQEPVLFATtIAENIRYGRE--DVTM------DEIEKAVKEAnaYDF---IMKLPHQFDTLV--------- 523
Cdd:cd03271   91 Y----TGVFDEIRELFCE-VCKGKRYNREtlEVRYkgksiaDVLDMTVEEA--LEFfenIPKIARKLQTLCdvglgyikl 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   524 GERGAQLSGGQKQRIAIARALVR---NPKILLLDEATSALDTESEAVVQAALDKARE-GRTTIVIAHRLSTVRNADVI-- 597
Cdd:cd03271  164 GQPATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDkGNTVVVIEHNLDVIKCADWIid 243
                        250
                 ....*....|....*..
gi 6755046   598 ----AGFDGGVIVEQGN 610
Cdd:cd03271  244 lgpeGGDGGGQVVASGT 260
ABC_6TM_exporter_like cd18563
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
709-869 7.93e-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: 350007 [Multi-domain]  Cd Length: 296  Bit Score: 61.37  E-value: 7.93e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   709 LLVGVLCAVINGCIQPVFAIVFSRIVgvfsrDDDHETKRQNCNLFSLFFLVMGLI-----SFVTYFFQGFTFGKAGEILT 783
Cdd:cd18563    1 LILGFLLMLLGTALGLVPPYLTKILI-----DDVLIQLGPGGNTSLLLLLVLGLAgayvlSALLGILRGRLLARLGERIT 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   784 KRVRYMVFKSMLRQDISWFDdhKNSTGSLTTRLASDASSVKGAMGARLAVVTQNVANL-GTGVILsLVYGWQLTLLLVVI 862
Cdd:cd18563   76 ADLRRDLYEHLQRLSLSFFD--KRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIiGIGVVL-FSLNWKLALLVLIP 152

                 ....*..
gi 6755046   863 IPLIVLG 869
Cdd:cd18563  153 VPLVVWG 159
PLN03140 PLN03140
ABC transporter G family member; Provisional
402-611 8.41e-10

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 63.71  E-value: 8.41e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    402 SRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTtvqlmqrLYDPLEGVVS---IDGqDIRTINVRYLREIIGVVS----- 473
Cdd:PLN03140  889 TEDRLQLLREVTGAFRPGVLTALMGVSGAGKTT-------LMDVLAGRKTggyIEG-DIRISGFPKKQETFARISgyceq 960
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    474 ----------QEPVLFATTIAENIRYGREDVTM--DEIEKAVKEANAYDFIMKLPhqfdtlvGERGaqLSGGQKQRIAIA 541
Cdd:PLN03140  961 ndihspqvtvRESLIYSAFLRLPKEVSKEEKMMfvDEVMELVELDNLKDAIVGLP-------GVTG--LSTEQRKRLTIA 1031
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6755046    542 RALVRNPKILLLDEATSALDTESEAVVQAAL-DKAREGRTTIVIAHRLSTvrnaDVIAGFDGGVIVEQGNH 611
Cdd:PLN03140 1032 VELVANPSIIFMDEPTSGLDARAAAIVMRTVrNTVDTGRTVVCTIHQPSI----DIFEAFDELLLMKRGGQ 1098
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
400-586 1.04e-09

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: 60.50  E-value: 1.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   400 YPSRSEVQILKGLNLKVKSG-----QTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDI----RTINVRYlreiig 470
Cdd:cd03237    1 YTYPTMKKTLGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVsykpQYIKADY------ 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   471 vvsqepvlfattiaenirYGREDVTMDEIEKAVKEANAYDF-IMKlPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPK 549
Cdd:cd03237   75 ------------------EGTVRDLLSSITKDFYTHPYFKTeIAK-PLQIEQILDREVPELSGGELQRVAIAACLSKDAD 135
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 6755046   550 ILLLDEATSALDTESEAVVQAALDKAREG--RTTIVIAH 586
Cdd:cd03237  136 IYLLDEPSAYLDVEQRLMASKVIRRFAENneKTAFVVEH 174
ABC_6TM_T1SS_like cd18555
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ...
119-342 1.23e-09

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: 60.99  E-value: 1.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   119 GIGAGVLIVAYIQVSLwclAAGRQIHKIRQKFFHAIMNQEIG--------WFDVHDVGELNTRLtDDVSKINDGIGDKIG 190
Cdd:cd18555   45 GIGILILFLLYGLFSF---LRGYIIIKLQTKLDKSLMSDFFEhllklpysFFENRSSGDLLFRA-NSNVYIRQILSNQVI 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   191 MFFQSITTFLAGFIIGFISGWKLTLVILAVSPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQ 270
Cdd:cd18555  121 SLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLLLLLTRKKIKKLNQEEIVAQTKVQSYLTETLYGIETIKSLGSEK 200
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6755046   271 KELERYNKNLEEAKNVGIKKAITASISIGIAYLLVYASYALAFWYGTSLVLSNEYSIGEVLTvfFSILLGTF 342
Cdd:cd18555  201 NIYKKWENLFKKQLKAFKKKERLSNILNSISSSIQFIAPLLILWIGAYLVINGELTLGELIA--FSSLAGSF 270
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
407-564 1.46e-09

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 62.06  E-value: 1.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    407 QILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEG-VVSIDGqdirtINVRYLreiigvvSQEPVLFAT-TIA 484
Cdd:PRK11819   21 QILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGeARPAPG-----IKVGYL-------PQEPQLDPEkTVR 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    485 ENI-------------------RYGREDVTMD-------EIEKAVKEANAYDfimkLPHQF------------DTLVGer 526
Cdd:PRK11819   89 ENVeegvaevkaaldrfneiyaAYAEPDADFDalaaeqgELQEIIDAADAWD----LDSQLeiamdalrcppwDAKVT-- 162
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 6755046    527 gaQLSGGQKQRIAIARALVRNPKILLLDEATSALDTES 564
Cdd:PRK11819  163 --KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
405-591 1.58e-09

Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 62.82  E-value: 1.58e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     405 EVQILKGLNLKVKSGQTVALVGNSGCGKST-----TVQLMQRLYDpLEGVVSIDGQDIRTINVRYLREIIGVVSQE---P 476
Cdd:TIGR00956   73 TFDILKPMDGLIKPGELTVVLGRPGSGCSTllktiASNTDGFHIG-VEGVITYDGITPEEIKKHYRGDVVYNAETDvhfP 151
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     477 VLfatTIAENIRYGREDVT-------MDEIEKAVKEANAYDFIMKLPHQFDTLVGE---RGaqLSGGQKQRIAIARALVR 546
Cdd:TIGR00956  152 HL---TVGETLDFAARCKTpqnrpdgVSREEYAKHIADVYMATYGLSHTRNTKVGNdfvRG--VSGGERKRVSIAEASLG 226
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 6755046     547 NPKILLLDEATSALDTESeavvqaALDKAREGRTTIVIAHRLSTV 591
Cdd:TIGR00956  227 GAKIQCWDNATRGLDSAT------ALEFIRALKTSANILDTTPLV 265
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
406-565 1.64e-09

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 62.05  E-value: 1.64e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    406 VQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRY-LREIIGVVSQE-PVLFATTI 483
Cdd:PRK10982   11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEaLENGISMVHQElNLVLQRSV 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    484 AENI---RYGREDVTMDEiEKAVKEANAYdfimklphqFDTL-----VGERGAQLSGGQKQRIAIARALVRNPKILLLDE 555
Cdd:PRK10982   91 MDNMwlgRYPTKGMFVDQ-DKMYRDTKAI---------FDELdididPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDE 160
                         170
                  ....*....|
gi 6755046    556 ATSALdTESE 565
Cdd:PRK10982  161 PTSSL-TEKE 169
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
411-609 1.83e-09

leucine/isoleucine/valine transporter ATP-binding subunit; Provisional


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 60.00  E-value: 1.83e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    411 GLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDI--------------RTI-NVRYLREIIGV---- 471
Cdd:PRK11300   23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIeglpghqiarmgvvRTFqHVRLFREMTVIenll 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    472 VSQE--------PVLFATTiaeniRYGREDvtMDEIEKAvkeANAYDFIMKLPhqfdtLVGERGAQLSGGQKQRIAIARA 543
Cdd:PRK11300  103 VAQHqqlktglfSGLLKTP-----AFRRAE--SEALDRA---ATWLERVGLLE-----HANRQAGNLAYGQQRRLEIARC 167
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6755046    544 LVRNPKILLLDEATSALDTESEAVVQAALDKARE--GRTTIVIAHRLSTVRN-ADVIagfdggVIVEQG 609
Cdd:PRK11300  168 MVTQPEILMLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGiSDRI------YVVNQG 230
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
1014-1239 1.89e-09

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 61.57  E-value: 1.89e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1014 PEIDSYSTeglKPTLLEGNVKF---NG-VQFNyptrpNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYdPMA 1089
Cdd:PRK10938  243 PEPDEPSA---RHALPANEPRIvlnNGvVSYN-----DRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDH-PQG 313
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1090 GS--VFLDGK---------EIKQlnvqwlraHLGIVSQEPIL---FDCSIAENIAYG--DN---SRAVSHeeivRAAKEA 1150
Cdd:PRK10938  314 YSndLTLFGRrrgsgetiwDIKK--------HIGYVSSSLHLdyrVSTSVRNVILSGffDSigiYQAVSD----RQQKLA 381
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1151 NihQFIDSLpdKYNTRVGDKGTQ-LSGGQkQRIA-IARALVRQPHILLLDEATSALDTESEKVVQEALDK-AREGRT--- 1224
Cdd:PRK10938  382 Q--QWLDIL--GIDKRTADAPFHsLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVlISEGETqll 456
                         250       260
                  ....*....|....*....|....*.
gi 6755046   1225 -----------CivIAHRLSTIQNAD 1239
Cdd:PRK10938  457 fvshhaedapaC--ITHRLEFVPDGD 480
ABC_6TM_PrtD_LapB_HlyB_like cd18782
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ...
120-340 2.27e-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: 60.30  E-value: 2.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   120 IGAGVLIVAYIQVSLWCL-------AAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLtDDVSKINDGIGDkigmf 192
Cdd:cd18782   44 IGVVMLVAALLEAVLTALrtylftdTANRIDLELGGTIIDHLLRLPLGFFDKRPVGELSTRI-SELDTIRGFLTG----- 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   193 fQSITTFL-AGFIIGFIS-----GWKLTLVILAVSPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAf 266
Cdd:cd18782  118 -TALTTLLdVLFSVIYIAvlfsySPLLTLVVLATVPLQLLLTFLFGPILRRQIRRRAEASAKTQSYLVESLTGIQTVKA- 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   267 ggQQKEL-------ERYNKNLEEaknvGIKKAITASISIGIAYLLVYASYALAFWYGTSLVLSNEYSIGEVLTvfFSILL 339
Cdd:cd18782  196 --QNAELkarwrwqNRYARSLGE----GFKLTVLGTTSGSLSQFLNKLSSLLVLWVGAYLVLRGELTLGQLIA--FRILS 267

                 .
gi 6755046   340 G 340
Cdd:cd18782  268 G 268
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
1054-1205 2.29e-09

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 61.61  E-value: 2.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1054 LSLEVKKGQTLALVGSSGCGKStvvQLLERFY---DPMAGSVFLDGKEIKQLNVQwLRAHLGIV-----SQEPILF-DCS 1124
Cdd:PRK15439  282 ISLEVRAGEILGLAGVVGAGRT---ELAETLYglrPARGGRIMLNGKEINALSTA-QRLARGLVylpedRQSSGLYlDAP 357
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1125 IAENIAygdnsrAVSHEEI---VRAAKEANI-HQFIDSLPDKYNTRVGDKGTqLSGGQKQRIAIARALVRQPHILLLDEA 1200
Cdd:PRK15439  358 LAWNVC------ALTHNRRgfwIKPARENAVlERYRRALNIKFNHAEQAART-LSGGNQQKVLIAKCLEASPQLLIVDEP 430

                  ....*
gi 6755046   1201 TSALD 1205
Cdd:PRK15439  431 TRGVD 435
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
1055-1259 2.39e-09

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 61.47  E-value: 2.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1055 SLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNV-QWLRAhlGIV------SQEPILFDCSIAE 1127
Cdd:PRK11288  273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPrDAIRA--GIMlcpedrKAEGIIPVHSVAD 350
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1128 NI---AYGDNSRAVSheeIVRAAKEA-NIHQFIDSLPDKynTRVGD-KGTQLSGGQKQRIAIARALVRQPHILLLDEATS 1202
Cdd:PRK11288  351 NInisARRHHLRAGC---LINNRWEAeNADRFIRSLNIK--TPSREqLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTR 425
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6755046   1203 ALDTESEKVVQEAL-DKAREGRTCIVIAHRLSTIQN-ADLIVVIENGKV-----KEHGTHQQLL 1259
Cdd:PRK11288  426 GIDVGAKHEIYNVIyELAAQGVAVLFVSSDLPEVLGvADRIVVMREGRIagelaREQATERQAL 489
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
395-618 2.97e-09

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 61.50  E-value: 2.97e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    395 NVHFNYPSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTtvqLMQrlydPLEGVVSID-GQDIRTINVrylreiigVVS 473
Cdd:PRK11147    5 SIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKST---LMK----ILNGEVLLDdGRIIYEQDL--------IVA 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    474 ---QEPVLFATT-----IAENI--------RYGR--EDVTMDEIEKAVKE-ANAYDfimKLPH----QFDTLVGERGAQ- 529
Cdd:PRK11147   70 rlqQDPPRNVEGtvydfVAEGIeeqaeylkRYHDisHLVETDPSEKNLNElAKLQE---QLDHhnlwQLENRINEVLAQl 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    530 ----------LSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALdKAREGrTTIVIAHRLSTVRN-ADVIA 598
Cdd:PRK11147  147 gldpdaalssLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFL-KTFQG-SIIFISHDRSFIRNmATRIV 224
                         250       260
                  ....*....|....*....|.
gi 6755046    599 GFDGGVIVE-QGNHDELMREK 618
Cdd:PRK11147  225 DLDRGKLVSyPGNYDQYLLEK 245
PLN03211 PLN03211
ABC transporter G-25; Provisional
405-609 3.19e-09

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 61.43  E-value: 3.19e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    405 EVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQ-LMQRLY-DPLEGVVSIDGqdiRTINVRYLREIiGVVSQEPVLFA-T 481
Cdd:PLN03211   80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNaLAGRIQgNNFTGTILANN---RKPTKQILKRT-GFVTQDDILYPhL 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    482 TIAENIRYGREDVTMDEIEKAVKEANAYDFI--MKLPHQFDTLVGE---RGaqLSGGQKQRIAIARALVRNPKILLLDEA 556
Cdd:PLN03211  156 TVRETLVFCSLLRLPKSLTKQEKILVAESVIseLGLTKCENTIIGNsfiRG--ISGGERKRVSIAHEMLINPSLLILDEP 233
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 6755046    557 TSALD-TESEAVVQAALDKAREGRTTIVIAHRLSTvrnaDVIAGFDGGVIVEQG 609
Cdd:PLN03211  234 TSGLDaTAAYRLVLTLGSLAQKGKTIVTSMHQPSS----RVYQMFDSVLVLSEG 283
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
392-563 4.88e-09

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 60.73  E-value: 4.88e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    392 EFKNVHFNYPSRsevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQdirtINVRYL---REI 468
Cdd:PRK11147  321 EMENVNYQIDGK---QLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTK----LEVAYFdqhRAE 393
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    469 IgvvsqEPvlfATTIAENIRYGREDVTMDEIEKAVKeanAY--DFIMKlPHQFDTLVgergAQLSGGQKQRIAIARALVR 546
Cdd:PRK11147  394 L-----DP---EKTVMDNLAEGKQEVMVNGRPRHVL---GYlqDFLFH-PKRAMTPV----KALSGGERNRLLLARLFLK 457
                         170
                  ....*....|....*..
gi 6755046    547 NPKILLLDEATSALDTE 563
Cdd:PRK11147  458 PSNLLILDEPTNDLDVE 474
ABC_6TM_exporter_like cd18540
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
706-969 5.91e-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: 349984 [Multi-domain]  Cd Length: 295  Bit Score: 59.03  E-value: 5.91e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   706 WPYLLVGVLCAVINGCIQPVFAIVFSRIVGVFSRDDDHETKRQncnLFSLFFLVMGLISFVTYFFQGFTfGKAGEILTKR 785
Cdd:cd18540    1 KKLLILLIILMLLVALLDAVFPLLTKYAIDHFITPGTLDGLTG---FILLYLGLILIQALSVFLFIRLA-GKIEMGVSYD 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   786 VRYMVFKSMLRQDISWFDdhKNSTGSLTTRLASDASSVKGAMGARLAVVTQNVANLGTGVILSLVYGWQLTLLLVVIIP- 864
Cdd:cd18540   77 LRKKAFEHLQTLSFSYFD--KTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVPv 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   865 LIVLGGIIEMKLLSGQALKDKKQLEISGKIaTEAIENFRTIVSLTREQK----F----ETMYAQSlqvpyrnaMKKAHVF 936
Cdd:cd18540  155 LAVVSIYFQKKILKAYRKVRKINSRITGAF-NEGITGAKTTKTLVREEKnlreFkeltEEMRRAS--------VRAARLS 225
                        250       260       270
                 ....*....|....*....|....*....|...
gi 6755046   937 GITFSFTQAMMYFSYAACFRFGAYLVAQQLMTF 969
Cdd:cd18540  226 ALFLPIVLFLGSIATALVLWYGGILVLAGAITI 258
ABC_6TM_Rv0194_D2_like cd18546
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ...
752-968 5.93e-09

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: 58.65  E-value: 5.93e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   752 LFSLFFLVMGLISFVTYFFQGFTFGKAGEILTKRVRYMVFKSMLRQDISWFDDHKnsTGSLTTRLASDASSVKGAMGARL 831
Cdd:cd18546   40 LAAAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFAHLQRLSLDFHERET--SGRIMTRMTSDIDALSELLQTGL 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   832 AVVTQNVANL-GTGVILsLVYGWQLTLLLVVIIPLIVLGGII---EMKLLSGQAlkdkkQLEISGKIAT--EAIENFRTI 905
Cdd:cd18546  118 VQLVVSLLTLvGIAVVL-LVLDPRLALVALAALPPLALATRWfrrRSSRAYRRA-----RERIAAVNADlqETLAGIRVV 191
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6755046   906 VSLTREQKFETMYAQsLQVPYRNAMKKAH-VFGITFSFTQAMMYFSYAACFRFGAYLVAQQLMT 968
Cdd:cd18546  192 QAFRRERRNAERFAE-LSDDYRDARLRAQrLVAIYFPGVELLGNLATAAVLLVGAWRVAAGTLT 254
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
409-584 6.10e-09

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 60.03  E-value: 6.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   409 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRY-LREIIGVVS----QEPVLFATTI 483
Cdd:COG1129  268 VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDaIRAGIAYVPedrkGEGLVLDLSI 347
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   484 AENI------RYGREDVtMDEiEKAVKEANAY--DFIMKLPHQfDTLVGergaQLSGGQKQRIAIARALVRNPKILLLDE 555
Cdd:COG1129  348 RENItlasldRLSRGGL-LDR-RRERALAEEYikRLRIKTPSP-EQPVG----NLSGGNQQKVVLAKWLATDPKVLILDE 420
                        170       180       190
                 ....*....|....*....|....*....|
gi 6755046   556 ATSALDTESEAVVQAALDK-AREGRTTIVI 584
Cdd:COG1129  421 PTRGIDVGAKAEIYRLIRElAAEGKAVIVI 450
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
1049-1263 6.42e-09

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: 60.80  E-value: 6.42e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    1049 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQlNVQWLRAHLGIVSQEPILFDCSIA-E 1127
Cdd:TIGR01257 1953 PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDVHQNMGYCPQFDAIDDLLTGrE 2031
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    1128 NIAYGDNSRAVSHEEIVRAA----KEANIHQFIDSLPDKYntrvgdkgtqlSGGQKQRIAIARALVRQPHILLLDEATSA 1203
Cdd:TIGR01257 2032 HLYLYARLRGVPAEEIEKVAnwsiQSLGLSLYADRLAGTY-----------SGGNKRKLSTAIALIGCPPLVLLDEPTTG 2100
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6755046    1204 LDTESEKVVQEAL-DKAREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLLAQKG 1263
Cdd:TIGR01257 2101 MDPQARRMLWNTIvSIIREGRAVVLTSHSMEECEAlCTRLAIMVKGAFQCLGTIQHLKSKFG 2162
ABC_6TM_PCAT1_LagD_like cd18570
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ...
751-1003 8.31e-09

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: 58.23  E-value: 8.31e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   751 NLFSLFFLVMGLISFVTYFFQGFTFGKAGEILTKRVRYMVFKSMLRQDISWFDDHKnsTGSLTTRLaSDASSVKGAmgar 830
Cdd:cd18570   42 NIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILGYFKHLLKLPLSFFETRK--TGEIISRF-NDANKIREA---- 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   831 lavVTQNVANL--------GTGVILsLVYGWQLTLLLVVIIPLIVLGGIIEMKLLSGqalKDKKQLEISGKIATEAIENF 902
Cdd:cd18570  115 ---ISSTTISLfldllmviISGIIL-FFYNWKLFLITLLIIPLYILIILLFNKPFKK---KNREVMESNAELNSYLIESL 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   903 R---TIVSLTREQKFetmyAQSLQVPYRNAMKKAHVFGITF----SFTQAMMYFSYAACFRFGAYLVAQ------QLMTF 969
Cdd:cd18570  188 KgieTIKSLNAEEQF----LKKIEKKFSKLLKKSFKLGKLSnlqsSIKGLISLIGSLLILWIGSYLVIKgqlslgQLIAF 263
                        250       260       270
                 ....*....|....*....|....*....|....
gi 6755046   970 eNVMLVFsavVFGAMAagNTSSFAPDYAKAKVSA 1003
Cdd:cd18570  264 -NALLGY---FLGPIE--NLINLQPKIQEAKVAA 291
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
1051-1242 9.93e-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: 57.62  E-value: 9.93e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1051 LQGLSLEVKKGQTLALVGSSGCGKSTVVqlLERFYDPMAGSVFLDGKEIKQLNVQWLRAHLG---IVSQEPI-------- 1119
Cdd:cd03271   11 LKNIDVDIPLGVLTCVTGVSGSGKSSLI--NDTLYPALARRLHLKKEQPGNHDRIEGLEHIDkviVIDQSPIgrtprsnp 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1120 -----LFD------CSIAENIAYGDNSRAVSH---------EEIVRAAKE-----ANIHQFIDSLPD---KYnTRVGDKG 1171
Cdd:cd03271   89 atytgVFDeirelfCEVCKGKRYNRETLEVRYkgksiadvlDMTVEEALEffeniPKIARKLQTLCDvglGY-IKLGQPA 167
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6755046  1172 TQLSGGQKQRIAIARALVRQ---PHILLLDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIV 1242
Cdd:cd03271  168 TTLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRLVDkGNTVVVIEHNLDVIKCADWII 242
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
1059-1244 1.07e-08

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: 59.41  E-value: 1.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1059 KKGQTLALVGSSGCGKSTVVQLLerfydpmAGSvfldgkeikqlnvqwLRAHLGIVSQEPilfdcSIAENIAY------G 1132
Cdd:COG1245   97 KKGKVTGILGPNGIGKSTALKIL-------SGE---------------LKPNLGDYDEEP-----SWDEVLKRfrgtelQ 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1133 DNSRAVSHEEIVRAAKEanihQFIDSLPDKYNTRVGD-------KG-------------------TQLSGGQKQRIAIAR 1186
Cdd:COG1245  150 DYFKKLANGEIKVAHKP----QYVDLIPKVFKGTVREllekvdeRGkldelaeklglenildrdiSELSGGELQRVAIAA 225
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6755046  1187 ALVRQPHILLLDEATSALD----TESEKVVQEAldkAREGRTCIVIAHRLSTIQN-ADLIVVI 1244
Cdd:COG1245  226 ALLRDADFYFFDEPSSYLDiyqrLNVARLIREL---AEEGKYVLVVEHDLAILDYlADYVHIL 285
ABC_6TM_ABCC_D2 cd18580
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ...
113-339 1.19e-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: 57.90  E-value: 1.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   113 YAYYYTGIGAGVLIVAYIQVSLW----CLAAGRQIHkirQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDK 188
Cdd:cd18580   40 YLGVYAALLVLASVLLVLLRWLLfvlaGLRASRRLH---DKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLA 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   189 IGMFFQSITTFLAGFIIGFISGWkltLVILAVSPLIGLSSALWAKVLTsfTNKELQ---AYAKAGAVA--EEVLAAIRTV 263
Cdd:cd18580  117 LLDFLQSLFSVLGSLIVIAIVSP---YFLIVLPPLLVVYYLLQRYYLR--TSRQLRrleSESRSPLYShfSETLSGLSTI 191
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6755046   264 IAFGGQQKELERYNKNLEEaknvgikkaitasiSIGIAYLLVYASYALAFWYG--TSLVLsneysigeVLTVFFSILL 339
Cdd:cd18580  192 RAFGWQERFIEENLRLLDA--------------SQRAFYLLLAVQRWLGLRLDllGALLA--------LVVALLAVLL 247
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
1048-1261 1.33e-08

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


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 58.17  E-value: 1.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1048 IPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRaHLGIV----SQepILFDC 1123
Cdd:COG4586   35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFAR-RIGVVfgqrSQ--LWWDL 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1124 SIAENIA-----YGdnsraVSHEEIvraakEANIHQFID--SLPDKYNTRVgdkgTQLSGGQKQRIAIARALVRQPHILL 1196
Cdd:COG4586  112 PAIDSFRllkaiYR-----IPDAEY-----KKRLDELVEllDLGELLDTPV----RQLSLGQRMRCELAAALLHRPKILF 177
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6755046  1197 LDEATSALDTESEKVVQEALDK--AREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLLAQ 1261
Cdd:COG4586  178 LDEPTIGLDVVSKEAIREFLKEynRERGTTILLTSHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKER 245
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
1036-1208 1.43e-08

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: 59.18  E-value: 1.43e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    1036 NGVQFNYPtrPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLlerfydpMAGsvfLD----GKEIKQLNVQwlrahL 1111
Cdd:TIGR03719    8 NRVSKVVP--PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRI-------MAG---VDkdfnGEARPQPGIK-----V 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    1112 GIVSQEPILfDCS--IAENIAYG--------DNSRAVSH-------------------EEIVRAAKEANIHQFIDSLPDK 1162
Cdd:TIGR03719   71 GYLPQEPQL-DPTktVRENVEEGvaeikdalDRFNEISAkyaepdadfdklaaeqaelQEIIDAADAWDLDSQLEIAMDA 149
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 6755046    1163 YNTRVGD-KGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTES 1208
Cdd:TIGR03719  150 LRCPPWDaDVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES 196
PLN03073 PLN03073
ABC transporter F family; Provisional
1033-1256 1.63e-08

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 59.10  E-value: 1.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1033 VKFNGVQFNYPTRPNIpvLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKE----IKQLNVQWLR 1108
Cdd:PLN03073  509 ISFSDASFGYPGGPLL--FKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVrmavFSQHHVDGLD 586
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1109 ahlgiVSQEPILFdcsiaeniaygdnsravsHEEIVRAAKEANIHQFIDSLPDKYNTRVGDKGTqLSGGQKQRIAIARAL 1188
Cdd:PLN03073  587 -----LSSNPLLY------------------MMRCFPGVPEQKLRAHLGSFGVTGNLALQPMYT-LSGGQKSRVAFAKIT 642
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1189 VRQPHILLLDEATSALDTESEKVVQEALDKAREGrtCIVIAHRLSTIQNA-DLIVVIENGKVKE-HGTHQ 1256
Cdd:PLN03073  643 FKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGG--VLMVSHDEHLISGSvDELWVVSEGKVTPfHGTFH 710
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
1046-1233 1.70e-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: 56.99  E-value: 1.70e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1046 PNIPVLQGLSLeVKKGQTLALVGSSGCGKSTVVQLLE--------RFYDPMAGSVFLD---GKEIKQLNVQWLRAHLGI- 1113
Cdd:cd03236   12 PNSFKLHRLPV-PREGQVLGLVGPNGIGKSTALKILAgklkpnlgKFDDPPDWDEILDefrGSELQNYFTKLLEGDVKVi 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1114 -----VSQEPILFDCSIAENIAYGDNSRAVshEEIVraaKEANIHQFIDSLPDkyntrvgdkgtQLSGGQKQRIAIARAL 1188
Cdd:cd03236   91 vkpqyVDLIPKAVKGKVGELLKKKDERGKL--DELV---DQLELRHVLDRNID-----------QLSGGELQRVAIAAAL 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 6755046  1189 VRQPHILLLDEATSALDT----ESEKVVQEAldkAREGRTCIVIAHRLS 1233
Cdd:cd03236  155 ARDADFYFFDEPSSYLDIkqrlNAARLIREL---AEDDNYVLVVEHDLA 200
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
409-614 2.32e-08

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: 58.87  E-value: 2.32e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     409 LKGLNLKVKSGQTVALVGNSGCGKSTTVQ------LMQRL---------YDPLEG------VVSID----GQDIRTINVR 463
Cdd:TIGR00630  624 LKNITVSIPLGLFTCITGVSGSGKSTLINdtlypaLANRLngaktvpgrYTSIEGlehldkVIHIDqspiGRTPRSNPAT 703
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     464 YlreiIGVVSQEPVLFATT------------IAENIRYGRED---------VTM-------------------------- 496
Cdd:TIGR00630  704 Y----TGVFDEIRELFAETpeakvrgytpgrFSFNVKGGRCEacqgdgvikIEMhflpdvyvpcevckgkrynretlevk 779
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     497 -------DEIEKAVKEAnaYDFIMKLP---HQFDTLV---------GERGAQLSGGQKQRIAIARALVR---NPKILLLD 554
Cdd:TIGR00630  780 ykgkniaDVLDMTVEEA--YEFFEAVPsisRKLQTLCdvglgyirlGQPATTLSGGEAQRIKLAKELSKrstGRTLYILD 857
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     555 EATSALDTESEA----VVQAALDKareGRTTIVIAHRLSTVRNADVI------AGFDGGVIVEQGNHDEL 614
Cdd:TIGR00630  858 EPTTGLHFDDIKklleVLQRLVDK---GNTVVVIEHNLDVIKTADYIidlgpeGGDGGGTVVASGTPEEV 924
ABC_6TM_exporter_like cd18564
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
752-915 2.70e-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: 350008 [Multi-domain]  Cd Length: 307  Bit Score: 57.14  E-value: 2.70e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   752 LFSLFFLVMGLISFVTYFFQGFTFGKAGEILTKRVRYMVFKSMLRQDISWFDDHKnsTGSLTTRLASDASSVKG-AMGAR 830
Cdd:cd18564   55 LAAAALVGIALLRGLASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRR--TGDLLSRLTGDVGAIQDlLVSGV 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   831 LAVVTQNVANLGTGVILsLVYGWQLTLLLVVIIPLIVLGgiieMKLLSG---QALKDKKQLEisGKIAT---EAIENFRT 904
Cdd:cd18564  133 LPLLTNLLTLVGMLGVM-FWLDWQLALIALAVAPLLLLA----ARRFSRrikEASREQRRRE--GALASvaqESLSAIRV 205
                        170
                 ....*....|.
gi 6755046   905 IVSLTREQKFE 915
Cdd:cd18564  206 VQAFGREEHEE 216
ABC_6TM_CyaB_HlyB_like cd18588
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ...
194-343 4.39e-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: 4.39e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   194 QSITTFL-AGFIIGFIS-----GWKLTLVILAVSPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFG 267
Cdd:cd18588  118 SALTLVLdLVFSVVFLAvmfyySPTLTLIVLASLPLYALLSLLVTPILRRRLEEKFQRGAENQSFLVETVTGIETVKSLA 197
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6755046   268 GQQKELERYNKNLEEAKNVGIKKAITASISIGIAYLLVYASYALAFWYGTSLVLSNEYSIGEVltVFFSILLGTFS 343
Cdd:cd18588  198 VEPQFQRRWEELLARYVKASFKTANLSNLASQIVQLIQKLTTLAILWFGAYLVMDGELTIGQL--IAFNMLAGQVS 271
ABC_6TM_PrtD_LapB_HlyB_like cd18566
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ...
754-988 5.14e-08

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: 56.05  E-value: 5.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   754 SLFFLVMG-----LISFVTYFFQGFTFGKAGEILTKRVRYMVFKSMLRQDISWFDdhKNSTGSLTTRLAsDASSVKGAMG 828
Cdd:cd18566   40 TLQVLVIGvviaiLLESLLRLLRSYILAWIGARFDHRLSNAAFEHLLSLPLSFFE--REPSGAHLERLN-SLEQIREFLT 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   829 ARLAVVTQNVANLGTGVILSLVYGWQLTLLLVVIIPLIVLGGIIEMKLLSgQALKDK-KQLEISGKIATEAIENFRTIVS 907
Cdd:cd18566  117 GQALLALLDLPFVLIFLGLIWYLGGKLVLVPLVLLGLFVLVAILLGPILR-RALKERsRADERRQNFLIETLTGIHTIKA 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   908 LTREQ----KFETMYAQSLQVPYRNAMKKAHVFGITFSFTQAMMyfsyAACFRFGAYLVAQQLMTfenvmlvfsavvFGA 983
Cdd:cd18566  196 MAMEPqmlrRYERLQANAAYAGFKVAKINAVAQTLGQLFSQVSM----VAVVAFGALLVINGDLT------------VGA 259

                 ....*
gi 6755046   984 MAAGN 988
Cdd:cd18566  260 LIACT 264
ABC_6TM_exporter_like cd18565
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
752-981 5.36e-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: 350009 [Multi-domain]  Cd Length: 313  Bit Score: 56.04  E-value: 5.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   752 LFSLFFLVMGLISFVTYFFQGFTFGKAGEILTKRVRYMVFKSMLRQDISWFDDHknSTGSLTTRLASDASSVKGAMGARL 831
Cdd:cd18565   55 LLGGLTVAAFLLESLFQYLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDR--QTGDLMSVLNNDVNQLERFLDDGA 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   832 AVVTQNVAN-LGTGVILsLVYGWQLTLLLVVIIPLIVLGGIIEMKLLSGQALKDKKQL-EISGKIATeAIENFRTIVSLT 909
Cdd:cd18565  133 NSIIRVVVTvLGIGAIL-FYLNWQLALVALLPVPLIIAGTYWFQRRIEPRYRAVREAVgDLNARLEN-NLSGIAVIKAFT 210
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6755046   910 REQkFET--MYAQSLQvpYRNAMKKAHVFGITFSFT-QAMMYFSYAACFRFGAYLVAQQLMTFENVMLVFSAVVF 981
Cdd:cd18565  211 AED-FERerVADASEE--YRDANWRAIRLRAAFFPViRLVAGAGFVATFVVGGYWVLDGPPLFTGTLTVGTLVTF 282
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
1051-1254 5.65e-08

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: 55.11  E-value: 5.65e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1051 LQGLSLEVKKG-----QTLALVGSSGCGKSTVVQLLerfydpmAGSVFLDGKEIKQLNVQwlrahlgiVSQEP----ILF 1121
Cdd:cd03237   10 LGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKML-------AGVLKPDEGDIEIELDT--------VSYKPqyikADY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1122 DCSIAENIAYGDNSRAVSHEEIVRAAKEANIHQFIDS-LPDkyntrvgdkgtqLSGGQKQRIAIARALVRQPHILLLDEA 1200
Cdd:cd03237   75 EGTVRDLLSSITKDFYTHPYFKTEIAKPLQIEQILDReVPE------------LSGGELQRVAIAACLSKDADIYLLDEP 142
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 6755046  1201 TSALDTESE----KVVQEALDKARegRTCIVIAHRLSTIQN-ADLIVVIEnGKVKEHGT 1254
Cdd:cd03237  143 SAYLDVEQRlmasKVIRRFAENNE--KTAFVVEHDIIMIDYlADRLIVFE-GEPSVNGV 198
PRK13543 PRK13543
heme ABC exporter ATP-binding protein CcmA;
402-586 6.03e-08

heme ABC exporter ATP-binding protein CcmA;


Pssm-ID: 184129 [Multi-domain]  Cd Length: 214  Bit Score: 54.85  E-value: 6.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    402 SRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTIN-VRYlreiIGVVSQEPVLFA 480
Cdd:PRK13543   20 SRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDrSRF----MAYLGHLPGLKA 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    481 TTIA-ENIRY-----GREDVTMdeiekavkEANAYDfIMKLPHQFDTLVgergAQLSGGQKQRIAIARALVRNPKILLLD 554
Cdd:PRK13543   96 DLSTlENLHFlcglhGRRAKQM--------PGSALA-IVGLAGYEDTLV----RQLSAGQKKRLALARLWLSPAPLWLLD 162
                         170       180       190
                  ....*....|....*....|....*....|...
gi 6755046    555 EATSALDTESEAVVQAALD-KAREGRTTIVIAH 586
Cdd:PRK13543  163 EPYANLDLEGITLVNRMISaHLRGGGAALVTTH 195
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
1049-1260 6.54e-08

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 56.94  E-value: 6.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1049 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAHlGIV------SQEPILFD 1122
Cdd:PRK10762  266 PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLAN-GIVyisedrKRDGLVLG 344
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1123 CSIAENI---AYGDNSRAVSHeeIVRAAKEANIHQFIDSLPDKYNTRVGDKGTqLSGGQKQRIAIARALVRQPHILLLDE 1199
Cdd:PRK10762  345 MSVKENMsltALRYFSRAGGS--LKHADEQQAVSDFIRLFNIKTPSMEQAIGL-LSGGNQQKVAIARGLMTRPKVLILDE 421
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6755046   1200 ATSALDTESEKVVQEALDKAR-EGRTCIVIAHRLSTIQN-ADLIVVIENGKV-----KEHGTHQQLLA 1260
Cdd:PRK10762  422 PTRGVDVGAKKEIYQLINQFKaEGLSIILVSSEMPEVLGmSDRILVMHEGRIsgeftREQATQEKLMA 489
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
1147-1242 8.64e-08

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: 56.95  E-value: 8.64e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    1147 AKEANIHQFIDSLPD---KYnTRVGDKGTQLSGGQKQRIAIARALVRQ---PHILLLDEATSALDTESEK----VVQEAL 1216
Cdd:TIGR00630  801 EAVPSISRKLQTLCDvglGY-IRLGQPATTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKklleVLQRLV 879
                           90       100
                   ....*....|....*....|....*.
gi 6755046    1217 DKareGRTCIVIAHRLSTIQNADLIV 1242
Cdd:TIGR00630  880 DK---GNTVVVIEHNLDVIKTADYII 902
ABC_6TM_YknV_like cd18545
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ...
751-978 9.07e-08

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: 55.17  E-value: 9.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   751 NLFSLFFLVMGLISFVTYFFQGFTFGKAGEILTKRVRYMVFKSMLRQDISWFDdhKNSTGSLTTRLASDASSVKGAMGAR 830
Cdd:cd18545   40 LIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFD--SRPVGKILSRVINDVNSLSDLLSNG 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   831 LAVVTQNVANL-GTGVILsLVYGWQLTLLLVVIIPLIVLGgiieMKLLSGQALK-----DKKQLEISGKIAtEAIENFRT 904
Cdd:cd18545  118 LINLIPDLLTLvGIVIIM-FSLNVRLALVTLAVLPLLVLV----VFLLRRRARKawqrvRKKISNLNAYLH-ESISGIRV 191
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6755046   905 IVSLTRE----QKFETMYAQSLQVpYRNAMKKAHVFGITFSFTQAmmyFSYAACFRFGAYLVAQQLMTFeNVMLVFSA 978
Cdd:cd18545  192 IQSFAREdeneEIFDELNRENRKA-NMRAVRLNALFWPLVELISA---LGTALVYWYGGKLVLGGAITV-GVLVAFIG 264
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
1057-1241 1.14e-07

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 55.97  E-value: 1.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1057 EVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDgkeikqLNV----QWLRA-HLGIVSQepilFDCSIAENiaY 1131
Cdd:PRK13409  361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE------LKIsykpQYIKPdYDGTVED----LLRSITDD--L 428
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1132 GDNsraVSHEEIVraaKEANIHQFIDSlpdkyntRVGDkgtqLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKV 1211
Cdd:PRK13409  429 GSS---YYKSEII---KPLQLERLLDK-------NVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLA 491
                         170       180       190
                  ....*....|....*....|....*....|..
gi 6755046   1212 VQEALDKAREGR--TCIVIAHRLSTIqnaDLI 1241
Cdd:PRK13409  492 VAKAIRRIAEEReaTALVVDHDIYMI---DYI 520
PRK13543 PRK13543
heme ABC exporter ATP-binding protein CcmA;
1044-1207 1.20e-07

heme ABC exporter ATP-binding protein CcmA;


Pssm-ID: 184129 [Multi-domain]  Cd Length: 214  Bit Score: 53.70  E-value: 1.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1044 TRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNvqwlRA-HLGIVSQEPIL-F 1121
Cdd:PRK13543   20 SRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD----RSrFMAYLGHLPGLkA 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1122 DCSIAENIAY--GDNSRavsheeivRAAKEANIHQFIDSLPDKYNTRVgdkgTQLSGGQKQRIAIARALVRQPHILLLDE 1199
Cdd:PRK13543   96 DLSTLENLHFlcGLHGR--------RAKQMPGSALAIVGLAGYEDTLV----RQLSAGQKKRLALARLWLSPAPLWLLDE 163

                  ....*...
gi 6755046   1200 ATSALDTE 1207
Cdd:PRK13543  164 PYANLDLE 171
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
1055-1261 1.26e-07

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 55.79  E-value: 1.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1055 SLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGS--------VFLDGKEIKQL-NVQWLRAHLGIVSQEPILFDCSI 1125
Cdd:PRK10938   23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGErqsqfshiTRLSFEQLQKLvSDEWQRNNTDMLSPGEDDTGRTT 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1126 AENIAYGdnsravsHEEIVRAAKEANihQF-IDSLPDKyntrvgdKGTQLSGGQKQRIAIARALVRQPHILLLDEATSAL 1204
Cdd:PRK10938  103 AEIIQDE-------VKDPARCEQLAQ--QFgITALLDR-------RFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGL 166
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 6755046   1205 DTESEKVVQEALDK-AREGRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLLAQ 1261
Cdd:PRK10938  167 DVASRQQLAELLASlHQSGITLVLVLNRFDEIPDfVQFAGVLADCTLAETGEREEILQQ 225
ABC_6TM_Rv0194_D1_like cd18543
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ...
755-968 1.65e-07

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: 54.41  E-value: 1.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   755 LFFLVMGLISFVTYFFQGFTFGKAGEILTKRVRYMVFKSMLRQDISWFDdhKNSTGSLTTRLASDASSVKG--AMGARLA 832
Cdd:cd18543   43 LLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFAHLQRLDGAFHD--RWQSGQLLSRATSDLSLVQRflAFGPFLL 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   833 VvtqNVANLGTGVILSLVYGWQLTLLLVVIIPLIVLGGIIEMKLLSGQALKDKKQLeisGKIATEAIEN---FRTIVSLT 909
Cdd:cd18543  121 G---NLLTLVVGLVVMLVLSPPLALVALASLPPLVLVARRFRRRYFPASRRAQDQA---GDLATVVEESvtgIRVVKAFG 194
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6755046   910 RE----QKFETMyAQSLqvpYRNAMKKAHVFGITFSFTQAMMYFSYAACFRFGAYLVAQQLMT 968
Cdd:cd18543  195 RErrelDRFEAA-ARRL---RATRLRAARLRARFWPLLEALPELGLAAVLALGGWLVANGSLT 253
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
400-588 1.79e-07

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: 56.18  E-value: 1.79e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     400 YPSRSEVQILKgLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTiNVRYLREIIGVVSQEPVLf 479
Cdd:TIGR01257 1947 YSGTSSPAVDR-LCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDVHQNMGYCPQFDAI- 2023
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     480 attiaENIRYGRED---------VTMDEIEKAvkeANAYDFIMKLPHQFDTLVGergaQLSGGQKQRIAIARALVRNPKI 550
Cdd:TIGR01257 2024 -----DDLLTGREHlylyarlrgVPAEEIEKV---ANWSIQSLGLSLYADRLAG----TYSGGNKRKLSTAIALIGCPPL 2091
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 6755046     551 LLLDEATSALDTESEAVV-QAALDKAREGRTTIVIAHRL 588
Cdd:TIGR01257 2092 VLLDEPTTGMDPQARRMLwNTIVSIIREGRAVVLTSHSM 2130
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
1058-1271 2.22e-07

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 55.18  E-value: 2.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1058 VKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGkeikqlnvQWlraHLGIVSQEPILFDCSIAENIAYGDNS-R 1136
Cdd:PRK10636   24 INPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPG--------NW---QLAWVNQETPALPQPALEYVIDGDREyR 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1137 AVshEEIVRAAKEAN-------IHQFIDSLpDKYNTR---------VGDKGTQL-------SGGQKQRIAIARALVRQPH 1193
Cdd:PRK10636   93 QL--EAQLHDANERNdghaiatIHGKLDAI-DAWTIRsraasllhgLGFSNEQLerpvsdfSGGWRMRLNLAQALICRSD 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1194 ILLLDEATSALDTESEKVVQEALdKAREGrTCIVIAHR---LSTIqnADLIVVIENGKVKEH-GTHQQLLAQKGIYFSMV 1269
Cdd:PRK10636  170 LLLLDEPTNHLDLDAVIWLEKWL-KSYQG-TLILISHDrdfLDPI--VDKIIHIEQQSLFEYtGNYSSFEVQRATRLAQQ 245

                  ..
gi 6755046   1270 QA 1271
Cdd:PRK10636  246 QA 247
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
391-591 2.51e-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: 54.83  E-value: 2.51e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     391 LEFKNVHFNYPSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYD-PLEGVVSIDGQ--DIRT-------- 459
Cdd:TIGR02633  258 LEARNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGKpvDIRNpaqairag 337
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     460 -INVRYLREIIGVVSQEPVLFATTIAENIRYGREDVTMDEIEKAVKEANAYDFIMKLPHQFDTLvgergAQLSGGQKQRI 538
Cdd:TIGR02633  338 iAMVPEDRKRHGIVPILGVGKNITLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLPI-----GRLSGGNQQKA 412
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 6755046     539 AIARALVRNPKILLLDEATSALDTESEAVVQAALDK-AREGRTTIVIAHRLSTV 591
Cdd:TIGR02633  413 VLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQlAQEGVAIIVVSSELAEV 466
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
1057-1254 2.68e-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: 54.79  E-value: 2.68e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1057 EVKKGQTLALVGSSGCGKSTVVQLLerfydpmAGSVFLDGKEI-KQLNV----QWL--------RAHLGIVSQEPilFDC 1123
Cdd:COG1245  362 EIREGEVLGIVGPNGIGKTTFAKIL-------AGVLKPDEGEVdEDLKIsykpQYIspdydgtvEEFLRSANTDD--FGS 432
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1124 SIAEniaygdnsravshEEIVRAAKeanihqfIDSLPDKYntrVGDkgtqLSGGQKQRIAIARALVRQPHILLLDEATSA 1203
Cdd:COG1245  433 SYYK-------------TEIIKPLG-------LEKLLDKN---VKD----LSGGELQRVAIAACLSRDADLYLLDEPSAH 485
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 6755046  1204 LDTESEKVVQEALDKAREGR--TCIVIAHRLSTIqnaDLI---VVIENGKVKEHGT 1254
Cdd:COG1245  486 LDVEQRLAVAKAIRRFAENRgkTAMVVDHDIYLI---DYIsdrLMVFEGEPGVHGH 538
ABC_6TM_PrtD_LapB_HlyB_like cd18566
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ...
100-340 2.74e-07

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: 53.74  E-value: 2.74e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   100 IISNSSLEEEMAIyayyytGIGAGVLIVAYI-------QVSLWclaAGRQI-HKIRQKFFHAIMNQEIGWFDVHDVGELN 171
Cdd:cd18566   32 VIPNESIPTLQVL------VIGVVIAILLESllrllrsYILAW---IGARFdHRLSNAAFEHLLSLPLSFFEREPSGAHL 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   172 TRLTDdVSKINDgigdkigmFF--QSITT---------FLAgfIIGFISGWkLTLVILAVSPLIGLSSALWAKVLTSFTN 240
Cdd:cd18566  103 ERLNS-LEQIRE--------FLtgQALLAlldlpfvliFLG--LIWYLGGK-LVLVPLVLLGLFVLVAILLGPILRRALK 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   241 KELQAYAKAGAVAEEVLAAIRTVIAFGGQQKELERYNKNLEEAKNVGIKKAITASISIGIAYLLVYASYALAFWYGTSLV 320
Cdd:cd18566  171 ERSRADERRQNFLIETLTGIHTIKAMAMEPQMLRRYERLQANAAYAGFKVAKINAVAQTLGQLFSQVSMVAVVAFGALLV 250
                        250       260
                 ....*....|....*....|
gi 6755046   321 LSNEYSIGEVltVFFSILLG 340
Cdd:cd18566  251 INGDLTVGAL--IACTMLSG 268
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
1050-1216 2.77e-07

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 54.79  E-value: 2.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLdGKEIK-----QLNVQWLRAhlgivSQEPIlfdcs 1124
Cdd:PRK10636  327 ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL-AKGIKlgyfaQHQLEFLRA-----DESPL----- 395
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1125 iaeniaygdnsravshEEIVRAAKEANIHQFIDSLP------DKyntrVGDKGTQLSGGQKQRIAIARALVRQPHILLLD 1198
Cdd:PRK10636  396 ----------------QHLARLAPQELEQKLRDYLGgfgfqgDK----VTEETRRFSGGEKARLVLALIVWQRPNLLLLD 455
                         170
                  ....*....|....*...
gi 6755046   1199 EATSALDTESEKVVQEAL 1216
Cdd:PRK10636  456 EPTNHLDLDMRQALTEAL 473
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
1058-1244 2.84e-07

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 54.81  E-value: 2.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1058 VKKGQTLALVGSSGCGKSTVVQLLerfydpmAGSvfldgkeikqlnvqwLRAHLGIVSQEPilfdcSIAENIAY------ 1131
Cdd:PRK13409   96 PKEGKVTGILGPNGIGKTTAVKIL-------SGE---------------LIPNLGDYEEEP-----SWDEVLKRfrgtel 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1132 GDNSRAVSHEEIVRAAKEanihQFIDSLPDKYNTRVGD--KGT------------------------QLSGGQKQRIAIA 1185
Cdd:PRK13409  149 QNYFKKLYNGEIKVVHKP----QYVDLIPKVFKGKVREllKKVdergkldevverlglenildrdisELSGGELQRVAIA 224
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6755046   1186 RALVRQPHILLLDEATSALDtesekvVQEALDKAR------EGRTCIVIAHRLSTIQN-ADLIVVI 1244
Cdd:PRK13409  225 AALLRDADFYFFDEPTSYLD------IRQRLNVARlirelaEGKYVLVVEHDLAVLDYlADNVHIA 284
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
1172-1208 2.94e-07

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 54.74  E-value: 2.94e-07
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 6755046   1172 TQLSGGQKQRIAIARALVRQPHILLLDEATSALDTES 1208
Cdd:PRK11819  162 TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
391-620 3.35e-07

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 54.51  E-value: 3.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    391 LEFKNVHFNYPSRsevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIdgqdirTINVRylreiIG 470
Cdd:PRK15064  320 LEVENLTKGFDNG---PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKW------SENAN-----IG 385
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    471 VVSQEPVL-FATTIA---------------ENIR--YGREDVTMDEIEKAVKeanaydfimklphqfdtlvgergaQLSG 532
Cdd:PRK15064  386 YYAQDHAYdFENDLTlfdwmsqwrqegddeQAVRgtLGRLLFSQDDIKKSVK------------------------VLSG 441
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    533 GQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKArEGrTTIVIAH------RLSTvrnaDVIAGFDGGVIV 606
Cdd:PRK15064  442 GEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKY-EG-TLIFVSHdrefvsSLAT----RIIEITPDGVVD 515
                         250
                  ....*....|....
gi 6755046    607 EQGNHDELMREKGI 620
Cdd:PRK15064  516 FSGTYEEYLRSQGI 529
ABC_6TM_Rv0194_D2_like cd18546
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ...
118-335 3.39e-07

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: 53.26  E-value: 3.39e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   118 TGIGAGVLIVAYIQVSLWCLAAGRQ----IHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDKIGMFF 193
Cdd:cd18546   42 AAAYLAVVLAGWVAQRAQTRLTGRTgerlLYDLRLRVFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLV 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   194 QSITTFLAGFIIGFISGWKLTLVILAVSPLIGLSSaLWAKVLTSFtnkelqAYAKA-GAVAE------EVLAAIRTVIAF 266
Cdd:cd18546  122 VSLLTLVGIAVVLLVLDPRLALVALAALPPLALAT-RWFRRRSSR------AYRRArERIAAvnadlqETLAGIRVVQAF 194
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6755046   267 GGQQKELERYNKNLEEAKNVGIKKAITASISIGIAYLLVYASYALAFWYGTSLVLSNEYSIGeVLTVFF 335
Cdd:cd18546  195 RRERRNAERFAELSDDYRDARLRAQRLVAIYFPGVELLGNLATAAVLLVGAWRVAAGTLTVG-VLVAFL 262
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
1055-1276 5.46e-07

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 54.19  E-value: 5.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1055 SLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGKeikqLNVQWL---RAHLgivsqEPilfDCSIAENIAY 1131
Cdd:PRK11147  339 SAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTK----LEVAYFdqhRAEL-----DP---EKTVMDNLAE 406
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1132 GDnsravshEEIVRAAKEANIHQFI-DSL--PDKYNTRVgdkgTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTES 1208
Cdd:PRK11147  407 GK-------QEVMVNGRPRHVLGYLqDFLfhPKRAMTPV----KALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVET 475
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6755046   1209 EKVVQEALDkAREGrTCIVIAHRLSTIQNAdlivVIE------NGKVKEH-GTHQQLLAQKGIYFSMVQAGAKRS 1276
Cdd:PRK11147  476 LELLEELLD-SYQG-TVLLVSHDRQFVDNT----VTEcwifegNGKIGRYvGGYHDARQQQAQYLALKQPAVKKK 544
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
1034-1205 6.26e-07

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: 51.49  E-value: 6.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1034 KFNGVQFNYPTRPNIPVLQGLSLEVKKGQTLALVGSSGCGKST----VVQLLERFYDPmAGSVFLDGKEIKQLNVQWlRA 1109
Cdd:cd03233    6 WRNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTllkaLANRTEGNVSV-EGDIHYNGIPYKEFAEKY-PG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1110 HLGIVSQEpilfDCSIAEniaygdnsraVSHEEIVRAAKEANIHQFIdslpdkyntrvgdKGtqLSGGQKQRIAIARALV 1189
Cdd:cd03233   84 EIIYVSEE----DVHFPT----------LTVRETLDFALRCKGNEFV-------------RG--ISGGERKRVSIAEALV 134
                        170
                 ....*....|....*.
gi 6755046  1190 RQPHILLLDEATSALD 1205
Cdd:cd03233  135 SRASVLCWDNSTRGLD 150
PLN03073 PLN03073
ABC transporter F family; Provisional
391-569 7.16e-07

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 53.71  E-value: 7.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    391 LEFKNVHFNYPSRSevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVsidgqdIRTINVRylreiIG 470
Cdd:PLN03073  509 ISFSDASFGYPGGP--LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV------FRSAKVR-----MA 575
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    471 VVSQEPVLFATTIAENIRYgredvtMDEIEKAVKEanaydfiMKLPHQFDT--LVGERGAQ----LSGGQKQRIAIARAL 544
Cdd:PLN03073  576 VFSQHHVDGLDLSSNPLLY------MMRCFPGVPE-------QKLRAHLGSfgVTGNLALQpmytLSGGQKSRVAFAKIT 642
                         170       180
                  ....*....|....*....|....*.
gi 6755046    545 VRNPKILLLDEATSALDTES-EAVVQ 569
Cdd:PLN03073  643 FKKPHILLLDEPSNHLDLDAvEALIQ 668
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
1049-1264 7.71e-07

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 53.36  E-value: 7.71e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1049 PVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVfldgkeikqlnvQWL-RAHLGIVSQEP--------I 1119
Cdd:PRK15064  333 PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV------------KWSeNANIGYYAQDHaydfendlT 400
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1120 LFDCsIAENIAYGDNSRAV---------SHEEIVRAAKeanihqfidslpdkyntrvgdkgtQLSGGQKQRIAIARALVR 1190
Cdd:PRK15064  401 LFDW-MSQWRQEGDDEQAVrgtlgrllfSQDDIKKSVK------------------------VLSGGEKGRMLFGKLMMQ 455
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1191 QPHILLLDEATSALDTESEKVVQEALDKArEGrTCIVIAH------RLSTiqnaDLIVVIENGKVKEHGTHQQLLAQKGI 1264
Cdd:PRK15064  456 KPNVLVMDEPTNHMDMESIESLNMALEKY-EG-TLIFVSHdrefvsSLAT----RIIEITPDGVVDFSGTYEEYLRSQGI 529
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
409-586 1.14e-06

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 52.89  E-value: 1.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    409 LKGLNLKVKSGQ-----TVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDgqdirtINVRYLREIIGVVSQEPV-LFATT 482
Cdd:PRK13409  350 LGDFSLEVEGGEiyegeVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE------LKISYKPQYIKPDYDGTVeDLLRS 423
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    483 IAENIR--YGREDVtmdeIEKavkeanaydfiMKLPHQFDTLVGErgaqLSGGQKQRIAIARALVRNPKILLLDEATSAL 560
Cdd:PRK13409  424 ITDDLGssYYKSEI----IKP-----------LQLERLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHL 484
                         170       180
                  ....*....|....*....|....*...
gi 6755046    561 DTESEAVVQAALDKAREGR--TTIVIAH 586
Cdd:PRK13409  485 DVEQRLAVAKAIRRIAEEReaTALVVDH 512
ABC_6TM_VMR1_D2_like cd18604
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ...
114-270 1.14e-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: 51.70  E-value: 1.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   114 AYY---YTGIGAGVLIVAYIQVSLWC---LAAGRQIHkirQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGD 187
Cdd:cd18604   43 LYYlgiYALISLLSVLLGTLRYLLFFfgsLRASRKLH---ERLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELAD 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   188 KIGMFFQSITTFLAGFIIGFISGWKL---TLVILAVSPLIG---LSSALWAK---------VLTSFTnkelqayakagav 252
Cdd:cd18604  120 SLSSLLESTLSLLVILIAIVVVSPAFllpAVVLAALYVYIGrlyLRASRELKrlesvarspILSHFG------------- 186
                        170
                 ....*....|....*...
gi 6755046   253 aeEVLAAIRTVIAFGGQQ 270
Cdd:cd18604  187 --ETLAGLVTIRAFGAEE 202
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
529-590 1.56e-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: 1.56e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6755046   529 QLSGGQKQRIAIARALVRNPKILLLDEATSALD-TESEAVVQAALDKAREGRTTIVIAHRLST 590
Cdd:COG1245  212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLDiYQRLNVARLIRELAEEGKYVLVVEHDLAI 274
ABC_6TM_exporter_like cd18550
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
755-868 2.65e-06

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: 50.56  E-value: 2.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   755 LFFLVMGLI-----SFVTYFFQGFTFGKAGEILTKRVRYMVFKSMLRQDISWFDDHKnsTGSLTTRLASDASSVKGAMGA 829
Cdd:cd18550   38 LVLLALGMVavavaSALLGVVQTYLSARIGQGVMYDLRVQLYAHLQRMSLAFFTRTR--TGEIQSRLNNDVGGAQSVVTG 115
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 6755046   830 RLAVVTQNVANLGTGVILSLVYGWQLTLLLVVIIPLIVL 868
Cdd:cd18550  116 TLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVL 154
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
403-561 3.30e-06

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 51.16  E-value: 3.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    403 RSEVQILKG-----LNLKVKSGQTVALVGNSGCGKSttvQLMQRLYDPL---EGVVSIDGQDIRTIN--------VRYLR 466
Cdd:PRK10762  257 RLKVDNLSGpgvndVSFTLRKGEILGVSGLMGAGRT---ELMKVLYGALprtSGYVTLDGHEVVTRSpqdglangIVYIS 333
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    467 E-------IIGV-VSQEPVLFA----TTIAENIRYGREDVTMDeiekavkeanayDFIM----KLPHQfDTLVGErgaqL 530
Cdd:PRK10762  334 EdrkrdglVLGMsVKENMSLTAlryfSRAGGSLKHADEQQAVS------------DFIRlfniKTPSM-EQAIGL----L 396
                         170       180       190
                  ....*....|....*....|....*....|.
gi 6755046    531 SGGQKQRIAIARALVRNPKILLLDEATSALD 561
Cdd:PRK10762  397 SGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
ABC_6TM_AarD_CydDC_like cd18561
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ...
138-335 3.32e-06

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: 50.36  E-value: 3.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   138 AAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDKIGMFFQSITTFLAGFIIGFISGWKLTLVI 217
Cdd:cd18561   63 AAQRVKQHLRRRLFAKLLKLGPGYLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVALIL 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   218 LAVSPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQKELERYNKNLEEAKNVGIKKAITASIS 297
Cdd:cd18561  143 LVFALLIPLSPALWDRLAKDTGRRHWAAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLRQATMKVLAVSLLS 222
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 6755046   298 IGIAYLLVYASYALAFWYGTSLVLSNEYSIGEVLTVFF 335
Cdd:cd18561  223 SGIMGLATALGTALALGVGALRVLGGQLTLSSLLLILF 260
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
391-613 3.32e-06

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: 51.47  E-value: 3.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     391 LEFKNVHFNYPSRsevQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIdGQDIRTINVRYLREIIg 470
Cdd:TIGR03719  323 IEAENLTKAFGDK---LLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVKLAYVDQSRDAL- 397
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046     471 vvsqEPvlfATTIAENIRYGredvtMDEIEKAVKEAN--AY--DFIMKLPHQfDTLVGergaQLSGGQKQRIAIARALVR 546
Cdd:TIGR03719  398 ----DP---NKTVWEEISGG-----LDIIKLGKREIPsrAYvgRFNFKGSDQ-QKKVG----QLSGGERNRVHLAKTLKS 460
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 6755046     547 NPKILLLDEATSALDTES-EAVVQAALDKAreGrTTIVIAH-RLSTVRNADVIAGFDGGVIVE--QGNHDE 613
Cdd:TIGR03719  461 GGNVLLLDEPTNDLDVETlRALEEALLNFA--G-CAVVISHdRWFLDRIATHILAFEGDSHVEwfEGNFSE 528
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
404-586 4.36e-06

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 50.94  E-value: 4.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    404 SEVQILKGLNL-------KVKSGQTVALVGNSGCGKSTTVQLmqrlydpLEGVVSIDGQDIRTINVRYLreiiGVVSQE- 475
Cdd:PRK10636    5 SSLQIRRGVRVlldnataTINPGQKVGLVGKNGCGKSTLLAL-------LKNEISADGGSYTFPGNWQL----AWVNQEt 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    476 PVLFATTIAENIRYGREdvtMDEIEKAVKEANAYD---FIMKLPHQFDTL----VGERGAQL------------------ 530
Cdd:PRK10636   74 PALPQPALEYVIDGDRE---YRQLEAQLHDANERNdghAIATIHGKLDAIdawtIRSRAASLlhglgfsneqlerpvsdf 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 6755046    531 SGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALdKAREGrTTIVIAH 586
Cdd:PRK10636  151 SGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWL-KSYQG-TLILISH 204
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
530-609 4.98e-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: 4.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   530 LSGGQKQRIAIARALVRNPK--ILLLDEATSALDTESEAVVQAALDKAR-EGRTTIVIAHRLSTVRNADVI------AGF 600
Cdd:cd03238   88 LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIdLGNTVILIEHNLDVLSSADWIidfgpgSGK 167

                 ....*....
gi 6755046   601 DGGVIVEQG 609
Cdd:cd03238  168 SGGKVVFSG 176
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
1155-1242 5.32e-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: 5.32e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046  1155 FIDSLPDKYNT-----RVGDKGTQLSGGQKQRIAIARALVRQPH--ILLLDEATSALDTESEKVVQEALDKAR-EGRTCI 1226
Cdd:cd03238   64 FIDQLQFLIDVglgylTLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIdLGNTVI 143
                         90
                 ....*....|....*.
gi 6755046  1227 VIAHRLSTIQNADLIV 1242
Cdd:cd03238  144 LIEHNLDVLSSADWII 159
ABC_6TM_CvaB_RaxB_like cd18567
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ...
150-336 5.44e-06

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: 49.77  E-value: 5.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   150 FFHAIMNQEIGWFDVHDVGELNTRLtDDVSKINDGIGDK-IGMFFQSITTFLAGFIIGFISgWKLTLVILAVSPLIGLSS 228
Cdd:cd18567   81 LFRHLLRLPLSYFEKRHLGDIVSRF-GSLDEIQQTLTTGfVEALLDGLMAILTLVMMFLYS-PKLALIVLAAVALYALLR 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   229 ALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAFGGQQKELERYNKNLEEAKNVGIKKAITASISIGIAYLLVYAS 308
Cdd:cd18567  159 LALYPPLRRATEEQIVASAKEQSHFLETIRGIQTIKLFGREAEREARWLNLLVDAINADIRLQRLQILFSAANGLLFGLE 238
                        170       180
                 ....*....|....*....|....*...
gi 6755046   309 YALAFWYGTSLVLSNEYSIGeVLTVFFS 336
Cdd:cd18567  239 NILVIYLGALLVLDGEFTVG-MLFAFLA 265
PRK13541 PRK13541
cytochrome c biogenesis protein CcmA; Provisional
1068-1241 5.49e-06

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184128 [Multi-domain]  Cd Length: 195  Bit Score: 48.71  E-value: 5.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1068 GSSGCGKSTVVQLLERFYDPMAGSVFLDGKEIKQLNVQWLRAhlgIVSQEPILFDCSIAENIAYGdnSRAVSHEEIVRAA 1147
Cdd:PRK13541   33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTY---IGHNLGLKLEMTVFENLKFW--SEIYNSAETLYAA 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1148 keanIHQF-IDSLPDKyntrvgdKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALD-KAREGRTC 1225
Cdd:PRK13541  108 ----IHYFkLHDLLDE-------KCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVmKANSGGIV 176
                         170
                  ....*....|....*.
gi 6755046   1226 IVIAHRLSTIQNADLI 1241
Cdd:PRK13541  177 LLSSHLESSIKSAQIL 192
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
401-633 6.48e-06

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 50.29  E-value: 6.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    401 PSRSEVQILKG------LNLKVKSGQTVALVGNSGCGKSttvQLMQRLY---DPLEGVVSIDGQdirTINVRYLREII-- 469
Cdd:PRK11288  255 EVRLRLDGLKGpglrepISFSVRAGEIVGLFGLVGAGRS---ELMKLLYgatRRTAGQVYLDGK---PIDIRSPRDAIra 328
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    470 GVV------SQEPVLFATTIAENIRYG--REDVTMDEIEKAVKEA-NAYDFIMKL----PHQfDTLVGergaQLSGGQKQ 536
Cdd:PRK11288  329 GIMlcpedrKAEGIIPVHSVADNINISarRHHLRAGCLINNRWEAeNADRFIRSLniktPSR-EQLIM----NLSGGNQQ 403
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    537 RIAIARALVRNPKILLLDEATSALDTESEAVVQAAL-DKAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDEL 614
Cdd:PRK11288  404 KAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIyELAAQGVAVLFVSSDLPEVLGvADRIVVMREGRIAGELAREQA 483
                         250
                  ....*....|....*....
gi 6755046    615 MREKGIyfKLVMTQTRGNE 633
Cdd:PRK11288  484 TERQAL--SLALPRTSAAV 500
ABC_6TM_exporter_like cd18778
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
709-968 6.60e-06

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: 49.46  E-value: 6.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   709 LLVGVLCAVINGCIQPVFAIVFSRIVgvfsrDDDHETKRQncnLFSLFFLVMGLIsfVTYFFQ-GFTFG------KAGEI 781
Cdd:cd18778    1 LILTLLCALLSTLLGLVPPWLIRELV-----DLVTIGSKS---LGLLLGLALLLL--GAYLLRaLLNFLriylnhVAEQK 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   782 LTKRVRYMVFKSMLRQDISWFDDHknSTGSLTTRLASDASSVKgamgaRLAV--VTQNVAN----LGTGVILsLVYGWQL 855
Cdd:cd18778   71 VVADLRSDLYDKLQRLSLRYFDDR--QTGDLMSRVINDVANVE-----RLIAdgIPQGITNvltlVGVAIIL-FSINPKL 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   856 TLLLVVIIPLIVLGGIIEMKLLSGQAlkdKKQLEISGKIATEAIENF---RTIVSLTREQ----KFETmYAQSLQVPYRN 928
Cdd:cd18778  143 ALLTLIPIPFLALGAWLYSKKVRPRY---RKVREALGELNALLQDNLsgiREIQAFGREEeeakRFEA-LSRRYRKAQLR 218
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 6755046   929 AMKKAHVFGITFSFTQAMmyfSYAACFRFGAYLVAQQLMT 968
Cdd:cd18778  219 AMKLWAIFHPLMEFLTSL---GTVLVLGFGGRLVLAGELT 255
ABC_6TM_YwjA_like cd18549
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ...
752-969 6.78e-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: 49.37  E-value: 6.78e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   752 LFSLFFLVMGLISFVTYFfqgftfgkaGEILTKRVRY-M---VFKSMLRQDISWFDDHKnsTGSLTTRLASDASSVkgam 827
Cdd:cd18549   48 LLALYILRTLLNYFVTYW---------GHVMGARIETdMrrdLFEHLQKLSFSFFDNNK--TGQLMSRITNDLFDI---- 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   828 gARLA------VVTQNVANLGTGVILSLVYgWQLTLLLVVIIPLIVLGGIIEMKLLSGQALKDKKQL-EISGKIaTEAIE 900
Cdd:cd18549  113 -SELAhhgpedLFISIITIIGSFIILLTIN-VPLTLIVFALLPLMIIFTIYFNKKMKKAFRRVREKIgEINAQL-EDSLS 189
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6755046   901 NFRTIVSLTRE----QKFETMYAQslqvpYRNAMKKAH-VFGITFSFTQAMMYFSYAACFRFGAYLVAQQLMTF 969
Cdd:cd18549  190 GIRVVKAFANEeyeiEKFDEGNDR-----FLESKKKAYkAMAYFFSGMNFFTNLLNLVVLVAGGYFIIKGEITL 258
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
408-648 8.27e-06

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 50.17  E-value: 8.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    408 ILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDgqdiRTINVRYlreiigvvsqepvlFATtiaENI 487
Cdd:PRK10636  327 ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLA----KGIKLGY--------------FAQ---HQL 385
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    488 RYGREDVT----MDEIEKAVKEANAYDFIMKLPHQFDTlVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTE 563
Cdd:PRK10636  386 EFLRADESplqhLARLAPQELEQKLRDYLGGFGFQGDK-VTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLD 464
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    564 -SEAVVQAALDkaREGrTTIVIAHRLSTVRNA--DVIAGFDGGVIVEQGNHDELMRekgIYFKLVMTQTRGNEIEPGNNA 640
Cdd:PRK10636  465 mRQALTEALID--FEG-ALVVVSHDRHLLRSTtdDLYLVHDGKVEPFDGDLEDYQQ---WLSDVQKQENQTDEAPKENNA 538

                  ....*...
gi 6755046    641 YGSQSDTD 648
Cdd:PRK10636  539 NSAQARKD 546
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
409-586 9.25e-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: 49.78  E-value: 9.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   409 LKGLNLKVKSGQ-----TVALVGNSGCGKSTTVQLmqrlydpLEGVVSIDGQDIR-TINVRYLREIIGVVSQEPVlfatt 482
Cdd:COG1245  351 YGGFSLEVEGGEiregeVLGIVGPNGIGKTTFAKI-------LAGVLKPDEGEVDeDLKISYKPQYISPDYDGTV----- 418
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   483 iaenirygrEDVTMDEIEKAVKEANAYDFIMK---LPHQFDTLVGErgaqLSGGQKQRIAIARALVRNPKILLLDEATSA 559
Cdd:COG1245  419 ---------EEFLRSANTDDFGSSYYKTEIIKplgLEKLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAH 485
                        170       180
                 ....*....|....*....|....*....
gi 6755046   560 LDTESEAVVQAALDKAREGR--TTIVIAH 586
Cdd:COG1245  486 LDVEQRLAVAKAIRRFAENRgkTAMVVDH 514
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
1044-1251 1.07e-05

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 49.78  E-value: 1.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1044 TRPNIPVLQGLSLEVKKGQTLALVGSSGCGKStvvQLLERFY--DPMA-GSVFLDGKEIKQLN-VQWLRAHLGIVSQ--- 1116
Cdd:PRK09700  272 TSRDRKKVRDISFSVCRGEILGFAGLVGSGRT---ELMNCLFgvDKRAgGEIRLNGKDISPRSpLDAVKKGMAYITEsrr 348
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1117 EPILF-DCSIAENIA---------YGDNSRAVSHEEIVRAAKEANihqfiDSLPDKYNTrVGDKGTQLSGGQKQRIAIAR 1186
Cdd:PRK09700  349 DNGFFpNFSIAQNMAisrslkdggYKGAMGLFHEVDEQRTAENQR-----ELLALKCHS-VNQNITELSGGNQQKVLISK 422
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6755046   1187 ALVRQPHILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQNA-DLIVVIENGKVKE 1251
Cdd:PRK09700  423 WLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQlADDGKVILMVSSELPEIITVcDRIAVFCEGRLTQ 489
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
1138-1248 1.12e-05

Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 50.11  E-value: 1.12e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    1138 VSHEEivRAAKEANIHQFIDSLPDKYNTRVGD---KGtqLSGGQKQRIAIARALVRQPHILLLDEATSALDTESekvvqe 1214
Cdd:TIGR00956  175 VSREE--YAKHIADVYMATYGLSHTRNTKVGNdfvRG--VSGGERKRVSIAEASLGGAKIQCWDNATRGLDSAT------ 244
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 6755046    1215 ALDKAREGRTCIVIAHRLSTI------QNA----DLIVVIENGK 1248
Cdd:TIGR00956  245 ALEFIRALKTSANILDTTPLVaiyqcsQDAyelfDKVIVLYEGY 288
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
416-588 1.48e-05

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 49.42  E-value: 1.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    416 VKSGQTVALVGNSGCGKSTTV-----QLMQRLYDPlEGVVSID-------GQDIRTinvrYLREiigvVSQEPVlfatTI 483
Cdd:PRK13409   96 PKEGKVTGILGPNGIGKTTAVkilsgELIPNLGDY-EEEPSWDevlkrfrGTELQN----YFKK----LYNGEI----KV 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    484 AENIRYgredvtMDEIEKAVKeANAYDFIMKlphqfdtlVGERGA-------------------QLSGGQKQRIAIARAL 544
Cdd:PRK13409  163 VHKPQY------VDLIPKVFK-GKVRELLKK--------VDERGKldevverlglenildrdisELSGGELQRVAIAAAL 227
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 6755046    545 VRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRL 588
Cdd:PRK13409  228 LRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDL 271
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
1033-1234 1.65e-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: 49.16  E-value: 1.65e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    1033 VKFNGVQFNYPTRPnipVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLdGKEIKQLNVQWLRAHLg 1112
Cdd:TIGR03719  323 IEAENLTKAFGDKL---LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVKLAYVDQSRDAL- 397
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    1113 ivsqEPilfDCSIAENIAYGdnsravsHEEIVRAAKEANIHQFIDSlpdkYNTRVGD---KGTQLSGGQKQRIAIARALV 1189
Cdd:TIGR03719  398 ----DP---NKTVWEEISGG-------LDIIKLGKREIPSRAYVGR----FNFKGSDqqkKVGQLSGGERNRVHLAKTLK 459
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 6755046    1190 RQPHILLLDEATSALDTESEKVVQEALDKAreGRTCIVIAH------RLST 1234
Cdd:TIGR03719  460 SGGNVLLLDEPTNDLDVETLRALEEALLNF--AGCAVVISHdrwfldRIAT 508
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
388-617 2.21e-05

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 48.47  E-value: 2.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    388 MGNLEFKNVHFnypSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVRYLRE 467
Cdd:PRK10938    1 MSSLQISQGTF---RLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQK 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    468 IigvVSQEpvlFATTIAENIRYGREDV---TMDEIEKAVKEANAydfIMKLPHQF--DTLVGERGAQLSGGQKQRIAIAR 542
Cdd:PRK10938   78 L---VSDE---WQRNNTDMLSPGEDDTgrtTAEIIQDEVKDPAR---CEQLAQQFgiTALLDRRFKYLSTGETRKTLLCQ 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6755046    543 ALVRNPKILLLDEATSALDTESEAVVQAALDK-AREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDELMRE 617
Cdd:PRK10938  149 ALMSEPDLLILDEPFDGLDVASRQQLAELLASlHQSGITLVLVLNRFDEIPDfVQFAGVLADCTLAETGEREEILQQ 225
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
1174-1245 2.63e-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: 46.03  E-value: 2.63e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6755046  1174 LSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTIQN-ADLIVVIE 1245
Cdd:cd03222   72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEegKKTALVVEHDLAVLDYlSDRIHVFE 146
ABC_6TM_T1SS_like cd18779
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ...
194-349 2.87e-05

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: 47.54  E-value: 2.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   194 QSITTFL-AGFIIGFIsgwkltLVILAVSPLIGL----SSALWAKVLTSF-------TNKELQAYAKAGAVAEEVLAAIR 261
Cdd:cd18779  118 QTLSALLdGTLVLGYL------ALLFAQSPLLGLvvlgLAALQVALLLATrrrvrelMARELAAQAEAQSYLVEALSGIE 191
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   262 TVIAFGGQQKELERYNKNLEEAKNVGIKKAITASISIGIAYLLVYASYALAFWYGTSLVLSNEYSIGEVLTvffsilLGT 341
Cdd:cd18779  192 TLKASGAEDRALDRWSNLFVDQLNASLRRGRLDALVDALLATLRLAAPLVLLWVGAWQVLDGQLSLGTMLA------LNA 265

                 ....*...
gi 6755046   342 FSIGHLAP 349
Cdd:cd18779  266 LAGAFLAP 273
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
530-602 3.00e-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: 46.03  E-value: 3.00e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6755046   530 LSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKARE--GRTTIVIAHRLSTVRN-ADVIAGFDG 602
Cdd:cd03222   72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEegKKTALVVEHDLAVLDYlSDRIHVFEG 147
PRK13541 PRK13541
cytochrome c biogenesis protein CcmA; Provisional
391-597 5.50e-05

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184128 [Multi-domain]  Cd Length: 195  Bit Score: 45.63  E-value: 5.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    391 LEFKNVHFNypsrSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTInvrylreiig 470
Cdd:PRK13541    2 LSLHQLQFN----IEQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNI---------- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    471 vvsQEPvlFATTIAENIRYGREDVTMDEIEKAVKEANAYDFIMKLPHQF--DTLVGERGAQLSGGQKQRIAIARALVRNP 548
Cdd:PRK13541   68 ---AKP--YCTYIGHNLGLKLEMTVFENLKFWSEIYNSAETLYAAIHYFklHDLLDEKCYSLSSGMQKIVAIARLIACQS 142
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 6755046    549 KILLLDEATSALDTESEAVVQAALD-KAREGRTTIVIAHRLSTVRNADVI 597
Cdd:PRK13541  143 DLWLLDEVETNLSKENRDLLNNLIVmKANSGGIVLLSSHLESSIKSAQIL 192
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
402-603 6.19e-05

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 47.52  E-value: 6.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    402 SRSEVQILKGLNLKVKSGQTVALVGNSGCGKS-----TTVQLMQRL----YDP--------LEGVVSID----GQDIRTI 460
Cdd:PRK00635  604 SKATKHNLKDLTISLPLGRLTVVTGVSGSGKSslindTLVPAVEEFieqgFCSnlsiqwgaISRLVHITrdlpGRSQRSI 683
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    461 NVRY------LREI----------------------IGVVSQEPVLFATTIAEN--------------------IRYGRE 492
Cdd:PRK00635  684 PLTYikafddLRELfaeqprskrlgltkshfsfntpLGACAECQGLGSITTTDNrtsipcpsclgkrflpqvleVRYKGK 763
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    493 DVTmDEIEKAVKEANayDFIMKLPH-----------QFDTL-VGERGAQLSGGQKQRIAIARAL---VRNPKILLLDEAT 557
Cdd:PRK00635  764 NIA-DILEMTAYEAE--KFFLDEPSihekihalcslGLDYLpLGRPLSSLSGGEIQRLKLAYELlapSKKPTLYVLDEPT 840
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 6755046    558 SALDTES-EAVVQAALDKAREGRTTIVIAHRLSTVRNADVIA--GFDGG 603
Cdd:PRK00635  841 TGLHTHDiKALIYVLQSLTHQGHTVVIIEHNMHVVKVADYVLelGPEGG 889
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
529-600 7.69e-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: 44.66  E-value: 7.69e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6755046   529 QLSGGQKQRIAIARAL----VRNPKILLLDEATSALDTES-EAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGF 600
Cdd:cd03227   77 QLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDgQALAEAILEHLVKGAQVIVITHLPELAELADKLIHI 153
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
391-561 7.70e-05

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 46.85  E-value: 7.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    391 LEFKNVHFNYPSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYD-PLEGVVSIDGQDIRTINVR-YLREI 468
Cdd:PRK13549  260 LEVRNLTAWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIRNPQqAIAQG 339
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    469 IGVVSQE-------PVLfatTIAENI------RYGREDVtmdeIEKAVKEANAYDFIMKL----PHQFdtlvgERGAQLS 531
Cdd:PRK13549  340 IAMVPEDrkrdgivPVM---GVGKNItlaaldRFTGGSR----IDDAAELKTILESIQRLkvktASPE-----LAIARLS 407
                         170       180       190
                  ....*....|....*....|....*....|
gi 6755046    532 GGQKQRIAIARALVRNPKILLLDEATSALD 561
Cdd:PRK13549  408 GGNQQKAVLAKCLLLNPKILILDEPTRGID 437
PRK13546 PRK13546
teichoic acids export ABC transporter ATP-binding subunit TagH;
409-617 8.03e-05

teichoic acids export ABC transporter ATP-binding subunit TagH;


Pssm-ID: 184131 [Multi-domain]  Cd Length: 264  Bit Score: 45.96  E-value: 8.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    409 LKGLNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQ-DIRTINVRYLREIIGVvsqepvlfattiaENI 487
Cdd:PRK13546   40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEvSVIAISAGLSGQLTGI-------------ENI 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    488 RYgrEDVTMDEIEKAVKEanaydfIMKLPHQFDTLvGERGAQ----LSGGQKQRIAIARALVRNPKILLLDEATSALDte 563
Cdd:PRK13546  107 EF--KMLCMGFKRKEIKA------MTPKIIEFSEL-GEFIYQpvkkYSSGMRAKLGFSINITVNPDILVIDEALSVGD-- 175
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 6755046    564 sEAVVQAALDKARE----GRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDELMRE 617
Cdd:PRK13546  176 -QTFAQKCLDKIYEfkeqNKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYGELDDVLPK 233
uvrA PRK00349
excinuclease ABC subunit UvrA;
1166-1242 9.14e-05

excinuclease ABC subunit UvrA;


Pssm-ID: 234734 [Multi-domain]  Cd Length: 943  Bit Score: 46.99  E-value: 9.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1166 RVGDKGTQLSGGQKQRIAIARALVRQPH---ILLLDEATSALDTES----EKVVQEALDKareGRTCIVIAHRLSTIQNA 1238
Cdd:PRK00349  823 KLGQPATTLSGGEAQRVKLAKELSKRSTgktLYILDEPTTGLHFEDirklLEVLHRLVDK---GNTVVVIEHNLDVIKTA 899

                  ....
gi 6755046   1239 DLIV 1242
Cdd:PRK00349  900 DWII 903
PLN03073 PLN03073
ABC transporter F family; Provisional
1173-1230 9.47e-05

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 46.78  E-value: 9.47e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 6755046   1173 QLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKARegRTCIVIAH 1230
Cdd:PLN03073  344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWP--KTFIVVSH 399
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
405-619 9.70e-05

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 46.27  E-value: 9.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    405 EVQILKGLNLKVKSGQTVALVGNSGCGKSTTVqLMQRLYDPLEGVVSIDGQdIRTINVRYLREIIGVvsQEPVLFATTIA 484
Cdd:NF000106   25 EVKAVDGVDLDVREGTVLGVLGP*GAA**RGA-LPAHV*GPDAGRRPWRF*-TWCANRRALRRTIG*--HRPVR*GRRES 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    485 ENiryGREDVTM--DEIEKAVKEANAYDFIMKLPHQFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDT 562
Cdd:NF000106  101 FS---GRENLYMigR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDP 177
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 6755046    563 ESE-AVVQAALDKAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIVEQGNHDELMREKG 619
Cdd:NF000106  178 RTRnEVWDEVRSMVRDGATVLLTTQYMEEAEQlAHELTVIDRGRVIADGKVDELKTKVG 236
ABC_6TM_HetC_like cd18568
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ...
845-968 1.16e-04

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: 45.63  E-value: 1.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   845 VILSLVYGWQLTLLLVVIIPLIVLggiieMKLLSGQALK--DKKQLEISGKIAT---EAIENFRTIVSLTREQKF----E 915
Cdd:cd18568  133 LGLMFYYNLQLTLIVLAFIPLYVL-----LTLLSSPKLKrnSREIFQANAEQQSflvEALTGIATIKALAAERPIrwrwE 207
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 6755046   916 TMYAQSLQVPYRNAmKKAHVFGITFSFtqaMMYFSYAACFRFGAYLVAQQLMT 968
Cdd:cd18568  208 NKFAKALNTRFRGQ-KLSIVLQLISSL---INHLGTIAVLWYGAYLVISGQLT 256
GguA NF040905
sugar ABC transporter ATP-binding protein;
1043-1228 1.17e-04

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 46.32  E-value: 1.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1043 PTRPNIPVLQGLSLEVKKGQTLALVGSSGCGKS-TVVQLLERFYDP-MAGSVFLDGKEIKQLNVQWL-----------RA 1109
Cdd:NF040905  268 PLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTeLAMSVFGRSYGRnISGTVFKDGKEVDVSTVSDAidaglayvtedRK 347
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1110 HLGIVSQEPILFDCSIAeniaygdNSRAVSHEEIVRAAKEANIHQfidSLPDKYNTR---VGDKGTQLSGGQKQRIAIAR 1186
Cdd:NF040905  348 GYGLNLIDDIKRNITLA-------NLGKVSRRGVIDENEEIKVAE---EYRKKMNIKtpsVFQKVGNLSGGNQQKVVLSK 417
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 6755046   1187 ALVRQPHILLLDEATSALDT----ESEKVVQEAldkAREGRTCIVI 1228
Cdd:NF040905  418 WLFTDPDVLILDEPTRGIDVgakyEIYTIINEL---AAEGKGVIVI 460
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
1168-1263 1.29e-04

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 45.88  E-value: 1.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1168 GDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESE-KVVQEALDKAREGRTCIVIAHRLSTI-QNADLIVVIE 1245
Cdd:NF000106  139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRnEVWDEVRSMVRDGATVLLTTQYMEEAeQLAHELTVID 218
                          90
                  ....*....|....*...
gi 6755046   1246 NGKVKEHGTHQQLLAQKG 1263
Cdd:NF000106  219 RGRVIADGKVDELKTKVG 236
PRK13546 PRK13546
teichoic acids export ABC transporter ATP-binding subunit TagH;
1051-1261 1.30e-04

teichoic acids export ABC transporter ATP-binding subunit TagH;


Pssm-ID: 184131 [Multi-domain]  Cd Length: 264  Bit Score: 45.19  E-value: 1.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1051 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGSVFLDGkeikQLNVQWLRAhlGIVSQepilfdCSIAENIA 1130
Cdd:PRK13546   40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG----EVSVIAISA--GLSGQ------LTGIENIE 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1131 YGDNSRAVSHEEIVRAAKE----ANIHQFIDSLPDKYntrvgdkgtqlSGGQKQRIAIARALVRQPHILLLDEATSALDt 1206
Cdd:PRK13546  108 FKMLCMGFKRKEIKAMTPKiiefSELGEFIYQPVKKY-----------SSGMRAKLGFSINITVNPDILVIDEALSVGD- 175
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1207 esEKVVQEALDKARE----GRTCIVIAHRLSTIQN-ADLIVVIENGKVKEHGTHQQLLAQ 1261
Cdd:PRK13546  176 --QTFAQKCLDKIYEfkeqNKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYGELDDVLPK 233
PLN03073 PLN03073
ABC transporter F family; Provisional
529-586 1.32e-04

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 46.39  E-value: 1.32e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 6755046    529 QLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKARegRTTIVIAH 586
Cdd:PLN03073  344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWP--KTFIVVSH 399
PLN03140 PLN03140
ABC transporter G family member; Provisional
1050-1233 1.88e-04

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 45.99  E-value: 1.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1050 VLQGLSLEVKKGQTLALVGSSGCGKSTVVQLL--ERFYDPMAGSVFLDGKEIKQLNVQWLRahlGIVSQEPILF-DCSIA 1126
Cdd:PLN03140  895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLagRKTGGYIEGDIRISGFPKKQETFARIS---GYCEQNDIHSpQVTVR 971
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1127 ENIAYGDNSR---AVSHEEIVRAAKEANIHQFIDSLPDKYntrVGDKG-TQLSGGQKQRIAIARALVRQPHILLLDEATS 1202
Cdd:PLN03140  972 ESLIYSAFLRlpkEVSKEEKMMFVDEVMELVELDNLKDAI---VGLPGvTGLSTEQRKRLTIAVELVANPSIIFMDEPTS 1048
                         170       180       190
                  ....*....|....*....|....*....|..
gi 6755046   1203 ALDTESEKVVQEAL-DKAREGRTCIVIAHRLS 1233
Cdd:PLN03140 1049 GLDARAAAIVMRTVrNTVDTGRTVVCTIHQPS 1080
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
1051-1263 2.22e-04

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 45.50  E-value: 2.22e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1051 LQGLSLEVKKGQTLALVGSSGCGKSTVVQLLerfydpmAGSvfldgKEIKQLNVQWL------RAHLGIVSQE------- 1117
Cdd:NF033858   17 LDDVSLDIPAGCMVGLIGPDGVGKSSLLSLI-------AGA-----RKIQQGRVEVLggdmadARHRRAVCPRiaympqg 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1118 ------PILfdcSIAENIA-----YGdNSRAVSHEEIVRAAKEANIHQFIDSLPDKyntrvgdkgtqLSGGQKQRIAIAR 1186
Cdd:NF033858   85 lgknlyPTL---SVFENLDffgrlFG-QDAAERRRRIDELLRATGLAPFADRPAGK-----------LSGGMKQKLGLCC 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1187 ALVRQPHILLLDEATSALDTESEKvvQ-----EALDKAREGRTCIViahrlST--IQNA---DLIVVIENGKVKEHGTHQ 1256
Cdd:NF033858  150 ALIHDPDLLILDEPTTGVDPLSRR--QfweliDRIRAERPGMSVLV-----ATayMEEAerfDWLVAMDAGRVLATGTPA 222

                  ....*..
gi 6755046   1257 QLLAQKG 1263
Cdd:NF033858  223 ELLARTG 229
UvrA COG0178
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
530-621 2.70e-04

Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];


Pssm-ID: 439948 [Multi-domain]  Cd Length: 941  Bit Score: 45.40  E-value: 2.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   530 LSGGQKQRIAIARALVR--NPKIL-LLDEATSALDTESEAVVQAALDKARE-GRTTIVIAHRLSTVRNAD-VI-----AG 599
Cdd:COG0178  827 LSGGEAQRVKLASELSKrsTGKTLyILDEPTTGLHFHDIRKLLEVLHRLVDkGNTVVVIEHNLDVIKTADwIIdlgpeGG 906
                         90       100
                 ....*....|....*....|..
gi 6755046   600 FDGGVIVEQGNHDELMREKGIY 621
Cdd:COG0178  907 DGGGEIVAEGTPEEVAKVKASY 928
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
530-595 3.12e-04

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 45.01  E-value: 3.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    530 LSGGQkQRIA-IARALVRNPKILLLDEATSALDTESEAVVQAALDK-AREGRTTIV------------IAHRLSTVRNAD 595
Cdd:PRK10938  402 LSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVlISEGETQLLfvshhaedapacITHRLEFVPDGD 480
PRK15093 PRK15093
peptide ABC transporter ATP-binding protein SapD;
1173-1260 3.30e-04

peptide ABC transporter ATP-binding protein SapD;


Pssm-ID: 185049 [Multi-domain]  Cd Length: 330  Bit Score: 44.41  E-value: 3.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1173 QLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKARE--GRTCIVIAHRLSTI-QNADLIVVIENGKV 1249
Cdd:PRK15093  158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnnNTTILLISHDLQMLsQWADKINVLYCGQT 237
                          90
                  ....*....|.
gi 6755046   1250 KEHGTHQQLLA 1260
Cdd:PRK15093  238 VETAPSKELVT 248
ABC_6TM_MRP7_D2_like cd18605
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ...
102-286 3.87e-04

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: 44.06  E-value: 3.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   102 SNSSLEEEMAIYAYYYTGIgAGVLIVAYIQVSLW--------CLAAGRQIHKirqKFFHAIMNQEIGWFDVHDVGELNTR 173
Cdd:cd18605   29 SNNSFFNFINDSFNFFLTV-YGFLAGLNSLFTLLraflfaygGLRAARRLHN---KLLSSILFAKMSFFDKTPVGRILNR 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   174 LTDDVSKINDGIGDKIGMFFQSITTfLAGFIIGFISGWKLTLVILAVSPLIG----------------LSSALWAKVLTS 237
Cdd:cd18605  105 FSSDVYTIDDSLPFILNILLAQLFG-LLGYLVVICYQLPWLLLLLLPLAFIYyriqryyratsrelkrLNSVNLSPLYTH 183
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 6755046   238 FTnkelqayakagavaeEVLAAIRTVIAFGGQQKELERYNKNLEEAKNV 286
Cdd:cd18605  184 FS---------------ETLKGLVTIRAFRKQERFLKEYLEKLENNQRA 217
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
530-609 4.46e-04

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: 43.40  E-value: 4.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   530 LSGGQKQRIAIARALVRNPK--ILLLDEATSALDTESEAVVQAALDKARE-GRTTIVIAHRLSTVRNADVI------AGF 600
Cdd:cd03270  138 LSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRLRDlGNTVLVVEHDEDTIRAADHVidigpgAGV 217

                 ....*....
gi 6755046   601 DGGVIVEQG 609
Cdd:cd03270  218 HGGEIVAQG 226
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
392-618 4.58e-04

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 44.39  E-value: 4.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    392 EFKNVhfnypSRSEVQILKGLNLKVKSGQTVALVGNSGCGKSttvQLMQRLY--DPL-EGVVSIDGQDIrTINVRY--LR 466
Cdd:PRK09700  267 EVRNV-----TSRDRKKVRDISFSVCRGEILGFAGLVGSGRT---ELMNCLFgvDKRaGGEIRLNGKDI-SPRSPLdaVK 337
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    467 EIIGVVSQ---EPVLFAT-TIAENI------RYGREDVTM----DEIEKAVKEANAYDFIMKLpHQFDTLVGErgaqLSG 532
Cdd:PRK09700  338 KGMAYITEsrrDNGFFPNfSIAQNMaisrslKDGGYKGAMglfhEVDEQRTAENQRELLALKC-HSVNQNITE----LSG 412
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    533 GQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDK-AREGRTTIVIAHRLSTVRNA-DVIAGFDGGVIVEQ-G 609
Cdd:PRK09700  413 GNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQlADDGKVILMVSSELPEIITVcDRIAVFCEGRLTQIlT 492

                  ....*....
gi 6755046    610 NHDELMREK 618
Cdd:PRK09700  493 NRDDMSEEE 501
GguA NF040905
sugar ABC transporter ATP-binding protein;
391-584 5.06e-04

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 44.40  E-value: 5.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    391 LEFKNVHFNYPSRSEVQILKGLNLKVKSGQTVALVGNSGCGKS-TTVQLMQRLYDP-LEGVVSIDGQDIRTINVR----- 463
Cdd:NF040905  258 FEVKNWTVYHPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTeLAMSVFGRSYGRnISGTVFKDGKEVDVSTVSdaida 337
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    464 ---YL---REIIGVVSQEPVLFATTIAENIRYGREDVtMDEIEKaVKEANAY--DFIMKLPHqfdtlVGERGAQLSGGQK 535
Cdd:NF040905  338 glaYVtedRKGYGLNLIDDIKRNITLANLGKVSRRGV-IDENEE-IKVAEEYrkKMNIKTPS-----VFQKVGNLSGGNQ 410
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 6755046    536 QRIAIARALVRNPKILLLDEATSALDT----ESEAVVQaalDKAREGRTTIVI 584
Cdd:NF040905  411 QKVVLSKWLFTDPDVLILDEPTRGIDVgakyEIYTIIN---ELAAEGKGVIVI 460
ABC_6TM_VMR1_D2_like cd18604
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ...
752-872 5.34e-04

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: 43.61  E-value: 5.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   752 LFSLFFLVMGLISFVTYFFQGFtfgKAGEILTKRVRYMVFKSMLRqdisWFDdhKNSTGSLTTRLASDASSVKGAMGARL 831
Cdd:cd18604   51 LISLLSVLLGTLRYLLFFFGSL---RASRKLHERLLHSVLRAPLR----WLD--TTPVGRILNRFSKDIETIDSELADSL 121
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 6755046   832 AVVTQNVANLGTGVILSLVYGWqltLLLVVIIPLIVLGGII 872
Cdd:cd18604  122 SSLLESTLSLLVILIAIVVVSP---AFLLPAVVLAALYVYI 159
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
530-585 5.69e-04

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 43.95  E-value: 5.69e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 6755046    530 LSGGQKQRIAIARALVRNPKILLLDEATSALDTESE-AVVQAALDKAREGRTTIVIA 585
Cdd:PRK10982  392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKfEIYQLIAELAKKDKGIIIIS 448
ABC_6TM_CvaB_RaxB_like cd18567
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ...
751-968 6.54e-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: 43.22  E-value: 6.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   751 NLFSLFFLVMGLISFVTYFFQGFTFGKAGEILTKRVRYMVFKSMLRQDISWFddHKNSTGSLTTRLASdASSVK-----G 825
Cdd:cd18567   42 TVLAIGFGLLLLLQALLSALRSWLVLYLSTSLNLQWTSNLFRHLLRLPLSYF--EKRHLGDIVSRFGS-LDEIQqtlttG 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   826 AMGARLAVVtqnVAnLGTGVILsLVYGWQLTLLLVVIIPLIVLggiieMKLLSGQALKD--KKQLEISGKIATEAIENFR 903
Cdd:cd18567  119 FVEALLDGL---MA-ILTLVMM-FLYSPKLALIVLAAVALYAL-----LRLALYPPLRRatEEQIVASAKEQSHFLETIR 188
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6755046   904 TIVSL-------TREQKFETMYAQSLqvpyrNAMKKAHVFGITFSFTQAM-MYFSYAACFRFGAYLVAQQLMT 968
Cdd:cd18567  189 GIQTIklfgreaEREARWLNLLVDAI-----NADIRLQRLQILFSAANGLlFGLENILVIYLGALLVLDGEFT 256
ABC_6TM_SUR1_D2_like cd18602
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ...
90-279 9.53e-04

Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group represents the six-transmembrane domain 2 (TMD2) of the sulphonylurea receptors SUR1/2 (ABCC8), which function as a modulator of ATP-sensitive potassium channels and insulin release, and belong to the ABCC subfamily. The ATP-sensitive (K-ATP) channel is an octameric complex of four pore-forming Kir6.2 subunits and four regulatory SUR subunits. Thus, in contrast to other ABC transporters, the SUR serves as the regulatory subunit of an ion channel. Mutations and deficiencies in the SUR proteins have been observed in patients with hyperinsulinemic hypoglycemia of infancy, an autosomal recessive disorder of unregulated and high insulin secretion. Mutations have also been associated with non-insulin-dependent diabetes mellitus type 2, an autosomal dominant disease of defective insulin secretion.


Pssm-ID: 350046 [Multi-domain]  Cd Length: 307  Bit Score: 42.98  E-value: 9.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    90 TNQSGPNSTLIISNSSLEEEMAIYAYY---YTGIGAGVLIVAYIQ---VSLWCLAAGRQIHkirQKFFHAIMNQEIGWFD 163
Cdd:cd18602   26 TEANHDVASVVFNITSSSLEDDEVSYYisvYAGLSLGAVILSLVTnlaGELAGLRAARRLH---DRMLRNIVRAPMRFFD 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   164 VHDVGELNTRLTDDVSKINDGIGDKIGMFFQSITTFLAGFII-GFISGWKLtlviLAVSPLIGLssalwAKVLTSF---T 239
Cdd:cd18602  103 TTPIGRILNRFSSDTNVIDQKLPTTLERLLRFLLLCLSAIIVnAIVTPYFL----IALIPIIIV-----YYFLQKFyraS 173
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 6755046   240 NKELQ---AYAKAGAVAE--EVLAAIRTVIAFGGQ----QKELERYNKN 279
Cdd:cd18602  174 SRELQrldNITKSPVFSHfsETLGGLTTIRAFRQQarftQQMLELIDRN 222
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
412-616 1.00e-03

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 43.12  E-value: 1.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    412 LNLKVKSGQTVALVGNSGCGKSTTVQLMQRLYDPLEGVVSIDGQDIRTINVR--------YL---REIIGVVSQEPVLFA 480
Cdd:PRK15439  282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAqrlarglvYLpedRQSSGLYLDAPLAWN 361
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    481 T-TIAEN-----IRYGREDVTMDEIEKAVKeanaydfiMKLPHqfdtlvGERGAQ-LSGGQKQRIAIARALVRNPKILLL 553
Cdd:PRK15439  362 VcALTHNrrgfwIKPARENAVLERYRRALN--------IKFNH------AEQAARtLSGGNQQKVLIAKCLEASPQLLIV 427
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    554 DEATSALDTESEA-VVQAALDKAREGRTTIVIAHRLSTVRN-ADVIAGFDGGVIV-----EQGNHDELMR 616
Cdd:PRK15439  428 DEPTRGVDVSARNdIYQLIRSIAAQNVAVLFISSDLEEIEQmADRVLVMHQGEISgaltgAAINVDTIMR 497
uvrA PRK00349
excinuclease ABC subunit UvrA;
488-621 1.02e-03

excinuclease ABC subunit UvrA;


Pssm-ID: 234734 [Multi-domain]  Cd Length: 943  Bit Score: 43.52  E-value: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    488 RYGRE---------------DVTMDEiekavkeanAYDF---IMKLPHQFDTLV---------GERGAQLSGGQKQRIAI 540
Cdd:PRK00349  771 RYNREtlevkykgkniadvlDMTVEE---------ALEFfeaIPKIARKLQTLVdvglgyiklGQPATTLSGGEAQRVKL 841
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    541 ARALVRNP--KIL-LLDEATSALDTESEA----VVQAALDKareGRTTIVIAHRLSTVRNADVI------AGFDGGVIVE 607
Cdd:PRK00349  842 AKELSKRStgKTLyILDEPTTGLHFEDIRklleVLHRLVDK---GNTVVVIEHNLDVIKTADWIidlgpeGGDGGGEIVA 918
                         170
                  ....*....|....
gi 6755046    608 QGNHDELMREKGIY 621
Cdd:PRK00349  919 TGTPEEVAKVEASY 932
UvrA COG0178
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
1172-1242 1.06e-03

Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];


Pssm-ID: 439948 [Multi-domain]  Cd Length: 941  Bit Score: 43.48  E-value: 1.06e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6755046  1172 TQLSGGQKQRIAIARALVR---QPHILLLDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIV 1242
Cdd:COG0178  825 TTLSGGEAQRVKLASELSKrstGKTLYILDEPTTGLHFHDIRKLLEVLHRLVDkGNTVVVIEHNLDVIKTADWII 899
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
402-597 1.15e-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: 41.82  E-value: 1.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   402 SRSEVQILKGLNLkvksgqtvaLVGNSGCGKSTTvqlmqrlydpLEGV-VSIDGQ-DIRTINVRYLREIIGVvsqepvlf 479
Cdd:cd03240   14 ERSEIEFFSPLTL---------IVGQNGAGKTTI----------IEALkYALTGElPPNSKGGAHDPKLIRE-------- 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   480 ATTIAEnIRYGREDVTMDEIeKAVKEANAYDFIMKLPH-QFDTLVGERGAQLSGGQKQ------RIAIARALVRNPKILL 552
Cdd:cd03240   67 GEVRAQ-VKLAFENANGKKY-TITRSLAILENVIFCHQgESNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILA 144
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 6755046   553 LDEATSALDTESEAVVQAALDKAREG---RTTIVIAHRLSTVRNADVI 597
Cdd:cd03240  145 LDEPTTNLDEENIEESLAEIIEERKSqknFQLIVITHDEELVDAADHI 192
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
1173-1242 1.36e-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: 1.36e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6755046  1173 QLSGGQKQRIAIARALVRQPH----ILLLDEATSALDTESEKVVQEALDKAR-EGRTCIVIAHRLSTIQNADLIV 1242
Cdd:cd03227   77 QLSGGEKELSALALILALASLkprpLYILDEIDRGLDPRDGQALAEAILEHLvKGAQVIVITHLPELAELADKLI 151
PRK15093 PRK15093
peptide ABC transporter ATP-binding protein SapD;
529-615 1.80e-03

peptide ABC transporter ATP-binding protein SapD;


Pssm-ID: 185049 [Multi-domain]  Cd Length: 330  Bit Score: 42.10  E-value: 1.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    529 QLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKARE--GRTTIVIAHRLSTVRN-ADVIAGFDGGVI 605
Cdd:PRK15093  158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnnNTTILLISHDLQMLSQwADKINVLYCGQT 237
                          90
                  ....*....|
gi 6755046    606 VEQGNHDELM 615
Cdd:PRK15093  238 VETAPSKELV 247
PRK01889 PRK01889
GTPase RsgA; Reviewed
1046-1081 2.01e-03

GTPase RsgA; Reviewed


Pssm-ID: 234988 [Multi-domain]  Cd Length: 356  Bit Score: 41.84  E-value: 2.01e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 6755046   1046 PNIPV-----LQGLSLEV-----KKGQTLALVGSSGCGKSTVV-QLL 1081
Cdd:PRK01889  170 PGVPVlavsaLDGEGLDVlaawlSGGKTVALLGSSGVGKSTLVnALL 216
ABC_6TM_PrtD_LapB_HlyB_like cd18782
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ...
707-969 3.61e-03

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: 41.04  E-value: 3.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   707 PYLLVGVLCAVINGCIQPVFAIVFSRIVGVFSRDDDHETkrqncnLFSLFFLVMGLISFVTYF--FQGFTFGKAGEILTK 784
Cdd:cd18782    2 RALIEVLALSFVVQLLGLANPLLFQVIIDKVLVQQDLAT------LYVIGVVMLVAALLEAVLtaLRTYLFTDTANRIDL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   785 RVRYMVFKSMLRQDISWFDdhKNSTGSLTTRLaSDASSVKG-AMGARLAVVTQNVANLGTGVILsLVYGWQLTLLLVVII 863
Cdd:cd18782   76 ELGGTIIDHLLRLPLGFFD--KRPVGELSTRI-SELDTIRGfLTGTALTTLLDVLFSVIYIAVL-FSYSPLLTLVVLATV 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   864 PLIVLggiieMKLLSGQALKD--KKQLEISGKIAT---EAIENFRTIVSLTRE----QKFETMYAQSLQVPYRNAMKKAH 934
Cdd:cd18782  152 PLQLL-----LTFLFGPILRRqiRRRAEASAKTQSylvESLTGIQTVKAQNAElkarWRWQNRYARSLGEGFKLTVLGTT 226
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 6755046   935 VFGITFSFTQammyFSYAACFRFGAYLVAQQLMTF 969
Cdd:cd18782  227 SGSLSQFLNK----LSSLLVLWVGAYLVLRGELTL 257
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
1167-1253 5.18e-03

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 41.35  E-value: 5.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1167 VGDKGTQLSGGQKQRIAIARALV---RQPHILLLDEATSALDTESEKVVQEALDK-AREGRTCIVIAHRLSTIQNADLIV 1242
Cdd:PRK00635 1693 LGQNLSSLSLSEKIAIKIAKFLYlppKHPTLFLLDEIATSLDNQQKSALLVQLRTlVSLGHSVIYIDHDPALLKQADYLI 1772
                          90
                  ....*....|.
gi 6755046   1243 VIENGKVKEHG 1253
Cdd:PRK00635 1773 EMGPGSGKTGG 1783
ABC_6TM_PrtD_LapB_HlyB_like cd18783
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ...
207-328 5.42e-03

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: 350056 [Multi-domain]  Cd Length: 294  Bit Score: 40.19  E-value: 5.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   207 FISGWKLTLVILAVSPLIGLSSALWAKVLTSFTNKELQAYAKAGAVAEEVLAAIRTVIAF---GGQQKE-LERYNKNLEE 282
Cdd:cd18783  137 FFYSPTLALVVLAFSALIALIILAFLPPFRRRLQALYRAEGERQAFLVETVHGIRTVKSLalePRQRREwDERVARAIRA 216
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 6755046   283 AKNVGIKKAITASISIGIAYLLVYASyalaFWYGTSLVLSNEYSIG 328
Cdd:cd18783  217 RFAVGRLSNWPQTLTGPLEKLMTVGV----IWVGAYLVFAGSLTVG 258
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
1149-1247 5.93e-03

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 40.97  E-value: 5.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   1149 EANIHQFI--------DSLPdkyntrVGDKGTQLSGGQKQRIAIARAL---VRQPHILLLDEATSALDTESEKVVQEALD 1217
Cdd:PRK00635  783 EPSIHEKIhalcslglDYLP------LGRPLSSLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDIKALIYVLQ 856
                          90       100       110
                  ....*....|....*....|....*....|.
gi 6755046   1218 K-AREGRTCIVIAHRLSTIQNADLivVIENG 1247
Cdd:PRK00635  857 SlTHQGHTVVIIEHNMHVVKVADY--VLELG 885
ABC_6TM_YOR1_D2_like cd18606
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ...
110-226 7.16e-03

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: 40.15  E-value: 7.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046   110 MAIYAYYytGIGAGVLIVAY-IQVSLWCLAAGRQIHkirQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINDGIGDK 188
Cdd:cd18606   38 IGIYAGL--GVLQAIFLFLFgLLLAYLGIRASKRLH---NKALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDS 112
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 6755046   189 IGMFFQSITTFLAGFIIGFISgwkLTLVILAVSPLIGL 226
Cdd:cd18606  113 LRMFLYTLSSIIGTFILIIIY---LPWFAIALPPLLVL 147
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
533-615 7.82e-03

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 40.26  E-value: 7.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6755046    533 GQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALdKAREGrTTIVIAH-R--LSTV--RNADViagfDGGVI-V 606
Cdd:PRK15064  159 GWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVL-NERNS-TMIIISHdRhfLNSVctHMADL----DYGELrV 232

                  ....*....
gi 6755046    607 EQGNHDELM 615
Cdd:PRK15064  233 YPGNYDEYM 241
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
1174-1242 8.14e-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: 39.55  E-value: 8.14e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6755046  1174 LSGGQKQRIAIARAL------VrqphILLLDEATSALDTESEKVVQEALDKARE-GRTCIVIAHRLSTIQNADLIV 1242
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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