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Conserved domains on  [gi|156095386|ref|XP_001613728|]
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multidrug resistance protein (mdr1) [Plasmodium vivax]

Protein Classification

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
1-1464 0e+00

multidrug resistance protein (mdr1); Provisional


:

Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 2894.34  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386    1 MKKDQRQPRDNSNSSNNLSIKDEVEKELNKKGTFELYKKIKTQKIPFFLPFKCLPSSHRKLLGVSFVCATISGGTLPFFV 80
Cdd:PTZ00265    1 MKKDQRQKKDNNSGGGNLSIKDEVEKELNKKGTFELYKKIKTQKIPFFLPFKCLPASHRKLLGVSFVCATISGGTLPFFV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   81 SVFGVIMKNMNLGENVNDIIFSLVLIGIFQFILSFISSFCMDVVTTKILKTLKIEFLKSVFYQDGQFHDNNPGSKLTSDL 160
Cdd:PTZ00265   81 SVFGVIMKNMNLGENVNDIIFSLVLIGIFQFILSFISSFCMDVVTTKILKTLKLEFLKSVFYQDGQFHDNNPGSKLTSDL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  161 DFYLEQVNAGIGTKFITIFTYASAFLGLYIWSLFKNARLTLCITCVFPLIYICGVICNKKVKINKKTSLLYNNNTMSIIE 240
Cdd:PTZ00265  161 DFYLEQVNAGIGTKFITIFTYASAFLGLYIWSLFKNARLTLCITCVFPLIYICGVICNKKVKINKKTSLLYNNNTMSIIE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  241 EALVGIRTVVSYCGENTILKKFNLSEKLYSKYTLKANLMESLHIGMINGFILASYAFGFWYGTRIIISDLSNQQPNNDFH 320
Cdd:PTZ00265  241 EALVGIRTVVSYCGEKTILKKFNLSEKLYSKYILKANFMESLHIGMINGFILASYAFGFWYGTRIIISDLSNQQPNNDFH 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  321 GGSVISILLGVLISMFMLTIILPNITEYMKSLEATNNLYEIINRKPLVENNQDGKKLKDIKKIQFKNVRFHYDTRKDVEI 400
Cdd:PTZ00265  321 GGSVISILLGVLISMFMLTIILPNITEYMKSLEATNSLYEIINRKPLVENNDDGKKLKDIKKIQFKNVRFHYDTRKDVEI 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  401 YKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDSHNLKDVNLKWWRSKIGVVSQDPLLFSNSIKNNI 480
Cdd:PTZ00265  401 YKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNI 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  481 KYSLYSLKDLEALSEESNEDGFSSQSDSNSRNSCRAKCAGDLNDMIQTTDSTELIQVRKNYETIEDSEVVSVSKKVLIHD 560
Cdd:PTZ00265  481 KYSLYSLKDLEALSNYYNEDGNDSQENKNKRNSCRAKCAGDLNDMSNTTDSNELIEMRKNYQTIKDSEVVDVSKKVLIHD 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  561 FVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRL 640
Cdd:PTZ00265  561 FVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRL 640
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  641 STIRYANTIFVLSNRENGSTVDVDVLGEDPTKDSNEKNEKHDKQEKGGKNSSANQKIGNAGSYIIEQGTHDALMKNKNGI 720
Cdd:PTZ00265  641 STIRYANTIFVLSNRERGSTVDVDIIGEDPTKDNKENNNKNNKDDNNNNNNNNNNKINNAGSYIIEQGTHDALMKNKNGI 720
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  721 YYTMINNQKVSSKSSSNNDNDKDSDMKSSIYKDSERGYDPDEANGNAK--NESASAKKSEKMSDAKASNTNAGGRLAFLR 798
Cdd:PTZ00265  721 YYTMINNQKVSSKKSSNNDNDKDSDMKSSAYKDSERGYDPDEMNGNSKheNESASNKKSCKMSDENASENNAGGKLPFLR 800
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  799 NLFKRKPKAPNNLRVVYREIFSYKKDIAIIALSIMVAGGLYPLFALLYAKYVGTLFDFANLEANSNKYSLYILVIAIAMF 878
Cdd:PTZ00265  801 NLFKRKPKAPNNLRIVYREIFSYKKDVTIIALSILVAGGLYPVFALLYAKYVSTLFDFANLEANSNKYSLYILVIAIAMF 880
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  879 ISETLKNYYNNVIGEKVEKTMKLRLFENIMYQEISFFDQDSHAPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVST 958
Cdd:PTZ00265  881 ISETLKNYYNNVIGEKVEKTMKRRLFENILYQEISFFDQDKHAPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSM 960
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  959 VMSFYFCPIVAAVLTGTYFIFMRVFAIRARIAANKDVEKKRVNQPGTAFVYNSDDEIFKDPSFLIQEAFYNMNTVIIYGL 1038
Cdd:PTZ00265  961 VMSFYFCPIVAAVLTGTYFIFMRVFAIRARLTANKDVEKKEINQPGTVFAYNSDDEIFKDPSFLIQEAFYNMNTVIIYGL 1040
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1039 EDYFCTLIEKAIDYSNKGQKRKTLINSMLWGFSQSAQFFINSFAYWFGSFLIRRGTIQVDDFMKSLFTFLFTGSYAGKLM 1118
Cdd:PTZ00265 1041 EDYFCNLIEKAIDYSNKGQKRKTLVNSMLWGFSQSAQLFINSFAYWFGSFLIRRGTILVDDFMKSLFTFLFTGSYAGKLM 1120
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1119 SLKGDSENAKLSFERYYPLITRKSLIDVRDNGGIKIKNSNDIKGKIEIMDVNFRYLSRPNVPIYKDLTFSCESKKTTAIV 1198
Cdd:PTZ00265 1121 SLKGDSENAKLSFEKYYPLIIRKSNIDVRDNGGIRIKNKNDIKGKIEIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIV 1200
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1199 GETGSGKSTVMSLLMRFYDLKNDHHIVFKNEQTGESSKEQMQQGDEEQNVGMKNANEFSSSKEGADGQSSTLFKNSGKIL 1278
Cdd:PTZ00265 1201 GETGSGKSTVMSLLMRFYDLKNDHHIVFKNEHTNDMTNEQDYQGDEEQNVGMKNVNEFSLTKEGGSGEDSTVFKNSGKIL 1280
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1279 LDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKENATREDVKRACKFAAIDEFIESLPNQYDTNVGPYGKSLS 1358
Cdd:PTZ00265 1281 LDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLS 1360
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1359 GGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKRSDKIVVFNNPDRTGSF 1438
Cdd:PTZ00265 1361 GGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKRSDKIVVFNNPDRTGSF 1440
                        1450      1460
                  ....*....|....*....|....*.
gi 156095386 1439 VQAQGTHEELLSVQDGVYKKYVKLAK 1464
Cdd:PTZ00265 1441 VQAHGTHEELLSVQDGVYKKYVKLAK 1466
 
Name Accession Description Interval E-value
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
1-1464 0e+00

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 2894.34  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386    1 MKKDQRQPRDNSNSSNNLSIKDEVEKELNKKGTFELYKKIKTQKIPFFLPFKCLPSSHRKLLGVSFVCATISGGTLPFFV 80
Cdd:PTZ00265    1 MKKDQRQKKDNNSGGGNLSIKDEVEKELNKKGTFELYKKIKTQKIPFFLPFKCLPASHRKLLGVSFVCATISGGTLPFFV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   81 SVFGVIMKNMNLGENVNDIIFSLVLIGIFQFILSFISSFCMDVVTTKILKTLKIEFLKSVFYQDGQFHDNNPGSKLTSDL 160
Cdd:PTZ00265   81 SVFGVIMKNMNLGENVNDIIFSLVLIGIFQFILSFISSFCMDVVTTKILKTLKLEFLKSVFYQDGQFHDNNPGSKLTSDL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  161 DFYLEQVNAGIGTKFITIFTYASAFLGLYIWSLFKNARLTLCITCVFPLIYICGVICNKKVKINKKTSLLYNNNTMSIIE 240
Cdd:PTZ00265  161 DFYLEQVNAGIGTKFITIFTYASAFLGLYIWSLFKNARLTLCITCVFPLIYICGVICNKKVKINKKTSLLYNNNTMSIIE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  241 EALVGIRTVVSYCGENTILKKFNLSEKLYSKYTLKANLMESLHIGMINGFILASYAFGFWYGTRIIISDLSNQQPNNDFH 320
Cdd:PTZ00265  241 EALVGIRTVVSYCGEKTILKKFNLSEKLYSKYILKANFMESLHIGMINGFILASYAFGFWYGTRIIISDLSNQQPNNDFH 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  321 GGSVISILLGVLISMFMLTIILPNITEYMKSLEATNNLYEIINRKPLVENNQDGKKLKDIKKIQFKNVRFHYDTRKDVEI 400
Cdd:PTZ00265  321 GGSVISILLGVLISMFMLTIILPNITEYMKSLEATNSLYEIINRKPLVENNDDGKKLKDIKKIQFKNVRFHYDTRKDVEI 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  401 YKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDSHNLKDVNLKWWRSKIGVVSQDPLLFSNSIKNNI 480
Cdd:PTZ00265  401 YKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNI 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  481 KYSLYSLKDLEALSEESNEDGFSSQSDSNSRNSCRAKCAGDLNDMIQTTDSTELIQVRKNYETIEDSEVVSVSKKVLIHD 560
Cdd:PTZ00265  481 KYSLYSLKDLEALSNYYNEDGNDSQENKNKRNSCRAKCAGDLNDMSNTTDSNELIEMRKNYQTIKDSEVVDVSKKVLIHD 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  561 FVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRL 640
Cdd:PTZ00265  561 FVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRL 640
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  641 STIRYANTIFVLSNRENGSTVDVDVLGEDPTKDSNEKNEKHDKQEKGGKNSSANQKIGNAGSYIIEQGTHDALMKNKNGI 720
Cdd:PTZ00265  641 STIRYANTIFVLSNRERGSTVDVDIIGEDPTKDNKENNNKNNKDDNNNNNNNNNNKINNAGSYIIEQGTHDALMKNKNGI 720
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  721 YYTMINNQKVSSKSSSNNDNDKDSDMKSSIYKDSERGYDPDEANGNAK--NESASAKKSEKMSDAKASNTNAGGRLAFLR 798
Cdd:PTZ00265  721 YYTMINNQKVSSKKSSNNDNDKDSDMKSSAYKDSERGYDPDEMNGNSKheNESASNKKSCKMSDENASENNAGGKLPFLR 800
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  799 NLFKRKPKAPNNLRVVYREIFSYKKDIAIIALSIMVAGGLYPLFALLYAKYVGTLFDFANLEANSNKYSLYILVIAIAMF 878
Cdd:PTZ00265  801 NLFKRKPKAPNNLRIVYREIFSYKKDVTIIALSILVAGGLYPVFALLYAKYVSTLFDFANLEANSNKYSLYILVIAIAMF 880
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  879 ISETLKNYYNNVIGEKVEKTMKLRLFENIMYQEISFFDQDSHAPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVST 958
Cdd:PTZ00265  881 ISETLKNYYNNVIGEKVEKTMKRRLFENILYQEISFFDQDKHAPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSM 960
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  959 VMSFYFCPIVAAVLTGTYFIFMRVFAIRARIAANKDVEKKRVNQPGTAFVYNSDDEIFKDPSFLIQEAFYNMNTVIIYGL 1038
Cdd:PTZ00265  961 VMSFYFCPIVAAVLTGTYFIFMRVFAIRARLTANKDVEKKEINQPGTVFAYNSDDEIFKDPSFLIQEAFYNMNTVIIYGL 1040
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1039 EDYFCTLIEKAIDYSNKGQKRKTLINSMLWGFSQSAQFFINSFAYWFGSFLIRRGTIQVDDFMKSLFTFLFTGSYAGKLM 1118
Cdd:PTZ00265 1041 EDYFCNLIEKAIDYSNKGQKRKTLVNSMLWGFSQSAQLFINSFAYWFGSFLIRRGTILVDDFMKSLFTFLFTGSYAGKLM 1120
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1119 SLKGDSENAKLSFERYYPLITRKSLIDVRDNGGIKIKNSNDIKGKIEIMDVNFRYLSRPNVPIYKDLTFSCESKKTTAIV 1198
Cdd:PTZ00265 1121 SLKGDSENAKLSFEKYYPLIIRKSNIDVRDNGGIRIKNKNDIKGKIEIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIV 1200
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1199 GETGSGKSTVMSLLMRFYDLKNDHHIVFKNEQTGESSKEQMQQGDEEQNVGMKNANEFSSSKEGADGQSSTLFKNSGKIL 1278
Cdd:PTZ00265 1201 GETGSGKSTVMSLLMRFYDLKNDHHIVFKNEHTNDMTNEQDYQGDEEQNVGMKNVNEFSLTKEGGSGEDSTVFKNSGKIL 1280
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1279 LDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKENATREDVKRACKFAAIDEFIESLPNQYDTNVGPYGKSLS 1358
Cdd:PTZ00265 1281 LDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLS 1360
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1359 GGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKRSDKIVVFNNPDRTGSF 1438
Cdd:PTZ00265 1361 GGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKRSDKIVVFNNPDRTGSF 1440
                        1450      1460
                  ....*....|....*....|....*.
gi 156095386 1439 VQAQGTHEELLSVQDGVYKKYVKLAK 1464
Cdd:PTZ00265 1441 VQAHGTHEELLSVQDGVYKKYVKLAK 1466
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
811-1462 4.93e-133

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 423.42  E-value: 4.93e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  811 LRVVYREIFSYKKDIAIIALSIMVAGGLYPLFALLYAKYVGTLFDFANLEAnSNKYSLYILVIAIAMFISETLKNYYNNV 890
Cdd:COG1132     9 LRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSA-LLLLLLLLLGLALLRALLSYLQRYLLAR 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  891 IGEKVEKTMKLRLFENIMYQEISFFDQdsHAPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSTVMSFYFCP---I 967
Cdd:COG1132    88 LAQRVVADLRRDLFEHLLRLPLSFFDR--RRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWrlaL 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  968 VAAVLTGTYFIFMRVFAIRARIAANKdvekkrvnqpgtafVYNSDDEIfkdpSFLIQEAFYNMNTVIIYGLEDYFCTLIE 1047
Cdd:COG1132   166 IVLLVLPLLLLVLRLFGRRLRKLFRR--------------VQEALAEL----NGRLQESLSGIRVVKAFGREERELERFR 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1048 KAIDYSNKGQKRKTLINSMLWGFSQSAQFFINSFAYWFGSFLIRRGTIQVDDFMksLFTFLFTGSYA--GKLMSLKGDSE 1125
Cdd:COG1132   228 EANEELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLV--AFILYLLRLFGplRQLANVLNQLQ 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1126 NAKLSFERYYPLITRKSLIDVRDNGgikiKNSNDIKGKIEIMDVNFRYlsRPNVPIYKDLTFSCESKKTTAIVGETGSGK 1205
Cdd:COG1132   306 RALASAERIFELLDEPPEIPDPPGA----VPLPPVRGEIEFENVSFSY--PGDRPVLKDISLTIPPGETVALVGPSGSGK 379
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1206 STVMSLLMRFYDLkndhhivfkneqtgesskeqmqqgdeeqnvgmknanefssskegadgqsstlfkNSGKILLDGVDIC 1285
Cdd:COG1132   380 STLVNLLLRFYDP------------------------------------------------------TSGRILIDGVDIR 405
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1286 DYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKENATREDVKRACKFAAIDEFIESLPNQYDTNVGPYGKSLSGGQKQRI 1365
Cdd:COG1132   406 DLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRI 485
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1366 AIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIkdKADKTIITIAHRIASIKRSDKIVVFNNpdrtGSfVQAQGTH 1445
Cdd:COG1132   486 AIARALLKDPPILILDEATSALDTETEALIQEALERL--MKGRTTIVIAHRLSTIRNADRILVLDD----GR-IVEQGTH 558
                         650
                  ....*....|....*..
gi 156095386 1446 EELLSvQDGVYKKYVKL 1462
Cdd:COG1132   559 EELLA-RGGLYARLYRL 574
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
1164-1463 6.06e-112

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: 352.61  E-value: 6.06e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYLSRPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfkneqtgesskeqmqqgd 1243
Cdd:cd03249     1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDP------------------------- 55
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 eeqnvgmknanefssskegadgqsstlfkNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKENATR 1323
Cdd:cd03249    56 -----------------------------TSGEILLDGVDIRDLNLRWLRSQIGLVSQEPVLFDGTIAENIRYGKPDATD 106
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1324 EDVKRACKFAAIDEFIESLPNQYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIk 1403
Cdd:cd03249   107 EEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRA- 185
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1404 dKADKTIITIAHRIASIKRSDKIVVFNNpdrtgSFVQAQGTHEELLSvQDGVYKKYVKLA 1463
Cdd:cd03249   186 -MKGRTTIVIAHRLSTIRNADLIAVLQN-----GQVVEQGTHDELMA-QKGVYAKLVKAQ 238
MsbA_rel TIGR02204
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ...
826-1462 5.61e-83

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: 284.29  E-value: 5.61e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   826 AIIALSIMVAGGLyplfALLYAkyVGTLFDFANLEANS---NKYSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMKLR 902
Cdd:TIGR02204   23 ALVALLITAAATL----SLPYA--VRLMIDHGFSKDSSgllNRYFAFLLVVALVLALGTAARFYLVTWLGERVVADIRRA 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   903 LFENIMYQEISFFDQDShaPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSTVMSFYFCPIVAA-VLTGTYFIF-- 979
Cdd:TIGR02204   97 VFAHLISLSPSFFDKNR--SGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTSlVLLAVPLVLlp 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   980 MRVFAIRARIAAnkdvekkRVNQpgtafvynsddEIFKDPSFLIQEAFYNMNTVIIYGLEDY----FCTLIEKAIDYSNK 1055
Cdd:TIGR02204  175 ILLFGRRVRKLS-------RESQ-----------DRIADAGSYAGETLGAIRTVQAFGHEDAersrFGGAVEKAYEAARQ 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1056 GQKRKTLINSMLWGFSQSAQFFInsfaYWFGSFLIRRGTIQVDDFMKSLFTFLFTGSYAGKLMSLKGDSENAKLSFERYY 1135
Cdd:TIGR02204  237 RIRTRALLTAIVIVLVFGAIVGV----LWVGAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGAAERLI 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1136 PLITRKSLIDVRDNggiKIKNSNDIKGKIEIMDVNFRYLSRPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRF 1215
Cdd:TIGR02204  313 ELLQAEPDIKAPAH---PKTLPVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRF 389
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1216 YDlkndhhivfkneqtgesskeqmqqgdeeqnvgmknanefssskegadgqsstlfKNSGKILLDGVDICDYNLKDLRNL 1295
Cdd:TIGR02204  390 YD------------------------------------------------------PQSGRILLDGVDLRQLDPAELRAR 415
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1296 FSIVSQEPMLFNMSIYENIKFGKENATREDVKRACKFAAIDEFIESLPNQYDTNVGPYGKSLSGGQKQRIAIARALLREP 1375
Cdd:TIGR02204  416 MALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDA 495
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1376 KILLLDEATSSLDSNSEKLIEKTIVDIkdKADKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVqAQGTHEELLSvQDGV 1455
Cdd:TIGR02204  496 PILLLDEATSALDAESEQLVQQALETL--MKGRTTLIIAHRLATVLKADRIVVMDQ----GRIV-AQGTHAELIA-KGGL 567

                   ....*..
gi 156095386  1456 YKKYVKL 1462
Cdd:TIGR02204  568 YARLARL 574
ABC_membrane pfam00664
ABC transporter transmembrane region; This family represents a unit of six transmembrane ...
62-309 1.45e-48

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: 174.75  E-value: 1.45e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386    62 LGVSFVCATISGGTLPFFVSVFGVIMKNM---NLGENVNDIIFSLVLI--GIFQFILSFISSFCMDVVTTKILKTLKIEF 136
Cdd:pfam00664    1 LILAILLAILSGAISPAFPLVLGRILDVLlpdGDPETQALNVYSLALLllGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   137 LKSVFYQDGQFHDNNPGSKLTSDLDFYLEQVNAGIGTKFITIFTYASAFLGLYIWSLFKNARLTLCITCVFPLIYICGVI 216
Cdd:pfam00664   81 FKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAV 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   217 CNKKVKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGENTILKKFNLSEKLYSKYTLKANLMESLHIGMINGFILASYA 296
Cdd:pfam00664  161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYA 240
                          250
                   ....*....|...
gi 156095386   297 FGFWYGTRIIISD 309
Cdd:pfam00664  241 LALWFGAYLVISG 253
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
1356-1429 1.71e-10

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 61.87  E-value: 1.71e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156095386 1356 SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkADKTIITIAHRIASIKRSDKIVVF 1429
Cdd:NF040873  119 ELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHA-RGATVVVVTHDLELVRRADPCVLL 191
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
1330-1433 5.17e-09

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: 56.61  E-value: 5.17e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   1330 CKFAAIDEFIESLPNQY-DTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVD-----IK 1403
Cdd:smart00382   33 VIYIDGEDILEEVLDQLlLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELrllllLK 112
                            90       100       110
                    ....*....|....*....|....*....|....*.
gi 156095386   1404 DKADKTIITIAHRIASIK------RSDKIVVFNNPD 1433
Cdd:smart00382  113 SEKNLTVILTTNDEKDLGpallrrRFDRRIVLLLIL 148
GguA NF040905
sugar ABC transporter ATP-binding protein;
403-673 1.02e-07

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 56.34  E-value: 1.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  403 DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYdPT---EGDVI----------INDSHnlkdvnlkwwRSKIGVVSQD- 468
Cdd:NF040905   19 DVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILfdgevcrfkdIRDSE----------ALGIVIIHQEl 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  469 ---PLLfsnSIKNNIkyslyslkdleALSEESNEDGFSSQSDSNSRnscrakcagdlndmiqttdSTELIqvrknyetie 545
Cdd:NF040905   88 aliPYL---SIAENI-----------FLGNERAKRGVIDWNETNRR-------------------ARELL---------- 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  546 dsevvsvsKKVlihdfvsALPDKYETLVgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSL-DNKSEYLVQkTINN 624
Cdd:NF040905  125 --------AKV-------GLDESPDTLV----TDIGVGKQQLVEIAKALSKDVKLLILDEPTAALnEEDSAALLD-LLLE 184
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 156095386  625 LKgnENRIT-IIIAHRLSTIRY-ANTIFVLsnrENGSTVD-VDVLGEDPTKD 673
Cdd:NF040905  185 LK--AQGITsIIISHKLNEIRRvADSITVL---RDGRTIEtLDCRADEVTED 231
GguA NF040905
sugar ABC transporter ATP-binding protein;
1177-1428 5.96e-07

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 54.03  E-value: 5.96e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1177 PNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYdlkndhhivfkneqtgesskeqmQQGDEEqnvgmknanef 1256
Cdd:NF040905   12 PGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-----------------------PHGSYE----------- 57
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1257 ssskegadgqsstlfknsGKILLDGvDICDYnlKDLRNlfS------IVSQE----PMLfnmSIYENIKFGKENATR--- 1323
Cdd:NF040905   58 ------------------GEILFDG-EVCRF--KDIRD--SealgivIIHQElaliPYL---SIAENIFLGNERAKRgvi 111
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1324 ---EDVKRACKFAAIDEFIESlPnqyDTNVgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSL-DSNSEKLIEkTI 1399
Cdd:NF040905  112 dwnETNRRARELLAKVGLDES-P---DTLV----TDIGVGKQQLVEIAKALSKDVKLLILDEPTAALnEEDSAALLD-LL 182
                         250       260       270
                  ....*....|....*....|....*....|
gi 156095386 1400 VDIKDKADKTIItIAHRIASIKR-SDKIVV 1428
Cdd:NF040905  183 LELKAQGITSII-ISHKLNEIRRvADSITV 211
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
580-652 6.85e-07

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 51.47  E-value: 6.85e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 156095386  580 LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGnENRITIIIAHRLSTIRYANTIFVL 652
Cdd:NF040873  120 LSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHA-RGATVVVVTHDLELVRRADPCVLL 191
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
403-611 6.58e-05

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 47.81  E-value: 6.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  403 DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVII----NDSHNLKDvnlkwwRSKIGVVSQdpllfsnsikn 478
Cdd:NF033858  284 HVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLfgqpVDAGDIAT------RRRVGYMSQ----------- 346
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  479 niKYSLYS-------LkDLEA----LSEEsnedgfssqsDSNSRnscrakcagdLNDMIQTTDsteliqvrknyetieds 547
Cdd:NF033858  347 --AFSLYGeltvrqnL-ELHArlfhLPAA----------EIAAR----------VAEMLERFD----------------- 386
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156095386  548 evvsvskkvlIHDFVSALPDKyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:NF033858  387 ----------LADVADALPDS-----------LPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
577-611 5.16e-04

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 44.73  E-value: 5.16e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 156095386  577 ASKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:NF033858  134 AGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVD 168
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
1293-1388 6.65e-03

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 40.88  E-value: 6.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1293 RNLFsivsqePMLfnmSIYENIKF-----GKENATREdvkrackfAAIDEFIESlpnqydTNVGPY-----GKsLSGGQK 1362
Cdd:NF033858   87 KNLY------PTL---SVFENLDFfgrlfGQDAAERR--------RRIDELLRA------TGLAPFadrpaGK-LSGGMK 142
                          90       100
                  ....*....|....*....|....*.
gi 156095386 1363 QRIAIARALLREPKILLLDEATSSLD 1388
Cdd:NF033858  143 QKLGLCCALIHDPDLLILDEPTTGVD 168
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
574-614 7.51e-03

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 40.49  E-value: 7.51e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 156095386  574 GSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS 614
Cdd:NF000106  139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRT 179
 
Name Accession Description Interval E-value
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
1-1464 0e+00

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 2894.34  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386    1 MKKDQRQPRDNSNSSNNLSIKDEVEKELNKKGTFELYKKIKTQKIPFFLPFKCLPSSHRKLLGVSFVCATISGGTLPFFV 80
Cdd:PTZ00265    1 MKKDQRQKKDNNSGGGNLSIKDEVEKELNKKGTFELYKKIKTQKIPFFLPFKCLPASHRKLLGVSFVCATISGGTLPFFV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   81 SVFGVIMKNMNLGENVNDIIFSLVLIGIFQFILSFISSFCMDVVTTKILKTLKIEFLKSVFYQDGQFHDNNPGSKLTSDL 160
Cdd:PTZ00265   81 SVFGVIMKNMNLGENVNDIIFSLVLIGIFQFILSFISSFCMDVVTTKILKTLKLEFLKSVFYQDGQFHDNNPGSKLTSDL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  161 DFYLEQVNAGIGTKFITIFTYASAFLGLYIWSLFKNARLTLCITCVFPLIYICGVICNKKVKINKKTSLLYNNNTMSIIE 240
Cdd:PTZ00265  161 DFYLEQVNAGIGTKFITIFTYASAFLGLYIWSLFKNARLTLCITCVFPLIYICGVICNKKVKINKKTSLLYNNNTMSIIE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  241 EALVGIRTVVSYCGENTILKKFNLSEKLYSKYTLKANLMESLHIGMINGFILASYAFGFWYGTRIIISDLSNQQPNNDFH 320
Cdd:PTZ00265  241 EALVGIRTVVSYCGEKTILKKFNLSEKLYSKYILKANFMESLHIGMINGFILASYAFGFWYGTRIIISDLSNQQPNNDFH 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  321 GGSVISILLGVLISMFMLTIILPNITEYMKSLEATNNLYEIINRKPLVENNQDGKKLKDIKKIQFKNVRFHYDTRKDVEI 400
Cdd:PTZ00265  321 GGSVISILLGVLISMFMLTIILPNITEYMKSLEATNSLYEIINRKPLVENNDDGKKLKDIKKIQFKNVRFHYDTRKDVEI 400
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  401 YKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDSHNLKDVNLKWWRSKIGVVSQDPLLFSNSIKNNI 480
Cdd:PTZ00265  401 YKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNI 480
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  481 KYSLYSLKDLEALSEESNEDGFSSQSDSNSRNSCRAKCAGDLNDMIQTTDSTELIQVRKNYETIEDSEVVSVSKKVLIHD 560
Cdd:PTZ00265  481 KYSLYSLKDLEALSNYYNEDGNDSQENKNKRNSCRAKCAGDLNDMSNTTDSNELIEMRKNYQTIKDSEVVDVSKKVLIHD 560
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  561 FVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRL 640
Cdd:PTZ00265  561 FVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRL 640
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  641 STIRYANTIFVLSNRENGSTVDVDVLGEDPTKDSNEKNEKHDKQEKGGKNSSANQKIGNAGSYIIEQGTHDALMKNKNGI 720
Cdd:PTZ00265  641 STIRYANTIFVLSNRERGSTVDVDIIGEDPTKDNKENNNKNNKDDNNNNNNNNNNKINNAGSYIIEQGTHDALMKNKNGI 720
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  721 YYTMINNQKVSSKSSSNNDNDKDSDMKSSIYKDSERGYDPDEANGNAK--NESASAKKSEKMSDAKASNTNAGGRLAFLR 798
Cdd:PTZ00265  721 YYTMINNQKVSSKKSSNNDNDKDSDMKSSAYKDSERGYDPDEMNGNSKheNESASNKKSCKMSDENASENNAGGKLPFLR 800
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  799 NLFKRKPKAPNNLRVVYREIFSYKKDIAIIALSIMVAGGLYPLFALLYAKYVGTLFDFANLEANSNKYSLYILVIAIAMF 878
Cdd:PTZ00265  801 NLFKRKPKAPNNLRIVYREIFSYKKDVTIIALSILVAGGLYPVFALLYAKYVSTLFDFANLEANSNKYSLYILVIAIAMF 880
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  879 ISETLKNYYNNVIGEKVEKTMKLRLFENIMYQEISFFDQDSHAPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVST 958
Cdd:PTZ00265  881 ISETLKNYYNNVIGEKVEKTMKRRLFENILYQEISFFDQDKHAPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSM 960
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  959 VMSFYFCPIVAAVLTGTYFIFMRVFAIRARIAANKDVEKKRVNQPGTAFVYNSDDEIFKDPSFLIQEAFYNMNTVIIYGL 1038
Cdd:PTZ00265  961 VMSFYFCPIVAAVLTGTYFIFMRVFAIRARLTANKDVEKKEINQPGTVFAYNSDDEIFKDPSFLIQEAFYNMNTVIIYGL 1040
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1039 EDYFCTLIEKAIDYSNKGQKRKTLINSMLWGFSQSAQFFINSFAYWFGSFLIRRGTIQVDDFMKSLFTFLFTGSYAGKLM 1118
Cdd:PTZ00265 1041 EDYFCNLIEKAIDYSNKGQKRKTLVNSMLWGFSQSAQLFINSFAYWFGSFLIRRGTILVDDFMKSLFTFLFTGSYAGKLM 1120
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1119 SLKGDSENAKLSFERYYPLITRKSLIDVRDNGGIKIKNSNDIKGKIEIMDVNFRYLSRPNVPIYKDLTFSCESKKTTAIV 1198
Cdd:PTZ00265 1121 SLKGDSENAKLSFEKYYPLIIRKSNIDVRDNGGIRIKNKNDIKGKIEIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIV 1200
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1199 GETGSGKSTVMSLLMRFYDLKNDHHIVFKNEQTGESSKEQMQQGDEEQNVGMKNANEFSSSKEGADGQSSTLFKNSGKIL 1278
Cdd:PTZ00265 1201 GETGSGKSTVMSLLMRFYDLKNDHHIVFKNEHTNDMTNEQDYQGDEEQNVGMKNVNEFSLTKEGGSGEDSTVFKNSGKIL 1280
                        1290      1300      1310      1320      1330      1340      1350      1360
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1279 LDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKENATREDVKRACKFAAIDEFIESLPNQYDTNVGPYGKSLS 1358
Cdd:PTZ00265 1281 LDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLS 1360
                        1370      1380      1390      1400      1410      1420      1430      1440
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1359 GGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKRSDKIVVFNNPDRTGSF 1438
Cdd:PTZ00265 1361 GGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKRSDKIVVFNNPDRTGSF 1440
                        1450      1460
                  ....*....|....*....|....*.
gi 156095386 1439 VQAQGTHEELLSVQDGVYKKYVKLAK 1464
Cdd:PTZ00265 1441 VQAHGTHEELLSVQDGVYKKYVKLAK 1466
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
811-1462 4.93e-133

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 423.42  E-value: 4.93e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  811 LRVVYREIFSYKKDIAIIALSIMVAGGLYPLFALLYAKYVGTLFDFANLEAnSNKYSLYILVIAIAMFISETLKNYYNNV 890
Cdd:COG1132     9 LRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSA-LLLLLLLLLGLALLRALLSYLQRYLLAR 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  891 IGEKVEKTMKLRLFENIMYQEISFFDQdsHAPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSTVMSFYFCP---I 967
Cdd:COG1132    88 LAQRVVADLRRDLFEHLLRLPLSFFDR--RRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWrlaL 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  968 VAAVLTGTYFIFMRVFAIRARIAANKdvekkrvnqpgtafVYNSDDEIfkdpSFLIQEAFYNMNTVIIYGLEDYFCTLIE 1047
Cdd:COG1132   166 IVLLVLPLLLLVLRLFGRRLRKLFRR--------------VQEALAEL----NGRLQESLSGIRVVKAFGREERELERFR 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1048 KAIDYSNKGQKRKTLINSMLWGFSQSAQFFINSFAYWFGSFLIRRGTIQVDDFMksLFTFLFTGSYA--GKLMSLKGDSE 1125
Cdd:COG1132   228 EANEELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLV--AFILYLLRLFGplRQLANVLNQLQ 305
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1126 NAKLSFERYYPLITRKSLIDVRDNGgikiKNSNDIKGKIEIMDVNFRYlsRPNVPIYKDLTFSCESKKTTAIVGETGSGK 1205
Cdd:COG1132   306 RALASAERIFELLDEPPEIPDPPGA----VPLPPVRGEIEFENVSFSY--PGDRPVLKDISLTIPPGETVALVGPSGSGK 379
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1206 STVMSLLMRFYDLkndhhivfkneqtgesskeqmqqgdeeqnvgmknanefssskegadgqsstlfkNSGKILLDGVDIC 1285
Cdd:COG1132   380 STLVNLLLRFYDP------------------------------------------------------TSGRILIDGVDIR 405
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1286 DYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKENATREDVKRACKFAAIDEFIESLPNQYDTNVGPYGKSLSGGQKQRI 1365
Cdd:COG1132   406 DLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRI 485
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1366 AIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIkdKADKTIITIAHRIASIKRSDKIVVFNNpdrtGSfVQAQGTH 1445
Cdd:COG1132   486 AIARALLKDPPILILDEATSALDTETEALIQEALERL--MKGRTTIVIAHRLSTIRNADRILVLDD----GR-IVEQGTH 558
                         650
                  ....*....|....*..
gi 156095386 1446 EELLSvQDGVYKKYVKL 1462
Cdd:COG1132   559 EELLA-RGGLYARLYRL 574
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
58-728 1.01e-125

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 403.39  E-value: 1.01e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   58 HRKLLGVSFVCATISGGTLPFFVSVFGVIMKNMNLGENVNDIIFS---LVLIGIFQFILSFISSFCMDVVTTKILKTLKI 134
Cdd:COG1132    19 YRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLlllLLGLALLRALLSYLQRYLLARLAQRVVADLRR 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  135 EFLKSVFYQDGQFHDNNP-G---SKLTSDLDfyleQVNAGIGTKFITIFTYASAFLGLYIWSLFKNARLTLCITCVFPLI 210
Cdd:COG1132    99 DLFEHLLRLPLSFFDRRRtGdllSRLTNDVD----AVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLALIVLLVLPLL 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  211 YICGVICNKKVKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGENTILKKFN-LSEKLYsKYTLKANLMESLHIGMING 289
Cdd:COG1132   175 LLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFReANEELR-RANLRAARLSALFFPLMEL 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  290 FILASYAFGFWYGTRIIIS-DLSnqqpnndfhGGSVISILLGVLISMFMLTIILPNITEYMKSLEATNNLYEIINRKPLV 368
Cdd:COG1132   254 LGNLGLALVLLVGGLLVLSgSLT---------VGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEI 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  369 ENNQDGKKLKDIK-KIQFKNVRFHYDTRKDVeiYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDs 447
Cdd:COG1132   325 PDPPGAVPLPPVRgEIEFENVSFSYPGDRPV--LKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDG- 401
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  448 HNLKDVNLKWWRSKIGVVSQDPLLFSNSIKNNIKYslyslkdlealseesnedgfssqsdsnsrnscrakcaGDLNdmiq 527
Cdd:COG1132   402 VDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRY-------------------------------------GRPD---- 440
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  528 ttdsteliqvrknyetIEDSEVVSVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEAT 607
Cdd:COG1132   441 ----------------ATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEAT 504
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  608 SSLDNKSEYLVQKTINNLKgnENRITIIIAHRLSTIRYANTIFVLsnrengstvdvdvlgedptkdsneknekhdkqeKG 687
Cdd:COG1132   505 SALDTETEALIQEALERLM--KGRTTIVIAHRLSTIRNADRILVL---------------------------------DD 549
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|.
gi 156095386  688 GKnssanqkignagsyIIEQGTHDALMKnKNGIYYTMINNQ 728
Cdd:COG1132   550 GR--------------IVEQGTHEELLA-RGGLYARLYRLQ 575
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
1164-1463 6.06e-112

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: 352.61  E-value: 6.06e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYLSRPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfkneqtgesskeqmqqgd 1243
Cdd:cd03249     1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDP------------------------- 55
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 eeqnvgmknanefssskegadgqsstlfkNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKENATR 1323
Cdd:cd03249    56 -----------------------------TSGEILLDGVDIRDLNLRWLRSQIGLVSQEPVLFDGTIAENIRYGKPDATD 106
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1324 EDVKRACKFAAIDEFIESLPNQYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIk 1403
Cdd:cd03249   107 EEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRA- 185
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1404 dKADKTIITIAHRIASIKRSDKIVVFNNpdrtgSFVQAQGTHEELLSvQDGVYKKYVKLA 1463
Cdd:cd03249   186 -MKGRTTIVIAHRLSTIRNADLIAVLQN-----GQVVEQGTHDELMA-QKGVYAKLVKAQ 238
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
383-728 1.55e-108

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: 343.37  E-value: 1.55e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDsHNLKDVNLKWWRSKI 462
Cdd:cd03249     1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDG-VDIRDLNLRWLRSQI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  463 GVVSQDPLLFSNSIKNNIKYSlyslkdlealseesnedgfssqsdsnsrnscrakcagdlndmiqttdsteliqvrKNYE 542
Cdd:cd03249    80 GLVSQEPVLFDGTIAENIRYG-------------------------------------------------------KPDA 104
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  543 TieDSEVVSVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI 622
Cdd:cd03249   105 T--DEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEAL 182
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  623 NNLKgnENRITIIIAHRLSTIRYANTIFVLSNrengstvdvdvlgedptkdsneknekhdkqekggknssanqkignagS 702
Cdd:cd03249   183 DRAM--KGRTTIVIAHRLSTIRNADLIAVLQN-----------------------------------------------G 213
                         330       340
                  ....*....|....*....|....*.
gi 156095386  703 YIIEQGTHDALMKNKnGIYYTMINNQ 728
Cdd:cd03249   214 QVVEQGTHDELMAQK-GVYAKLVKAQ 238
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
801-1461 1.63e-106

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: 355.30  E-value: 1.63e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  801 FKRKPKAPNNLRVVYREIFSYKKDIAIIALSIMVAGglypLFALLYAKYVGTLFDFAnlEANSNKYSLYILVIAIAM--- 877
Cdd:COG2274   134 FDKRGEKPFGLRWFLRLLRRYRRLLLQVLLASLLIN----LLALATPLFTQVVIDRV--LPNQDLSTLWVLAIGLLLall 207
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  878 --FISETLKNYYNNVIGEKVEKTMKLRLFENIMYQEISFFDQDShaPGLLSAHInRDVH----LLKTGLVNNIVIFThFI 951
Cdd:COG2274   208 feGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRS--VGDLASRF-RDVEsireFLTGSLLTALLDLL-FV 283
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  952 VLFLVstVMSFY-----FCPIVAAVLtgtYFIFMRVFAIRARIAANKDVEKKRVNQpgtafvynsddeifkdpSFLIqEA 1026
Cdd:COG2274   284 LIFLI--VLFFYspplaLVVLLLIPL---YVLLGLLFQPRLRRLSREESEASAKRQ-----------------SLLV-ET 340
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1027 FYNMNTVIIYGLEDYFCTLIEKAI-DYSNKGQKRKTLINSMLWgFSQSAQFFINSFAYWFGSFLIRRGTIQVDDFMK-SL 1104
Cdd:COG2274   341 LRGIETIKALGAESRFRRRWENLLaKYLNARFKLRRLSNLLST-LSGLLQQLATVALLWLGAYLVIDGQLTLGQLIAfNI 419
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1105 FTFLFTGSyAGKLMSLKGDSENAKLSFERYYPLITRKslidVRDNGGIKIKNSNDIKGKIEIMDVNFRYlSRPNVPIYKD 1184
Cdd:COG2274   420 LSGRFLAP-VAQLIGLLQRFQDAKIALERLDDILDLP----PEREEGRSKLSLPRLKGDIELENVSFRY-PGDSPPVLDN 493
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1185 LTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfkneqtgesskeqmqqgdeeqnvgmknanefssskegad 1264
Cdd:COG2274   494 ISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEP---------------------------------------------- 527
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1265 gqsstlfkNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKENATREDVKRACKFAAIDEFIESLPN 1344
Cdd:COG2274   528 --------TSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPM 599
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1345 QYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIkdKADKTIITIAHRIASIKRSD 1424
Cdd:COG2274   600 GYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRL--LKGRTVIIIAHRLSTIRLAD 677
                         650       660       670
                  ....*....|....*....|....*....|....*..
gi 156095386 1425 KIVVFNNpdrtGSFVQaQGTHEELLSvQDGVYKKYVK 1461
Cdd:COG2274   678 RIIVLDK----GRIVE-DGTHEELLA-RKGLYAELVQ 708
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
58-728 2.85e-92

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: 315.23  E-value: 2.85e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   58 HRKLLGVSFVCATISGG---TLPFFVSVF---GVIMKNMNLgenVNDIIFSLVLIGIFQFILSFISSFCMDVVTTKILKT 131
Cdd:COG2274   154 YRRLLLQVLLASLLINLlalATPLFTQVVidrVLPNQDLST---LWVLAIGLLLALLFEGLLRLLRSYLLLRLGQRIDLR 230
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  132 LKIEFLKSVFYQDGQFHDNNPGSKLTSDLdFYLEQVNAGIGTKFITIFTyASAFLGLYIWSLFK-NARLTLCITCVFPLI 210
Cdd:COG2274   231 LSSRFFRHLLRLPLSFFESRSVGDLASRF-RDVESIREFLTGSLLTALL-DLLFVLIFLIVLFFySPPLALVVLLLIPLY 308
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  211 YICGVICNKKVKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGENTILKKFnlsEKLYSKYtLKANlMESLHIGMINGF 290
Cdd:COG2274   309 VLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRW---ENLLAKY-LNAR-FKLRRLSNLLST 383
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  291 I-----LASYAFGFWYGTRIIIsdlsnqqpNNDFHGGSVI--SILLGVLISmFMLTIILpNITEYMKSLEATNNLYEIIN 363
Cdd:COG2274   384 LsgllqQLATVALLWLGAYLVI--------DGQLTLGQLIafNILSGRFLA-PVAQLIG-LLQRFQDAKIALERLDDILD 453
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  364 RKPLVENNQDGKKLKDIK-KIQFKNVRFHYDTRkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDV 442
Cdd:COG2274   454 LPPEREEGRSKLSLPRLKgDIELENVSFRYPGD-SPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRI 532
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  443 IINDsHNLKDVNLKWWRSKIGVVSQDPLLFSNSIKNNIkyslyslkdlealseesnedgfssqsdsnsrnscrakCAGDl 522
Cdd:COG2274   533 LIDG-IDLRQIDPASLRRQIGVVLQDVFLFSGTIRENI-------------------------------------TLGD- 573
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  523 ndmiqttdsteliqvrknyETIEDSEVVSVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILI 602
Cdd:COG2274   574 -------------------PDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILI 634
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  603 LDEATSSLDNKSEYLVQKTINNLKGneNRITIIIAHRLSTIRYANTIFVLSNrengstvdvdvlgedptkdsneknekhd 682
Cdd:COG2274   635 LDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIRLADRIIVLDK---------------------------- 684
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|....*.
gi 156095386  683 kqekgGKnssanqkignagsyIIEQGTHDALMKnKNGIYYTMINNQ 728
Cdd:COG2274   685 -----GR--------------IVEDGTHEELLA-RKGLYAELVQQQ 710
MsbA_rel TIGR02204
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ...
826-1462 5.61e-83

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: 284.29  E-value: 5.61e-83
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   826 AIIALSIMVAGGLyplfALLYAkyVGTLFDFANLEANS---NKYSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMKLR 902
Cdd:TIGR02204   23 ALVALLITAAATL----SLPYA--VRLMIDHGFSKDSSgllNRYFAFLLVVALVLALGTAARFYLVTWLGERVVADIRRA 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   903 LFENIMYQEISFFDQDShaPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSTVMSFYFCPIVAA-VLTGTYFIF-- 979
Cdd:TIGR02204   97 VFAHLISLSPSFFDKNR--SGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTSlVLLAVPLVLlp 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   980 MRVFAIRARIAAnkdvekkRVNQpgtafvynsddEIFKDPSFLIQEAFYNMNTVIIYGLEDY----FCTLIEKAIDYSNK 1055
Cdd:TIGR02204  175 ILLFGRRVRKLS-------RESQ-----------DRIADAGSYAGETLGAIRTVQAFGHEDAersrFGGAVEKAYEAARQ 236
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1056 GQKRKTLINSMLWGFSQSAQFFInsfaYWFGSFLIRRGTIQVDDFMKSLFTFLFTGSYAGKLMSLKGDSENAKLSFERYY 1135
Cdd:TIGR02204  237 RIRTRALLTAIVIVLVFGAIVGV----LWVGAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGAAERLI 312
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1136 PLITRKSLIDVRDNggiKIKNSNDIKGKIEIMDVNFRYLSRPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRF 1215
Cdd:TIGR02204  313 ELLQAEPDIKAPAH---PKTLPVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRF 389
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1216 YDlkndhhivfkneqtgesskeqmqqgdeeqnvgmknanefssskegadgqsstlfKNSGKILLDGVDICDYNLKDLRNL 1295
Cdd:TIGR02204  390 YD------------------------------------------------------PQSGRILLDGVDLRQLDPAELRAR 415
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1296 FSIVSQEPMLFNMSIYENIKFGKENATREDVKRACKFAAIDEFIESLPNQYDTNVGPYGKSLSGGQKQRIAIARALLREP 1375
Cdd:TIGR02204  416 MALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDA 495
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1376 KILLLDEATSSLDSNSEKLIEKTIVDIkdKADKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVqAQGTHEELLSvQDGV 1455
Cdd:TIGR02204  496 PILLLDEATSALDAESEQLVQQALETL--MKGRTTLIIAHRLATVLKADRIVVMDQ----GRIV-AQGTHAELIA-KGGL 567

                   ....*..
gi 156095386  1456 YKKYVKL 1462
Cdd:TIGR02204  568 YARLARL 574
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
1164-1459 1.71e-81

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: 267.56  E-value: 1.71e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYLSRPNvPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfkneqtgesskeqmqqgd 1243
Cdd:cd03251     1 VEFKNVTFRYPGDGP-PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDV------------------------- 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 eeqnvgmknanefssskegadgqsstlfkNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKENATR 1323
Cdd:cd03251    55 -----------------------------DSGRILIDGHDVRDYTLASLRRQIGLVSQDVFLFNDTVAENIAYGRPGATR 105
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1324 EDVKRACKFAAIDEFIESLPNQYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIvdik 1403
Cdd:cd03251   106 EEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAAL---- 181
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 156095386 1404 DK--ADKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQaQGTHEELLSvQDGVYKKY 1459
Cdd:cd03251   182 ERlmKNRTTFVIAHRLSTIENADRIVVLED----GKIVE-RGTHEELLA-QGGVYAKL 233
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
57-727 3.51e-78

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: 270.43  E-value: 3.51e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386    57 SHRKLLGVSFVCATISGGTLPFFVSVFGVIMKNMNLGENVNDIIF-SLVLIGIF--QFILSFISSFCMDVVTTKILKTLK 133
Cdd:TIGR02203   11 PYKAGLVLAGVAMILVAATESTLAALLKPLLDDGFGGRDRSVLWWvPLVVIGLAvlRGICSFVSTYLLSWVSNKVVRDIR 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   134 IEFLKSVFYQDGQFHDNNPGSKLTSDLDFYLEQVNAGIGTKFITIFTYASAFLGLYIWSLFKNARLTLCITCVFPLIYIC 213
Cdd:TIGR02203   91 VRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLTLIVVVMLPVLSIL 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   214 GVICNKKVK-INKKTSLLyNNNTMSIIEEALVGIRTVVSYCGENTILKKFNLSEKLYSKYTLKANLMESLHIGMINgfIL 292
Cdd:TIGR02203  171 MRRVSKRLRrISKEIQNS-MGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSAGSISSPITQ--LI 247
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   293 ASYAFGFwygtriIISDLSNQQPNNDFHGGSVISILlgvlisMFMLTIILP-----NITEYMKS-LEATNNLYEIINRKP 366
Cdd:TIGR02203  248 ASLALAV------VLFIALFQAQAGSLTAGDFTAFI------TAMIALIRPlksltNVNAPMQRgLAAAESLFTLLDSPP 315
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   367 LVennQDGKKLKD--IKKIQFKNVRFHYDTRkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVII 444
Cdd:TIGR02203  316 EK---DTGTRAIEraRGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILL 391
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   445 nDSHNLKDVNLKWWRSKIGVVSQDPLLFSNSIKNNIKYslyslkdlealseesnedgfssqsdsnsrnscrakcaGDLnd 524
Cdd:TIGR02203  392 -DGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAY-------------------------------------GRT-- 431
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   525 miqttdsteliqvrknyETIEDSEVVSVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILD 604
Cdd:TIGR02203  432 -----------------EQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILD 494
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   605 EATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLSTIRYANTIFVLSNrengstvdvdvlgedptkdsneknekhdkq 684
Cdd:TIGR02203  495 EATSALDNESERLVQAALERLM--QGRTTLVIAHRLSTIEKADRIVVMDD------------------------------ 542
                          650       660       670       680
                   ....*....|....*....|....*....|....*....|...
gi 156095386   685 ekgGKnssanqkignagsyIIEQGTHDALMkNKNGiYYTMINN 727
Cdd:TIGR02203  543 ---GR--------------IVERGTHNELL-ARNG-LYAQLHN 566
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
1162-1449 8.30e-77

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: 254.07  E-value: 8.30e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1162 GKIEIMDVNFRYlsRPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfkneqtgesskeqmqq 1241
Cdd:cd03254     1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYD------------------------ 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1242 gdeeqnvgmknanefssskegadgqsstlfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKENA 1321
Cdd:cd03254    55 ------------------------------PQKGQILIDGIDIRDISRKSLRSMIGVVLQDTFLFSGTIMENIRLGRPNA 104
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1322 TREDVKRACKFAAIDEFIESLPNQYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVD 1401
Cdd:cd03254   105 TDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEK 184
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 156095386 1402 IKDkaDKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQaQGTHEELL 1449
Cdd:cd03254   185 LMK--GRTSIIIAHRLSTIKNADKILVLDD----GKIIE-EGTHDELL 225
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
1164-1458 1.20e-76

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: 253.69  E-value: 1.20e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYlsRPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfkneqtgesskeqmqqgd 1243
Cdd:cd03253     1 IEFENVTFAY--DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDV------------------------- 53
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 eeqnvgmknanefssskegadgqsstlfkNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKENATR 1323
Cdd:cd03253    54 -----------------------------SSGSILIDGQDIREVTLDSLRRAIGVVPQDTVLFNDTIGYNIRYGRPDATD 104
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1324 EDVKRACKFAAIDEFIESLPNQYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIk 1403
Cdd:cd03253   105 EEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDV- 183
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 156095386 1404 dKADKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQaQGTHEELLSvQDGVYKK 1458
Cdd:cd03253   184 -SKGRTTIVIAHRLSTIVNADKIIVLKD----GRIVE-RGTHEELLA-KGGLYAE 231
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
383-724 3.60e-75

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: 249.46  E-value: 3.60e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHYDtRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIInDSHNLKDVNLKWWRSKI 462
Cdd:cd03251     1 VEFKNVTFRYP-GDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILI-DGHDVRDYTLASLRRQI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  463 GVVSQDPLLFSNSIKNNIKYSlyslkdlealseesnedgfssqsdsnsrnscrakcagdlndmiqTTDSTEliqvrknye 542
Cdd:cd03251    79 GLVSQDVFLFNDTVAENIAYG--------------------------------------------RPGATR--------- 105
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  543 tiedSEVVSVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI 622
Cdd:cd03251   106 ----EEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAAL 181
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  623 NNLKgnENRITIIIAHRLSTIRYANTIFVLsnrengstvdvdvlgedptkdsneknekhdkqEKGGknssanqkignags 702
Cdd:cd03251   182 ERLM--KNRTTFVIAHRLSTIENADRIVVL--------------------------------EDGK-------------- 213
                         330       340
                  ....*....|....*....|..
gi 156095386  703 yIIEQGTHDALMKnKNGIYYTM 724
Cdd:cd03251   214 -IVERGTHEELLA-QGGVYAKL 233
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
1162-1456 6.75e-75

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: 261.68  E-value: 6.75e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1162 GKIEIMDVNFRYlsRPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfkneqtgesskeqmqq 1241
Cdd:COG5265   356 GEVRFENVSFGY--DPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDV----------------------- 410
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1242 gdeeqnvgmknanefssskegadgqsstlfkNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKENA 1321
Cdd:COG5265   411 -------------------------------TSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDA 459
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1322 TREDVKRACKFAAIDEFIESLPNQYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVD 1401
Cdd:COG5265   460 SEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALRE 539
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 156095386 1402 IkdKADKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQaQGTHEELLSvQDGVY 1456
Cdd:COG5265   540 V--ARGRTTLVIAHRLSTIVDADEILVLEA----GRIVE-RGTHAELLA-QGGLY 586
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
100-652 3.91e-74

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 262.74  E-value: 3.91e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   100 IFSLVLIGIFQFILSFISSFCMDVVTTKILKTLKIEFLKSVFYQDGQFHDNNPG----SKLTSDLDFYLEQV--NAGIGT 173
Cdd:TIGR00958  204 IFFMCLLSIASSVSAGLRGGSFNYTMARINLRIREDLFRSLLRQDLGFFDENKTgeltSRLSSDTQTMSRSLslNVNVLL 283
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   174 KFITIFtyasafLGLYIWSLFKNARLTLCITCVFPLIYICGVICNKKV-KINKKT--SLLYNNNtmsIIEEALVGIRTVV 250
Cdd:TIGR00958  284 RNLVML------LGLLGFMLWLSPRLTMVTLINLPLVFLAEKVFGKRYqLLSEELqeAVAKANQ---VAEEALSGMRTVR 354
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   251 SYCGENTILKKFN--LSEKL---------YSKYTLkanLMESLHIGMINGfILasyafgfWYGTRIIISdlsnqqpnNDF 319
Cdd:TIGR00958  355 SFAAEEGEASRFKeaLEETLqlnkrkalaYAGYLW---TTSVLGMLIQVL-VL-------YYGGQLVLT--------GKV 415
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   320 HGGSVISILL---------GVLISMFmltiilpniTEYMKSLEATNNLYEIINRKPLVENNQDGKKLKDIKKIQFKNVRF 390
Cdd:TIGR00958  416 SSGNLVSFLLyqeqlgeavRVLSYVY---------SGMMQAVGASEKVFEYLDRKPNIPLTGTLAPLNLEGLIEFQDVSF 486
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   391 HYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIInDSHNLKDVNLKWWRSKIGVVSQDPL 470
Cdd:TIGR00958  487 SYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLL-DGVPLVQYDHHYLHRQVALVGQEPV 565
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   471 LFSNSIKNNIKYSLyslkdlealseesnedgfssqsdsnsrNSCrakcagdlndmiqttdsteliqvrknyetiEDSEVV 550
Cdd:TIGR00958  566 LFSGSVRENIAYGL---------------------------TDT------------------------------PDEEIM 588
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   551 SVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQktinNLKGNEN 630
Cdd:TIGR00958  589 AAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQ----ESRSRAS 664
                          570       580
                   ....*....|....*....|..
gi 156095386   631 RITIIIAHRLSTIRYANTIFVL 652
Cdd:TIGR00958  665 RTVLLIAHRLSTVERADQILVL 686
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
383-728 2.61e-72

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: 241.37  E-value: 2.61e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHYDTRKdvEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIInDSHNLKDVNLKWWRSKI 462
Cdd:cd03253     1 IEFENVTFAYDPGR--PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILI-DGQDIREVTLDSLRRAI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  463 GVVSQDPLLFSNSIKNNIKYslyslkdlealseesnedgfssqsdsnsrnscrakcaGDLNdmiqttdsteliqvrknye 542
Cdd:cd03253    78 GVVPQDTVLFNDTIGYNIRY-------------------------------------GRPD------------------- 101
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  543 tIEDSEVVSVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI 622
Cdd:cd03253   102 -ATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAAL 180
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  623 NNLKgnENRITIIIAHRLSTIRYANTIFVLSNrengstvdvdvlgedptkdsneknekhdkqekgGKnssanqkignags 702
Cdd:cd03253   181 RDVS--KGRTTIVIAHRLSTIVNADKIIVLKD---------------------------------GR------------- 212
                         330       340
                  ....*....|....*....|....*.
gi 156095386  703 yIIEQGTHDALMkNKNGIYYTMINNQ 728
Cdd:cd03253   213 -IVERGTHEELL-AKGGLYAEMWKAQ 236
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
331-728 2.91e-72

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: 253.97  E-value: 2.91e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  331 VLISMFMLTIILP-NI--TEY--MK-SLEATNNLYEIINRKPLVENNQDGKKLK-DIKKIQFKNVRFHYDTRKdvEIYKD 403
Cdd:COG5265   299 VLVNAYLIQLYIPlNFlgFVYreIRqALADMERMFDLLDQPPEVADAPDAPPLVvGGGEVRFENVSFGYDPER--PILKG 376
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  404 LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIInDSHNLKDVNLKWWRSKIGVVSQDPLLFSNSIKNNIKYS 483
Cdd:COG5265   377 VSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILI-DGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYG 455
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  484 lyslkDLEAlSEEsnedgfssqsdsnsrnscrakcagdlndmiqttdsteliqvrknyetiedsEVVSVSKKVLIHDFVS 563
Cdd:COG5265   456 -----RPDA-SEE---------------------------------------------------EVEAAARAAQIHDFIE 478
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  564 ALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLSTI 643
Cdd:COG5265   479 SLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVA--RGRTTLVIAHRLSTI 556
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  644 RYANTIFVLsnrengstvdvdvlgedptkdsneknekhdkqEKGgknssanqkignagsYIIEQGTHDALMKnKNGIYYT 723
Cdd:COG5265   557 VDADEILVL--------------------------------EAG---------------RIVERGTHAELLA-QGGLYAQ 588

                  ....*
gi 156095386  724 MINNQ 728
Cdd:COG5265   589 MWARQ 593
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
838-1460 7.25e-71

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 253.11  E-value: 7.25e-71
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   838 LYPLFALLYAKYVGTLFD--FANLEANSNKYSLYIL-VIAIAMFISETLKNYYNNVIGEKVEKTMKLRLFENIMYQEISF 914
Cdd:TIGR00958  172 LSSLGEMFIPFYTGRVIDtlGGDKGPPALASAIFFMcLLSIASSVSAGLRGGSFNYTMARINLRIREDLFRSLLRQDLGF 251
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   915 FDQdsHAPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSTVMSFYFCPIVAAVLtgtyFIFMR-VFAIRARIAANK 993
Cdd:TIGR00958  252 FDE--NKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTMVT----LINLPlVFLAEKVFGKRY 325
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   994 DVEKKRVnQPGTAfvyNSDDeifkdpsfLIQEAFYNMNTVIIYGLEDYFCTLIEKAIDYSNKGQKRKTLINSMLWGFSQS 1073
Cdd:TIGR00958  326 QLLSEEL-QEAVA---KANQ--------VAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRKALAYAGYLWTTSV 393
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1074 AQFFINSFAYWFGSFLIRRGTIQVDDfmksLFTFLF----TGSYAGKLMSLKGDSENAKLSFERYYPLITRKSLIDvrDN 1149
Cdd:TIGR00958  394 LGMLIQVLVLYYGGQLVLTGKVSSGN----LVSFLLyqeqLGEAVRVLSYVYSGMMQAVGASEKVFEYLDRKPNIP--LT 467
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1150 GGIKIKNsndIKGKIEIMDVNFRYLSRPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfkne 1229
Cdd:TIGR00958  468 GTLAPLN---LEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQ------------ 532
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1230 qtgesskeqmqqgdeeqnvgmknanefssskegadgqsstlfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMS 1309
Cdd:TIGR00958  533 ------------------------------------------PTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGS 570
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1310 IYENIKFGKENATREDVKRACKFAAIDEFIESLPNQYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDS 1389
Cdd:TIGR00958  571 VRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDA 650
                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 156095386  1390 NSEKLIEktivDIKDKADKTIITIAHRIASIKRSDKIVVFnnpdRTGSFVQaQGTHEELLSvQDGVYKKYV 1460
Cdd:TIGR00958  651 ECEQLLQ----ESRSRASRTVLLIAHRLSTVERADQILVL----KKGSVVE-MGTHKQLME-DQGCYKHLV 711
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
1164-1450 2.06e-70

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: 247.36  E-value: 2.06e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYLSRPNVPiyKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfkneqtgesskeqmqqgd 1243
Cdd:COG4988   337 IELEDVSFSYPGGRPAL--DGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPP------------------------- 389
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 eeqnvgmknanefssskegadgqsstlfkNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKENATR 1323
Cdd:COG4988   390 -----------------------------YSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASD 440
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1324 EDVKRACKFAAIDEFIESLPNQYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIk 1403
Cdd:COG4988   441 EELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRL- 519
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 156095386 1404 dKADKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQaQGTHEELLS 1450
Cdd:COG4988   520 -AKGRTVILITHRLALLAQADRILVLDD----GRIVE-QGTHEELLA 560
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
825-1458 1.21e-68

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 243.00  E-value: 1.21e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  825 IAIIALSIMVAGGLYpLFALLYAkyvgtLFD--FANleANSNKYSLYILVIAIAMF---ISETLKNYYNNVIGEKVEKTM 899
Cdd:PRK11176   29 VAGVALILNAASDTF-MLSLLKP-----LLDdgFGK--ADRSVLKWMPLVVIGLMIlrgITSFISSYCISWVSGKVVMTM 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  900 KLRLFENIMYQEISFFDQDShaPGLLSAHINRD---VHLLKTGLVNNIV-----IFTHFIVLFLVSTVMS---FYFCPIV 968
Cdd:PRK11176  101 RRRLFGHMMGMPVSFFDKQS--TGTLLSRITYDseqVASSSSGALITVVregasIIGLFIMMFYYSWQLSlilIVIAPIV 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  969 AavltgtyfIFMRVFAIRARiaankDVEKKRVNQPGTafVYNSDDEIFKdpsfliqeafyNMNTVIIYGLEDyfctLIEK 1048
Cdd:PRK11176  179 S--------IAIRVVSKRFR-----NISKNMQNTMGQ--VTTSAEQMLK-----------GHKEVLIFGGQE----VETK 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1049 AIDY-SN--KGQKRKTLINSmlwGFSQSAQFFINSFAYWFGSFLIrrgtiQVDDFMKSL----FTFLFTGSYAgkLMS-L 1120
Cdd:PRK11176  229 RFDKvSNrmRQQGMKMVSAS---SISDPIIQLIASLALAFVLYAA-----SFPSVMDTLtagtITVVFSSMIA--LMRpL 298
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1121 KGDSeNAKLSFER-YYPLITRKSLIDV---RDNGGIKIKNSndiKGKIEIMDVNFRYLSRpNVPIYKDLTFSCESKKTTA 1196
Cdd:PRK11176  299 KSLT-NVNAQFQRgMAACQTLFAILDLeqeKDEGKRVIERA---KGDIEFRNVTFTYPGK-EVPALRNINFKIPAGKTVA 373
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1197 IVGETGSGKSTVMSLLMRFYDLkndhhivfkneqtgesskeqmqqgdeeqnvgmknanefssskegadgqsstlfkNSGK 1276
Cdd:PRK11176  374 LVGRSGSGKSTIANLLTRFYDI------------------------------------------------------DEGE 399
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1277 ILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKENA-TREDVKRACKFAAIDEFIESLPNQYDTNVGPYGK 1355
Cdd:PRK11176  400 ILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAYAMDFINKMDNGLDTVIGENGV 479
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1356 SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkaDKTIITIAHRIASIKRSDKIVVFNNpdrt 1435
Cdd:PRK11176  480 LLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEKADEILVVED---- 553
                         650       660
                  ....*....|....*....|...
gi 156095386 1436 GSFVQaQGTHEELLSvQDGVYKK 1458
Cdd:PRK11176  554 GEIVE-RGTHAELLA-QNGVYAQ 574
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
382-654 1.51e-67

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: 227.49  E-value: 1.51e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  382 KIQFKNVRFHYDtrKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIInDSHNLKDVNLKWWRSK 461
Cdd:cd03254     2 EIEFENVNFSYD--EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILI-DGIDIRDISRKSLRSM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  462 IGVVSQDPLLFSNSIKNNIKYslyslkdlealseesnedgfssqsdsnsrnscrakcagdlndmiqttdsteliqvrkNY 541
Cdd:cd03254    79 IGVVLQDTFLFSGTIMENIRL---------------------------------------------------------GR 101
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  542 ETIEDSEVVSVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKT 621
Cdd:cd03254   102 PNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEA 181
                         250       260       270
                  ....*....|....*....|....*....|...
gi 156095386  622 INNLkgNENRITIIIAHRLSTIRYANTIFVLSN 654
Cdd:cd03254   182 LEKL--MKGRTSIIIAHRLSTIKNADKILVLDD 212
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
383-654 1.11e-64

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: 216.87  E-value: 1.11e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHYDTRkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDsHNLKDVNLKWWRSKI 462
Cdd:cd03228     1 IEFKNVSFSYPGR-PKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDG-VDLRDLDLESLRKNI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  463 GVVSQDPLLFSNSIKNNIkyslyslkdlealseesnedgfssqsdsnsrnscrakcagdlndmiqttdsteliqvrknye 542
Cdd:cd03228    79 AYVPQDPFLFSGTIRENI-------------------------------------------------------------- 96
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  543 tiedsevvsvskkvlihdfvsalpdkyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI 622
Cdd:cd03228    97 -------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEAL 139
                         250       260       270
                  ....*....|....*....|....*....|..
gi 156095386  623 NNLKGneNRITIIIAHRLSTIRYANTIFVLSN 654
Cdd:cd03228   140 RALAK--GKTVIVIAHRLSTIRDADRIIVLDD 169
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
1164-1462 8.49e-63

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: 225.42  E-value: 8.49e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYLSRPNvPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfkneqtgesskeqmqqgd 1243
Cdd:COG4987   334 LELEDVSFRYPGAGR-PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDP------------------------- 387
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 eeqnvgmknanefssskegadgqsstlfkNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKENATR 1323
Cdd:COG4987   388 -----------------------------QSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATD 438
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1324 EDVKRACKFAAIDEFIESLPNQYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIk 1403
Cdd:COG4987   439 EELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEA- 517
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 156095386 1404 dKADKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVqAQGTHEELLSvQDGVYKKYVKL 1462
Cdd:COG4987   518 -LAGRTVLLITHRLAGLERMDRILVLED----GRIV-EQGTHEELLA-QNGRYRQLYQR 569
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
349-654 8.88e-63

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: 225.02  E-value: 8.88e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  349 MKSLEATNNLYEIINR-KPLVENNQDGKKLKDIKKIQFKNVRFHYDTRKdvEIYKDLNFTLTEGKTYAFVGESGCGKSTI 427
Cdd:COG4988   302 ANGIAAAEKIFALLDApEPAAPAGTAPLPAAGPPSIELEDVSFSYPGGR--PALDGLSLTIPPGERVALVGPSGAGKSTL 379
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  428 LKLIERLYDPTEGDVIINDsHNLKDVNLKWWRSKIGVVSQDPLLFSNSIKNNIkyslyslkdlealseesnedgfssqsd 507
Cdd:COG4988   380 LNLLLGFLPPYSGSILING-VDLSDLDPASWRRQIAWVPQNPYLFAGTIRENL--------------------------- 431
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  508 snsrnscrakcagdlndMIQTTDSTeliqvrknyetieDSEVVSVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQR 587
Cdd:COG4988   432 -----------------RLGRPDAS-------------DEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQR 481
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156095386  588 ISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLSTIRYANTIFVLSN 654
Cdd:COG4988   482 LALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLA--KGRTVILITHRLALLAQADRILVLDD 546
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
99-662 3.36e-62

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 224.13  E-value: 3.36e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   99 IIFSLVLIG--IFQFILSFISSFCMDVVTTKILKTLKIEFLKSVFYQDGQFHDNNPGSKLTSDLDFYLEQVNAGIGTKFI 176
Cdd:PRK11176   65 KWMPLVVIGlmILRGITSFISSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALI 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  177 TIFTYASAFLGLYIWSLFKNARLTLCITCVFPLI-YICGVICNKKVKINKKTsllynNNTM----SIIEEALVGIRTVVS 251
Cdd:PRK11176  145 TVVREGASIIGLFIMMFYYSWQLSLILIVIAPIVsIAIRVVSKRFRNISKNM-----QNTMgqvtTSAEQMLKGHKEVLI 219
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  252 YCGENTILKKFNLSEKLYSKYTLKANLMESLHIGMINgfILASYAFGF-WYGTRI--IISDLSnqqpnndfhGGSvISIl 328
Cdd:PRK11176  220 FGGQEVETKRFDKVSNRMRQQGMKMVSASSISDPIIQ--LIASLALAFvLYAASFpsVMDTLT---------AGT-ITV- 286
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  329 lgVLISMFMLTIILPNIT----EYMKSLEATNNLYEIINRKPlvENNQDGKKLKDIK-KIQFKNVRFHYDTrKDVEIYKD 403
Cdd:PRK11176  287 --VFSSMIALMRPLKSLTnvnaQFQRGMAACQTLFAILDLEQ--EKDEGKRVIERAKgDIEFRNVTFTYPG-KEVPALRN 361
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  404 LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIInDSHNLKDVNLKWWRSKIGVVSQDPLLFSNSIKNNIKYS 483
Cdd:PRK11176  362 INFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILL-DGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYA 440
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  484 ---LYSLKDLEalseesnedgfssqsdsnsrNSCRAKCAgdlndMiqttdsteliqvrknyetiedsevvsvskkvlihD 560
Cdd:PRK11176  441 rteQYSREQIE--------------------EAARMAYA-----M----------------------------------D 461
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  561 FVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRL 640
Cdd:PRK11176  462 FINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQ--KNRTSLVIAHRL 539
                         570       580
                  ....*....|....*....|..
gi 156095386  641 STIRYANTIFVLsnrENGSTVD 662
Cdd:PRK11176  540 STIEKADEILVV---EDGEIVE 558
MsbA_rel TIGR02204
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ...
147-662 5.83e-62

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: 223.04  E-value: 5.83e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   147 FHDNNPGSKLTSDLDFYLEQVNAGIGTKFITIFTYASAFLGLYIWSLFKNARLTLCITCVFPLIYICGVICNKKVKINKK 226
Cdd:TIGR02204  108 FFDKNRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTSLVLLAVPLVLLPILLFGRRVRKLSR 187
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   227 TSLLYNNNTMSIIEEALVGIRTVVSYCGENTILKKFNLS-EKLYsKYTLKANLMESLHIGMINGFILASYAFGFWYGTRI 305
Cdd:TIGR02204  188 ESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAvEKAY-EAARQRIRTRALLTAIVIVLVFGAIVGVLWVGAHD 266
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   306 IISdlsnqqpnNDFHGGSVISILLGVLISMFMLTIILPNITEYMKSLEATNNLYEIINRKPLVENNQDGKKL--KDIKKI 383
Cdd:TIGR02204  267 VIA--------GKMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGAAERLIELLQAEPDIKAPAHPKTLpvPLRGEI 338
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   384 QFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIInDSHNLKDVNLKWWRSKIG 463
Cdd:TIGR02204  339 EFEQVNFAYPARPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILL-DGVDLRQLDPAELRARMA 417
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   464 VVSQDPLLFSNSIKNNIKYslyslkdlealseesnedGFSSQSDSNSRNSCRAKCAgdlndmiqttdsteliqvrknyet 543
Cdd:TIGR02204  418 LVPQDPVLFAASVMENIRY------------------GRPDATDEEVEAAARAAHA------------------------ 455
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   544 iedsevvsvskkvliHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTIN 623
Cdd:TIGR02204  456 ---------------HEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALE 520
                          490       500       510
                   ....*....|....*....|....*....|....*....
gi 156095386   624 NLKgnENRITIIIAHRLSTIRYANTIFVLsnrENGSTVD 662
Cdd:TIGR02204  521 TLM--KGRTTLIIAHRLATVLKADRIVVM---DQGRIVA 554
ABC_6TM_Pgp_ABCB1_D2_like cd18578
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ...
825-1144 1.38e-61

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: 213.85  E-value: 1.38e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  825 IAIIALSIMVAGGLYPLFALLYAKYVGTLF--DFANLEANSNKYSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMKLR 902
Cdd:cd18578    11 LLLGLIGAIIAGAVFPVFAILFSKLISVFSlpDDDELRSEANFWALMFLVLAIVAGIAYFLQGYLFGIAGERLTRRLRKL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  903 LFENIMYQEISFFDQDSHAPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSTVMSFYFCPIVAAVLTGTYFIFMRV 982
Cdd:cd18578    91 AFRAILRQDIAWFDDPENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLALVGLATVPLLLLA 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  983 FAIRARIAANKDVEKKRVNQPGTAFVYnsddeifkdpsfliqEAFYNMNTVIIYGLEDYFCTLIEKAIDYSNKGQKRKTL 1062
Cdd:cd18578   171 GYLRMRLLSGFEEKNKKAYEESSKIAS---------------EAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRAL 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1063 INSMLWGFSQSAQFFINSFAYWFGSFLIRRGTIQVDDFMKSLFTFLFTGSYAGKLMSLKGDSENAKLSFERYYPLITRKS 1142
Cdd:cd18578   236 ISGLGFGLSQSLTFFAYALAFWYGGRLVANGEYTFEQFFIVFMALIFGAQSAGQAFSFAPDIAKAKAAAARIFRLLDRKP 315

                  ..
gi 156095386 1143 LI 1144
Cdd:cd18578   316 EI 317
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
1164-1431 2.06e-61

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: 207.24  E-value: 2.06e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYLSRPNvPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfkneqtgesskeqmqqgd 1243
Cdd:cd03228     1 IEFKNVSFSYPGRPK-PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDP------------------------- 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 eeqnvgmknanefssskegadgqsstlfkNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIkfgkenatr 1323
Cdd:cd03228    55 -----------------------------TSGEILIDGVDLRDLDLESLRKNIAYVPQDPFLFSGTIRENI--------- 96
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1324 edvkrackfaaidefieslpnqydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIK 1403
Cdd:cd03228    97 ---------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRALA 143
                         250       260
                  ....*....|....*....|....*...
gi 156095386 1404 DkaDKTIITIAHRIASIKRSDKIVVFNN 1431
Cdd:cd03228   144 K--GKTVIVIAHRLSTIRDADRIIVLDD 169
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
815-1456 8.97e-61

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: 219.59  E-value: 8.97e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   815 YREIFSYKKDIAIIALSIMVAGGLYPLFALLYAKYVGTLFDFANLEANSNK---YSLYILVIAIAMFISETLKNYYNNVI 891
Cdd:TIGR02203    2 FRRLWSYVRPYKAGLVLAGVAMILVAATESTLAALLKPLLDDGFGGRDRSVlwwVPLVVIGLAVLRGICSFVSTYLLSWV 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   892 GEKVEKTMKLRLFENIMYQEISFFDQDSHAPGLL--------SAHINRDVhlLKTGLVNNIVIFTHFIVLFLvstvMSFY 963
Cdd:TIGR02203   82 SNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSritfdseqVASAATDA--FIVLVRETLTVIGLFIVLLY----YSWQ 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   964 FCPIVAAVLTGTYFIfMRVFAIRARiaankDVEKKRVNQPGTAfvynsddeifkdpSFLIQEAFYNMNTVIIYGLEDY-- 1041
Cdd:TIGR02203  156 LTLIVVVMLPVLSIL-MRRVSKRLR-----RISKEIQNSMGQV-------------TTVAEETLQGYRVVKLFGGQAYet 216
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1042 --FctlieKAIDYSNKG-QKRKTLINSMLWGFSQSAQFFINSFAYWFGSFLIRRGTIQVDDFMKSLFTFLFTGSYAGKLM 1118
Cdd:TIGR02203  217 rrF-----DAVSNRNRRlAMKMTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLT 291
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1119 SLKGDSENAKLSFERYYPLITRKsliDVRDNGGIKIKNsndIKGKIEIMDVNFRYLSRpNVPIYKDLTFSCESKKTTAIV 1198
Cdd:TIGR02203  292 NVNAPMQRGLAAAESLFTLLDSP---PEKDTGTRAIER---ARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALV 364
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1199 GETGSGKSTVMSLLMRFYDlkndhhivfkneqtgesskeqmqqgdeeqnvgmknanefssskegadgqsstlfKNSGKIL 1278
Cdd:TIGR02203  365 GRSGSGKSTLVNLIPRFYE------------------------------------------------------PDSGQIL 390
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1279 LDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGK-ENATREDVKRACKFAAIDEFIESLPNQYDTNVGPYGKSL 1357
Cdd:TIGR02203  391 LDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRtEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLL 470
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1358 SGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkaDKTIITIAHRIASIKRSDKIVVFNNpdrtGS 1437
Cdd:TIGR02203  471 SGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLSTIEKADRIVVMDD----GR 544
                          650
                   ....*....|....*....
gi 156095386  1438 FVQaQGTHEELLSvQDGVY 1456
Cdd:TIGR02203  545 IVE-RGTHNELLA-RNGLY 561
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
1145-1449 2.01e-59

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 215.98  E-value: 2.01e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1145 DVRDNGGIKikNSNDIKGKIEIMDVNFRYL-SRPNVpiyKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDLKndhh 1223
Cdd:PRK13657  318 DVRDPPGAI--DLGRVKGAVEFDDVSFSYDnSRQGV---EDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQ---- 388
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1224 ivfkneqtgesskeqmqqgdeeqnvgmknanefssskegadgqsstlfknSGKILLDGVDICDYNLKDLRNLFSIVSQEP 1303
Cdd:PRK13657  389 --------------------------------------------------SGRILIDGTDIRTVTRASLRRNIAVVFQDA 418
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1304 MLFNMSIYENIKFGKENATREDVKRACKFAAIDEFIESLPNQYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEA 1383
Cdd:PRK13657  419 GLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEA 498
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156095386 1384 TSSLDSNSEKLIEKTIVDIKDkaDKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQAqGTHEELL 1449
Cdd:PRK13657  499 TSALDVETEAKVKAALDELMK--GRTTFIIAHRLSTVRNADRILVFDN----GRVVES-GSFDELV 557
ABC_6TM_Pgp_ABCB1_D1_like cd18577
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ...
62-358 2.49e-59

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: 206.56  E-value: 2.49e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   62 LGVSFVCATISGGTLPFFVSVFGVIMKNMN-----------LGENVNDIIFSLVLIGIFQFILSFISSFCMDVVTTKILK 130
Cdd:cd18577     1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFTdfgsgesspdeFLDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQAR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  131 TLKIEFLKSVFYQDGQFHDNNPGSKLTSDLDFYLEQVNAGIGTKFITIFTYASAFLGLYIWSLFKNARLTLCITCVFPLI 210
Cdd:cd18577    81 RIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLPLI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  211 YICGVICNKKVKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGENTILKKFNLSEKLYSKYTLKANLMESLHIGMINGF 290
Cdd:cd18577   161 AIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLFFI 240
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156095386  291 ILASYAFGFWYGTRIIISDLSNqqpnndfhGGSVISILLGVLISMFMLTIILPNITEYMKSLEATNNL 358
Cdd:cd18577   241 IFAMYALAFWYGSRLVRDGEIS--------PGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
1159-1428 5.78e-59

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: 202.70  E-value: 5.78e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1159 DIKGKIEIMDVNFRYLSRPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYdlkndhhivfkneqtgesskeQ 1238
Cdd:cd03248     7 HLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFY---------------------Q 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1239 MQQGdeeqnvgmknanefssskegadgqsstlfknsgKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGK 1318
Cdd:cd03248    66 PQGG---------------------------------QVLLDGKPISQYEHKYLHSKVSLVGQEPVLFARSLQDNIAYGL 112
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1319 ENATREDVKRACKFAAIDEFIESLPNQYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKT 1398
Cdd:cd03248   113 QSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQA 192
                         250       260       270
                  ....*....|....*....|....*....|
gi 156095386 1399 IVDikDKADKTIITIAHRIASIKRSDKIVV 1428
Cdd:cd03248   193 LYD--WPERRTVLVIAHRLSTVERADQILV 220
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
382-652 1.13e-57

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: 198.85  E-value: 1.13e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  382 KIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIInDSHNLKDVNLKWWRSK 461
Cdd:cd03248    11 IVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLL-DGKPISQYEHKYLHSK 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  462 IGVVSQDPLLFSNSIKNNIKYSLyslkdlealseesnedgfssqsdsnsrnscrakcagdlndmiqttdsteliqvrkny 541
Cdd:cd03248    90 VSLVGQEPVLFARSLQDNIAYGL--------------------------------------------------------- 112
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  542 ETIEDSEVVSVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKT 621
Cdd:cd03248   113 QSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQA 192
                         250       260       270
                  ....*....|....*....|....*....|.
gi 156095386  622 INNlkGNENRITIIIAHRLSTIRYANTIFVL 652
Cdd:cd03248   193 LYD--WPERRTVLVIAHRLSTVERADQILVL 221
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
358-662 2.87e-55

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 203.65  E-value: 2.87e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  358 LYEIINRKPLVENNQDGKKLKDIK-KIQFKNVRFHYD-TRKDVEiykDLNFTLTEGKTYAFVGESGCGKSTILKLIERLY 435
Cdd:PRK13657  309 FFEVEDAVPDVRDPPGAIDLGRVKgAVEFDDVSFSYDnSRQGVE---DVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVF 385
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  436 DPTEGDVIInDSHNLKDVNLKWWRSKIGVVSQDPLLFSNSIKNNIKyslyslkdlealseesnedgfssqsdsnsrnscr 515
Cdd:PRK13657  386 DPQSGRILI-DGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIR---------------------------------- 430
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  516 akcagdlndmIQTTDSTeliqvrknyetieDSEVVSVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAII 595
Cdd:PRK13657  431 ----------VGRPDAT-------------DEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALL 487
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156095386  596 RNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLSTIRYANTIFVLsnrENGSTVD 662
Cdd:PRK13657  488 KDPPILILDEATSALDVETEAKVKAALDELM--KGRTTFIIAHRLSTVRNADRILVF---DNGRVVE 549
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
383-728 7.48e-55

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: 191.16  E-value: 7.48e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHYdtRKD-VEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIInDSHNLKDVNLKWWRSK 461
Cdd:cd03252     1 ITFEHVRFRY--KPDgPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLV-DGHDLALADPAWLRRQ 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  462 IGVVSQDPLLFSNSIKNNIkyslySLKDlEALSEEsnedgfssqsdsnsrnscrakcagdlndmiqttdsteliqvrkny 541
Cdd:cd03252    78 VGVVLQENVLFNRSIRDNI-----ALAD-PGMSME--------------------------------------------- 106
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  542 etiedsEVVSVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKT 621
Cdd:cd03252   107 ------RVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRN 180
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  622 INNLkgNENRITIIIAHRLSTIRYANTIFVLsnrengstvdvdvlgedptkdsneknekhdkqEKGGknssanqkignag 701
Cdd:cd03252   181 MHDI--CAGRTVIIIAHRLSTVKNADRIIVM--------------------------------EKGR------------- 213
                         330       340
                  ....*....|....*....|....*..
gi 156095386  702 syIIEQGTHDALMKnKNGIYYTMINNQ 728
Cdd:cd03252   214 --IVEQGSHDELLA-ENGLYAYLYQLQ 237
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
1162-1431 7.39e-54

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: 187.70  E-value: 7.39e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1162 GKIEIMDVNFRYlsRPN-VPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfkneqtgesskeqmq 1240
Cdd:cd03244     1 GDIEFKNVSLRY--RPNlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVEL---------------------- 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1241 qgdeeqnvgmknanefssskegadgqsstlfkNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIK-FGKe 1319
Cdd:cd03244    57 --------------------------------SSGSILIDGVDISKIGLHDLRSRISIIPQDPVLFSGTIRSNLDpFGE- 103
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1320 nATREDVKRACKFAAIDEFIESLPNQYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTi 1399
Cdd:cd03244   104 -YSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKT- 181
                         250       260       270
                  ....*....|....*....|....*....|...
gi 156095386 1400 vdIKDK-ADKTIITIAHRIASIKRSDKIVVFNN 1431
Cdd:cd03244   182 --IREAfKDCTVLTIAHRLDTIIDSDRILVLDK 212
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
1164-1462 1.45e-53

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: 187.69  E-value: 1.45e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYlsRPNVP-IYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYdlkndhhivfkneqtgesskeqmqqg 1242
Cdd:cd03252     1 ITFEHVRFRY--KPDGPvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFY-------------------------- 52
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1243 deeqnvgmknanefssskegadgqsstlFKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKENAT 1322
Cdd:cd03252    53 ----------------------------VPENGRVLVDGHDLALADPAWLRRQVGVVLQENVLFNRSIRDNIALADPGMS 104
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1323 REDVKRACKFAAIDEFIESLPNQYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDI 1402
Cdd:cd03252   105 MERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDI 184
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1403 kdKADKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQaQGTHEELLSvQDGVYKKYVKL 1462
Cdd:cd03252   185 --CAGRTVIIIAHRLSTVKNADRIIVMEK----GRIVE-QGSHDELLA-ENGLYAYLYQL 236
type_I_sec_HlyB TIGR01846
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ...
815-1458 1.36e-52

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: 198.04  E-value: 1.36e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   815 YREIFSykkDIAIIALSIMVAGGLYPLF------ALLYAKYVGTLfdfanleansNKYSLYILVIAIAMFISETLKNYYN 888
Cdd:TIGR01846  137 YRKQFR---EVLLISLALQLFALVTPLLfqvvidKVLVHRGLSTL----------SVLALAMLAVAIFEPALGGLRTYLF 203
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   889 NVIGEKVEKTMKLRLFENIMYQEISFFDqdSHAPGLLSAHInRDVHLLK---TGLVNNIVIFTHFIVLFLvsTVMSFYFC 965
Cdd:TIGR01846  204 AHLTSRIDVELGARLYRHLLGLPLGYFE--SRRVGDTVARV-RELEQIRnflTGSALTVVLDLLFVVVFL--AVMFFYSP 278
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   966 PIVAAVLTGTYFIFMRVFAIRARIaankdveKKRVNQpgtAFVYNSDDEifkdpSFLIqEAFYNMNTVIIYGLEDYFCTL 1045
Cdd:TIGR01846  279 TLTGVVIGSLVCYALLSVFVGPIL-------RKRVED---KFERSAAAT-----SFLV-ESVTGIETIKATATEPQFQNR 342
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1046 IEKAI-DYSNKGQKrktLINSMLWGfSQSAQFfIN--SFA--YWFGSFLIRRGTIQVDdfmkSLFTF-LFTGSYAG---K 1116
Cdd:TIGR01846  343 WDRQLaAYVAASFR---VTNLGNIA-GQAIEL-IQklTFAilLWFGAHLVIGGALSPG----QLVAFnMLAGRVTQpvlR 413
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1117 LMSLKGDSENAKLSFERyyplitrksLIDV----RDNGGIKIKNSNDIKGKIEIMDVNFRYlsRPNVP-IYKDLTFSCES 1191
Cdd:TIGR01846  414 LAQLWQDFQQTGIALER---------LGDIlnspTEPRSAGLAALPELRGAITFENIRFRY--APDSPeVLSNLNLDIKP 482
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1192 KKTTAIVGETGSGKSTVMSLLMRFYDLKNdhhivfkneqtgesskeqmqqgdeeqnvgmknanefssskegadgqsstlf 1271
Cdd:TIGR01846  483 GEFIGIVGPSGSGKSTLTKLLQRLYTPQH--------------------------------------------------- 511
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1272 knsGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKENATREDVKRACKFAAIDEFIESLPNQYDTNVG 1351
Cdd:TIGR01846  512 ---GQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCNPGAPFEHVIHAAKLAGAHDFISELPQGYNTEVG 588
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1352 PYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIkdKADKTIITIAHRIASIKRSDKIVVFNN 1431
Cdd:TIGR01846  589 EKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREI--CRGRTVIIIAHRLSTVRACDRIIVLEK 666
                          650       660
                   ....*....|....*....|....*..
gi 156095386  1432 pdrtGSFVQaQGTHEELLSvQDGVYKK 1458
Cdd:TIGR01846  667 ----GQIAE-SGRHEELLA-LQGLYAR 687
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
321-724 1.34e-51

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: 192.29  E-value: 1.34e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  321 GGSVISILL------------GVLISMFMLTII--------LPN-ITEYMKSLEATNNLYEIINRKPLVENNQDGKKLKD 379
Cdd:COG4987   251 GLAVVAVLWlaaplvaagalsGPLLALLVLAALalfealapLPAaAQHLGRVRAAARRLNELLDAPPAVTEPAEPAPAPG 330
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  380 IKKIQFKNVRFHYDTRkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDsHNLKDVNLKWWR 459
Cdd:COG4987   331 GPSLELEDVSFRYPGA-GRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGG-VDLRDLDEDDLR 408
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  460 SKIGVVSQDPLLFSNSIKNNIKyslysLKDLEAlseesnedgfssqsdsnsrnscrakcagdlndmiqttdsteliqvrk 539
Cdd:COG4987   409 RRIAVVPQRPHLFDTTLRENLR-----LARPDA----------------------------------------------- 436
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  540 nyetiEDSEVVSVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQ 619
Cdd:COG4987   437 -----TDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALL 511
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  620 KTInnLKGNENRITIIIAHRLSTIRYANTIFVLsnrENGStvdvdvlgedptkdsneknekhdkqekggknssanqkign 699
Cdd:COG4987   512 ADL--LEALAGRTVLLITHRLAGLERMDRILVL---EDGR---------------------------------------- 546
                         410       420
                  ....*....|....*....|....*
gi 156095386  700 agsyIIEQGTHDALMKnKNGIYYTM 724
Cdd:COG4987   547 ----IVEQGTHEELLA-QNGRYRQL 566
type_I_sec_HlyB TIGR01846
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ...
153-652 1.53e-50

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: 191.88  E-value: 1.53e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   153 GSKLTSDLDFYLEQVNAGIgtkfitIFTYASAFLGLYIWSLfknarltlciTCVFPLIYICGVICNKKVKINKKTSllyn 232
Cdd:TIGR01846  254 GSALTVVLDLLFVVVFLAV------MFFYSPTLTGVVIGSL----------VCYALLSVFVGPILRKRVEDKFERS---- 313
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   233 NNTMSIIEEALVGIRTVVSYCGENTILKKFN--LSEKLYSKYTL-KANLMESLHIGMINGFilaSYAFGFWYGTRIIIsd 309
Cdd:TIGR01846  314 AAATSFLVESVTGIETIKATATEPQFQNRWDrqLAAYVAASFRVtNLGNIAGQAIELIQKL---TFAILLWFGAHLVI-- 388
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   310 lsnqqpnndfhGGSvISILLGVLISMFMLTIILPNI------TEYMKSLEATNNLYEIINRKplVENNQDGK-KLKDIK- 381
Cdd:TIGR01846  389 -----------GGA-LSPGQLVAFNMLAGRVTQPVLrlaqlwQDFQQTGIALERLGDILNSP--TEPRSAGLaALPELRg 454
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   382 KIQFKNVRFHYDtRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIInDSHNLKDVNLKWWRSK 461
Cdd:TIGR01846  455 AITFENIRFRYA-PDSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLV-DGVDLAIADPAWLRRQ 532
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   462 IGVVSQDPLLFSNSIKNNIkyslyslkdlealseesnedgfsSQSDSNsrnscrakcagdlndmiqttdsteliqvrkny 541
Cdd:TIGR01846  533 MGVVLQENVLFSRSIRDNI-----------------------ALCNPG-------------------------------- 557
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   542 etIEDSEVVSVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKT 621
Cdd:TIGR01846  558 --APFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRN 635
                          490       500       510
                   ....*....|....*....|....*....|.
gi 156095386   622 INNLkgNENRITIIIAHRLSTIRYANTIFVL 652
Cdd:TIGR01846  636 MREI--CRGRTVIIIAHRLSTVRACDRIIVL 664
ABC_membrane pfam00664
ABC transporter transmembrane region; This family represents a unit of six transmembrane ...
62-309 1.45e-48

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: 174.75  E-value: 1.45e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386    62 LGVSFVCATISGGTLPFFVSVFGVIMKNM---NLGENVNDIIFSLVLI--GIFQFILSFISSFCMDVVTTKILKTLKIEF 136
Cdd:pfam00664    1 LILAILLAILSGAISPAFPLVLGRILDVLlpdGDPETQALNVYSLALLllGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   137 LKSVFYQDGQFHDNNPGSKLTSDLDFYLEQVNAGIGTKFITIFTYASAFLGLYIWSLFKNARLTLCITCVFPLIYICGVI 216
Cdd:pfam00664   81 FKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAV 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   217 CNKKVKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGENTILKKFNLSEKLYSKYTLKANLMESLHIGMINGFILASYA 296
Cdd:pfam00664  161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYA 240
                          250
                   ....*....|...
gi 156095386   297 FGFWYGTRIIISD 309
Cdd:pfam00664  241 LALWFGAYLVISG 253
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
1162-1431 3.87e-48

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: 171.23  E-value: 3.87e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1162 GKIEIMDVNFRYlsrPNVPI--YKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfkneqtgesskeqm 1239
Cdd:cd03245     1 GRIEFRNVSFSY---PNQEIpaLDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYK---------------------- 55
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1240 qqgdeeqnvgmknanefssskegadgqsstlfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKE 1319
Cdd:cd03245    56 --------------------------------PTSGSVLLDGTDIRQLDPADLRRNIGYVPQDVTLFYGTLRDNITLGAP 103
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1320 NATREDVKRACKFAAIDEFIESLPNQYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSE-KLIEKt 1398
Cdd:cd03245   104 LADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEeRLKER- 182
                         250       260       270
                  ....*....|....*....|....*....|....
gi 156095386 1399 ivdIKD-KADKTIITIAHRIASIKRSDKIVVFNN 1431
Cdd:cd03245   183 ---LRQlLGDKTLIIITHRPSLLDLVDRIIVMDS 213
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
1038-1458 1.34e-44

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: 173.77  E-value: 1.34e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1038 LEDYFCTLIEKAIDYSnKGQKRKTLINSMLwgfsqsaQFFINSFAYWFGSFLIRRGTIQVDdfmkSLFTFLFTGSY---- 1113
Cdd:TIGR01193  360 IDSEFGDYLNKSFKYQ-KADQGQQAIKAVT-------KLILNVVILWTGAYLVMRGKLTLG----QLITFNALLSYfltp 427
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1114 AGKLMSLKGDSENAKLSFERyyplITRKSLIDVRDNGGIKIKNSNDIKGKIEIMDVNFRYlsRPNVPIYKDLTFSCESKK 1193
Cdd:TIGR01193  428 LENIINLQPKLQAARVANNR----LNEVYLVDSEFINKKKRTELNNLNGDIVINDVSYSY--GYGSNILSDISLTIKMNS 501
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1194 TTAIVGETGSGKSTVMSLLMRFYDlkndhhivfkneqtgesskeqmqqgdeeqnvgmknanefssskegadgqsstlfKN 1273
Cdd:TIGR01193  502 KTTIVGMSGSGKSTLAKLLVGFFQ------------------------------------------------------AR 527
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1274 SGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFG-KENATREDVKRACKFAAIDEFIESLPNQYDTNVGP 1352
Cdd:TIGR01193  528 SGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGaKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSE 607
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1353 YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKdkaDKTIITIAHRIASIKRSDKIVVFNNp 1432
Cdd:TIGR01193  608 EGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQ---DKTIIFVAHRLSVAKQSDKIIVLDH- 683
                          410       420
                   ....*....|....*....|....*.
gi 156095386  1433 drtGSFVQaQGTHEELLSvQDGVYKK 1458
Cdd:TIGR01193  684 ---GKIIE-QGSHDELLD-RNGFYAS 704
ABC_membrane pfam00664
ABC transporter transmembrane region; This family represents a unit of six transmembrane ...
825-1110 4.91e-44

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: 161.66  E-value: 4.91e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   825 IAIIALSIMVAGGLYPLFALLYAKYVGTLFDFANLEAN-SNKYSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMKLRL 903
Cdd:pfam00664    1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQaLNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   904 FENIMYQEISFFDQdsHAPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSTVMSFYFCPIVAAVLTGTYFIFMRVF 983
Cdd:pfam00664   81 FKKILRQPMSFFDT--NSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVS 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   984 AIRARIAAN-KDVEKKRVNQPGTafvynsddeifkdpsfLIQEAFYNMNTVIIYGLEDYFCTLIEKAIDYSNKGQKRKTL 1062
Cdd:pfam00664  159 AVFAKILRKlSRKEQKAVAKASS----------------VAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAV 222
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 156095386  1063 INSMLWGFSQSAQFFINSFAYWFGSFLIRRGTIQVDDF--MKSLFTFLFT 1110
Cdd:pfam00664  223 ANGLSFGITQFIGYLSYALALWFGAYLVISGELSVGDLvaFLSLFAQLFG 272
ABC_6TM_Pgp_ABCB1_D2_like cd18578
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ...
58-366 9.30e-44

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: 162.24  E-value: 9.30e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   58 HRKLLGVSFVCATISGGTLPFFVSVFGVIMKNMNLG------ENVNDIIFSLVLIGIFQFILSFISSFCMDVVTTKILKT 131
Cdd:cd18578     7 EWPLLLLGLIGAIIAGAVFPVFAILFSKLISVFSLPdddelrSEANFWALMFLVLAIVAGIAYFLQGYLFGIAGERLTRR 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  132 LKIEFLKSVFYQDGQFHD---NNPGSkLTSDLDFYLEQVNAGIGTKFITIFTYASAFLGLYIWSLFKNARLTLCITCVFP 208
Cdd:cd18578    87 LRKLAFRAILRQDIAWFDdpeNSTGA-LTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLALVGLATVP 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  209 LIYICGVIcnkKVKINKKTSLLYNN---NTMSIIEEALVGIRTVVSYCGENTILKKFNLSEKLYSKYTLKANLMESLHIG 285
Cdd:cd18578   166 LLLLAGYL---RMRLLSGFEEKNKKayeESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGLGFG 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  286 MINGFILASYAFGFWYGTRIIISDLSNQQpnndfhggSVISILLGVLISMFMLTIILPNITEYMKSLEATNNLYEIINRK 365
Cdd:cd18578   243 LSQSLTFFAYALAFWYGGRLVANGEYTFE--------QFFIVFMALIFGAQSAGQAFSFAPDIAKAKAAAARIFRLLDRK 314

                  .
gi 156095386  366 P 366
Cdd:cd18578   315 P 315
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
349-652 1.10e-43

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: 167.85  E-value: 1.10e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   349 MKSLEATNNLYEIINRKPLVENNQDGKKLKDIKKIQFKNVRFHYDTRKDVeiYKDLNFTLTEGKTYAFVGESGCGKSTIL 428
Cdd:TIGR02857  288 ADGVAAAEALFAVLDAAPRPLAGKAPVTAAPASSLEFSGVSVAYPGRRPA--LRPVSFTVPPGERVALVGPSGAGKSTLL 365
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   429 KLIERLYDPTEGDVIINDShNLKDVNLKWWRSKIGVVSQDPLLFSNSIKNNIKyslysLKDLEAlseesnedgfssqsds 508
Cdd:TIGR02857  366 NLLLGFVDPTEGSIAVNGV-PLADADADSWRDQIAWVPQHPFLFAGTIAENIR-----LARPDA---------------- 423
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   509 nsrnscrakcagdlndmiqttdsteliqvrknyetiEDSEVVSVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRI 588
Cdd:TIGR02857  424 ------------------------------------SDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRL 467
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156095386   589 SIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLSTIRYANTIFVL 652
Cdd:TIGR02857  468 ALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALA--QGRTVLLVTHRLALAALADRIVVL 529
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
382-654 3.79e-43

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: 156.88  E-value: 3.79e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  382 KIQFKNVRFHYdtRKDVE-IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIInDSHNLKDVNLKWWRS 460
Cdd:cd03244     2 DIEFKNVSLRY--RPNLPpVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILI-DGVDISKIGLHDLRS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  461 KIGVVSQDPLLFSNSIKNNIkyslyslkdlealseesneDGFSSQSDSnsrnscrakcagdlndmiqttdsteliqvrkn 540
Cdd:cd03244    79 RISIIPQDPVLFSGTIRSNL-------------------DPFGEYSDE-------------------------------- 107
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  541 yetiedsEVVSVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQK 620
Cdd:cd03244   108 -------ELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQK 180
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 156095386  621 TI-NNLKgneNRITIIIAHRLSTIRYANTIFVLSN 654
Cdd:cd03244   181 TIrEAFK---DCTVLTIAHRLDTIIDSDRILVLDK 212
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
1164-1428 4.69e-43

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: 165.92  E-value: 4.69e-43
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1164 IEIMDVNFRYLSRPNVPiyKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfkneqtgesskeqmqqgd 1243
Cdd:TIGR02857  322 LEFSGVSVAYPGRRPAL--RPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVD-------------------------- 373
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1244 eeqnvgmknanefssskegadgqsstlfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKENATR 1323
Cdd:TIGR02857  374 ----------------------------PTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASD 425
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1324 EDVKRACKFAAIDEFIESLPNQYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIK 1403
Cdd:TIGR02857  426 AEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALA 505
                          250       260
                   ....*....|....*....|....*
gi 156095386  1404 DkaDKTIITIAHRIASIKRSDKIVV 1428
Cdd:TIGR02857  506 Q--GRTVLLVTHRLALAALADRIVV 528
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
382-652 9.30e-43

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: 155.83  E-value: 9.30e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  382 KIQFKNVRFHYDTRKDVEIyKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIInDSHNLKDVNLKWWRSK 461
Cdd:cd03245     2 RIEFRNVSFSYPNQEIPAL-DNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLL-DGTDIRQLDPADLRRN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  462 IGVVSQDPLLFSNSIKNNIkyslySLKDLEAlseesnedgfssqsdsnsrnscrakcagdlndmiqttdsteliqvrkny 541
Cdd:cd03245    80 IGYVPQDVTLFYGTLRDNI-----TLGAPLA------------------------------------------------- 105
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  542 etiEDSEVVSVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKT 621
Cdd:cd03245   106 ---DDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNSEERLKER 182
                         250       260       270
                  ....*....|....*....|....*....|.
gi 156095386  622 INNLKGneNRITIIIAHRLSTIRYANTIFVL 652
Cdd:cd03245   183 LRQLLG--DKTLIIITHRPSLLDLVDRIIVM 211
NHLM_micro_ABC1 TIGR03796
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ...
382-661 5.44e-41

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: 162.81  E-value: 5.44e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   382 KIQFKNVRFHYdTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIInDSHNLKDVNLKWWRSK 461
Cdd:TIGR03796  477 YVELRNITFGY-SPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILF-DGIPREEIPREVLANS 554
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   462 IGVVSQDPLLFSNSIKNNIkyslySLKDlealseesnedgfssqsdsnsrnscrakcagdlndmiqttdsteliqvrkny 541
Cdd:TIGR03796  555 VAMVDQDIFLFEGTVRDNL-----TLWD---------------------------------------------------- 577
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   542 ETIEDSEVVSVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVqkt 621
Cdd:TIGR03796  578 PTIPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKII--- 654
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 156095386   622 INNLKgneNR--ITIIIAHRLSTIRYANTIFVLsnrENGSTV 661
Cdd:TIGR03796  655 DDNLR---RRgcTCIIVAHRLSTIRDCDEIIVL---ERGKVV 690
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
1130-1462 7.04e-41

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 160.38  E-value: 7.04e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1130 SFERYYPLITRKSLIDVRDNGGIKIKnsndiKGKIEIMDVNFRYLSRPNvPIYKDLTFSCESKKTTAIVGETGSGKSTVM 1209
Cdd:PRK11160  310 SARRINEITEQKPEVTFPTTSTAAAD-----QVSLTLNNVSFTYPDQPQ-PVLKGLSLQIKAGEKVALLGRTGCGKSTLL 383
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1210 SLLMRFYDlkndhhivfkneqtgesskeqmqqgdeeqnvgmknanefssskegadgqsstlfKNSGKILLDGVDICDYNL 1289
Cdd:PRK11160  384 QLLTRAWD------------------------------------------------------PQQGEILLNGQPIADYSE 409
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1290 KDLRNLFSIVSQEPMLFNMSIYENIKFGKENATREDVKRACKFAAIDEFIESlPNQYDTNVGPYGKSLSGGQKQRIAIAR 1369
Cdd:PRK11160  410 AALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIAR 488
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1370 ALLREPKILLLDEATSSLDSNSEKLIEKTIVDIkdKADKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVqAQGTHEELL 1449
Cdd:PRK11160  489 ALLHDAPLLLLDEPTEGLDAETERQILELLAEH--AQNKTVLMITHRLTGLEQFDRICVMDN----GQII-EQGTHQELL 561
                         330
                  ....*....|...
gi 156095386 1450 SVQDGVYKKYVKL 1462
Cdd:PRK11160  562 AQQGRYYQLKQRL 574
NHLM_micro_ABC2 TIGR03797
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ...
1083-1461 9.34e-41

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: 161.66  E-value: 9.34e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1083 YWFGSFLIRRGTIQVDDFMKslFTFLFtGSYAGKLMSLKG---DSENAKLSFERYYPLItrKSLIDVRDNGgikiKNSND 1159
Cdd:TIGR03797  377 FAAAISLLGGAGLSLGSFLA--FNTAF-GSFSGAVTQLSNtliSILAVIPLWERAKPIL--EALPEVDEAK----TDPGK 447
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1160 IKGKIEIMDVNFRYlsRPNVP-IYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFydlkndhhivfknEQTGesskeq 1238
Cdd:TIGR03797  448 LSGAIEVDRVTFRY--RPDGPlILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGF-------------ETPE------ 506
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1239 mqqgdeeqnvgmknanefssskegadgqsstlfknSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKfGK 1318
Cdd:TIGR03797  507 -----------------------------------SGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIA-GG 550
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1319 ENATREDVKRACKFAAIDEFIESLPNQYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKT 1398
Cdd:TIGR03797  551 APLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSES 630
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 156095386  1399 IvdikDKADKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQaQGTHEELLSVqDGVYKKYVK 1461
Cdd:TIGR03797  631 L----ERLKVTRIVIAHRLSTIRNADRIYVLDA----GRVVQ-QGTYDELMAR-EGLFAQLAR 683
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
1185-1457 9.60e-41

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 160.01  E-value: 9.60e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1185 LTFSCESKKTTAIVGETGSGKSTVMSLLMRF--Ydlkndhhivfkneqtgesskeqmqqgdeeqnvgmknanefssskeg 1262
Cdd:PRK11174  369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFlpY---------------------------------------------- 402
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1263 adgqsstlfknSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKENATREDVKRACKFAAIDEFIESL 1342
Cdd:PRK11174  403 -----------QGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLL 471
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1343 PNQYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIkdKADKTIITIAHRIASIKR 1422
Cdd:PRK11174  472 PQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAA--SRRQTTLMVTHQLEDLAQ 549
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 156095386 1423 SDKIVVFNNpdrtGSFVQaQGTHEElLSVQDGVYK 1457
Cdd:PRK11174  550 WDQIWVMQD----GQIVQ-QGDYAE-LSQAGGLFA 578
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
1161-1450 2.13e-40

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: 158.76  E-value: 2.13e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1161 KGKIEIMDVNFRYlsrP--NVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfkneqtgesskeq 1238
Cdd:COG4618   328 KGRLSVENLTVVP---PgsKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLL-------------------------- 378
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1239 mqqgdeeqnVGMknanefssskegadgqsstLFKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENI-KFG 1317
Cdd:COG4618   379 ---------VGV-------------------WPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIaRFG 430
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1318 keNATREDVKRACKFAAIDEFIESLPNQYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEK 1397
Cdd:COG4618   431 --DADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAA 508
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 156095386 1398 TIVDIKdKADKTIITIAHRIASIKRSDKIVVFNNpdrtGSfVQAQGTHEELLS 1450
Cdd:COG4618   509 AIRALK-ARGATVVVITHRPSLLAAVDKLLVLRD----GR-VQAFGPRDEVLA 555
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
1166-1457 4.74e-40

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


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 157.95  E-value: 4.74e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1166 IMDVNFRYLSRP--NVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfkneqtgesskeqmqqgd 1243
Cdd:PRK10789  313 ELDVNIRQFTYPqtDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDV------------------------- 367
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 eeqnvgmknanefssskegadgqsstlfkNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKENATR 1323
Cdd:PRK10789  368 -----------------------------SEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDATQ 418
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1324 EDVKRACKFAAIDEFIESLPNQYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIK 1403
Cdd:PRK10789  419 QEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWG 498
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 156095386 1404 DKadKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQaQGTHEELLSvQDGVYK 1457
Cdd:PRK10789  499 EG--RTVIISAHRLSALTEASEILVMQH----GHIAQ-RGNHDQLAQ-QSGWYR 544
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
321-652 1.14e-39

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


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 156.80  E-value: 1.14e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  321 GGS--VI--SILLGVLIS--MFMLTIILP--------NITEymKSLEATNNLYEIINRKPLVEnnqDGKK-LKDIKKIQF 385
Cdd:PRK10789  241 GGSwmVVngSLTLGQLTSfvMYLGLMIWPmlalawmfNIVE--RGSAAYSRIRAMLAEAPVVK---DGSEpVPEGRGELD 315
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  386 KNVR-FHYDTrKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDsHNLKDVNLKWWRSKIGV 464
Cdd:PRK10789  316 VNIRqFTYPQ-TDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHD-IPLTKLQLDSWRSRLAV 393
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  465 VSQDPLLFSNSIKNNIkyslyslkdleALSEesnedgfssqsdsnsrnscrakcagdlndmiqtTDSTEliqvrknyETI 544
Cdd:PRK10789  394 VSQTPFLFSDTVANNI-----------ALGR---------------------------------PDATQ--------QEI 421
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  545 EDsevvsVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYlvqKTINN 624
Cdd:PRK10789  422 EH-----VARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEH---QILHN 493
                         330       340
                  ....*....|....*....|....*....
gi 156095386  625 LKG-NENRITIIIAHRLSTIRYANTIFVL 652
Cdd:PRK10789  494 LRQwGEGRTVIISAHRLSALTEASEILVM 522
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
1162-1459 1.78e-38

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


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 153.34  E-value: 1.78e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1162 GKIEIMDVNFRYlsRPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfkneqtgesskeqmqq 1241
Cdd:PRK10790  339 GRIDIDNVSFAY--RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPL----------------------- 393
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1242 gdeeqnvgmknanefssskegadgqsstlfkNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKeNA 1321
Cdd:PRK10790  394 -------------------------------TEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGR-DI 441
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1322 TREDVKRACKFAAIDEFIESLPNQYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVD 1401
Cdd:PRK10790  442 SEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAA 521
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 156095386 1402 IKDKAdkTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQaQGTHEELLSVQDGVYKKY 1459
Cdd:PRK10790  522 VREHT--TLVVIAHRLSTIVEADTILVLHR----GQAVE-QGTHQQLLAAQGRYWQMY 572
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
383-652 1.80e-38

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: 143.80  E-value: 1.80e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHYDTRKD-VEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIIN--DSHNLKDVNLKWWR 459
Cdd:cd03257     2 LEVKNLSVSFPTGGGsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDgkDLLKLSRRLRKIRR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  460 SKIGVVSQDPllfsnsiknnikyslyslkdlealseesnedgFSSqsdsnsrnscrakcagdLN------DMIqttdsTE 533
Cdd:cd03257    82 KEIQMVFQDP--------------------------------MSS-----------------LNprmtigEQI-----AE 107
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  534 LIQVRKNYETIEDSEVVSVSKKVLIHDfVSALPDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNK 613
Cdd:cd03257   108 PLRIHGKLSKKEARKEAVLLLLVGVGL-PEEVLNRY-------PHELSGGQRQRVAIARALALNPKLLIADEPTSALDVS 179
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 156095386  614 SEYLVQKTINNLKgNENRITII-IAHRLSTIRY-ANTIFVL 652
Cdd:cd03257   180 VQAQILDLLKKLQ-EELGLTLLfITHDLGVVAKiADRVAVM 219
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
1164-1431 4.90e-38

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: 142.70  E-value: 4.90e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYLSRPnvpIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDLKNDhhivfkneqtgesskeqmqqgd 1243
Cdd:cd03260     1 IELRDLNVYYGDKH---ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPG---------------------- 55
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 eeqnvgmknanefssskegadgqsstlFKNSGKILLDGVDIC--DYNLKDLRNLFSIVSQEPMLFNMSIYENIKFG---- 1317
Cdd:cd03260    56 ---------------------------APDEGEVLLDGKDIYdlDVDVLELRRRVGMVFQKPNPFPGSIYDNVAYGlrlh 108
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1318 ---KENATREDVKRACKFAAI-DEFIESLpnqydtnvgpYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEK 1393
Cdd:cd03260   109 gikLKEELDERVEEALRKAALwDEVKDRL----------HALGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTA 178
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 156095386 1394 LIEKTIVDIKDkaDKTIITIAHRIASIKR-SDKIVVFNN 1431
Cdd:cd03260   179 KIEELIAELKK--EYTIVIVTHNMQQAARvADRTAFLLN 215
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
401-608 4.67e-37

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: 137.01  E-value: 4.67e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   401 YKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDsHNLKDVNLKWWRSKIGVVSQDPLLFSN-SIKNN 479
Cdd:pfam00005    1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDG-QDLTDDERKSLRKEIGYVFQDPQLFPRlTVREN 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   480 IKYSLYslkdLEALSeesnedgfssqsdsnsrnscrakcagdlndmiQTTDSTELIQVRKNYetiedsevvsvskkvlih 559
Cdd:pfam00005   80 LRLGLL----LKGLS--------------------------------KREKDARAEEALEKL------------------ 105
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 156095386   560 dfvsALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATS 608
Cdd:pfam00005  106 ----GLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
1162-1428 3.87e-36

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: 136.39  E-value: 3.87e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1162 GKIEIMDVNFRYlsRPNVP-IYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDLKNdhhivfkneqtgesskeqmq 1240
Cdd:cd03369     5 GEIEVENLSVRY--APDLPpVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEE-------------------- 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1241 qgdeeqnvgmknanefssskegadgqsstlfknsGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENI-KFGKE 1319
Cdd:cd03369    63 ----------------------------------GKIEIDGIDISTIPLEDLRSSLTIIPQDPTLFSGTIRSNLdPFDEY 108
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1320 naTREDVKRACKfaaidefieslpnqydtnVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTI 1399
Cdd:cd03369   109 --SDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTI 168
                         250       260
                  ....*....|....*....|....*....
gi 156095386 1400 VdiKDKADKTIITIAHRIASIKRSDKIVV 1428
Cdd:cd03369   169 R--EEFTNSTILTIAHRLRTIIDYDKILV 195
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
1164-1450 4.05e-36

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: 137.08  E-value: 4.05e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYlsRPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFydLKNDhhivfkneqtgesskeqmqqgd 1243
Cdd:COG1122     1 IELENLSFSY--PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGL--LKPT---------------------- 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 eeqnvgmknanefssskegadgqsstlfknSGKILLDGVDICDYNLKDLRNLFSIVSQEP--MLFNMSIYENIKFGKENA 1321
Cdd:COG1122    55 ------------------------------SGEVLVDGKDITKKNLRELRRKVGLVFQNPddQLFAPTVEEDVAFGPENL 104
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1322 --TREDVKRACKfAAIDEF-IESLPNQYdtnvgPYgkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKT 1398
Cdd:COG1122   105 glPREEIRERVE-EALELVgLEHLADRP-----PH--ELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLEL 176
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 156095386 1399 IVDIKdKADKTIITIAHRIASI-KRSDKIVVFNNpdrtGSfVQAQGTHEELLS 1450
Cdd:COG1122   177 LKRLN-KEGKTVIIVTHDLDLVaELADRVIVLDD----GR-IVADGTPREVFS 223
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
383-654 4.17e-36

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: 137.08  E-value: 4.17e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHYDtrKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDsHNLKDVNLKWWRSKI 462
Cdd:COG1122     1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDG-KDITKKNLRELRRKV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  463 GVVSQDPL--LFSNSIKNNIKYSLYSLKdleaLSEEsnedgfssqsdsnsrnscrakcagdlndmiqttdsteliqvrkn 540
Cdd:COG1122    78 GLVFQNPDdqLFAPTVEEDVAFGPENLG----LPRE-------------------------------------------- 109
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  541 yetiedsEVVSVSKKVLihDFV--SALPDKyetlvgsNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLV 618
Cdd:COG1122   110 -------EIRERVEEAL--ELVglEHLADR-------PPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRREL 173
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 156095386  619 QKTINNLkgNENRITIIIA-HRLSTI-RYANTIFVLSN 654
Cdd:COG1122   174 LELLKRL--NKEGKTVIIVtHDLDLVaELADRVIVLDD 209
PLN03232 PLN03232
ABC transporter C family member; Provisional
206-1460 4.86e-36

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 149.74  E-value: 4.86e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  206 VFPLIYICGVICNKKVKINKKtSLLYNNNTMSIIEEALVGIRTVVSYCGENTILKKFNLSEKLYSKYTLKANLMESLHIG 285
Cdd:PLN03232  450 LFLLIPLQTLIVRKMRKLTKE-GLQWTDKRVGIINEILASMDTVKCYAWEKSFESRIQGIRNEELSWFRKAQLLSAFNSF 528
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  286 MINGFILASYAFGFwyGTRIIIS-DLSnqqPNNDFHGGSVISILLGVLismFMLTIILPNITEYMKSLEATNNLY----E 360
Cdd:PLN03232  529 ILNSIPVVVTLVSF--GVFVLLGgDLT---PARAFTSLSLFAVLRSPL---NMLPNLLSQVVNANVSLQRIEELLlseeR 600
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  361 IINRKPLVEnnqdgkklKDIKKIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILK-LIERLYDPTE 439
Cdd:PLN03232  601 ILAQNPPLQ--------PGAPAISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAET 672
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  440 GDVIIndshnlkdvnlkwwRSKIGVVSQDPLLFSNSIKNNIKYSlyslkdlealseesnedgfssqSDSNSRNSCRAkca 519
Cdd:PLN03232  673 SSVVI--------------RGSVAYVPQVSWIFNATVRENILFG----------------------SDFESERYWRA--- 713
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  520 gdlndmiqtTDSTeliqvrknyetiedsevvsvskkVLIHDfVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPK 599
Cdd:PLN03232  714 ---------IDVT-----------------------ALQHD-LDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSD 760
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  600 ILILDEATSSLDNKSEYLVQKTI--NNLKGnenRITIIIAHRLSTIRYANTIFVLSN---RENGSTVDVDVLGEdPTKDS 674
Cdd:PLN03232  761 IYIFDDPLSALDAHVAHQVFDSCmkDELKG---KTRVLVTNQLHFLPLMDRIILVSEgmiKEEGTFAELSKSGS-LFKKL 836
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  675 NEKNEKHDKQEKGGKNSSANQKIGNAGSYIIEQGTHDALMKNKNGiyytminnqkvssksssnndndkdsdmKSSIYKDS 754
Cdd:PLN03232  837 MENAGKMDATQEVNTNDENILKLGPTVTIDVSERNLGSTKQGKRG---------------------------RSVLVKQE 889
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  755 ERgydpdeangnaknesasakksekmsdakasntnAGGRLAFlrNLFKRKPKAPNNLRVVYREIFSYKkdiaiialsimv 834
Cdd:PLN03232  890 ER---------------------------------ETGIISW--NVLMRYNKAVGGLWVVMILLVCYL------------ 922
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  835 aggLYPLFALLYAKYVGTLFDFANLEANSNKYslYILVIAIAMF--ISETLKNYYNnVIGEKVEKTMKLR--LFENIMYQ 910
Cdd:PLN03232  923 ---TTEVLRVSSSTWLSIWTDQSTPKSYSPGF--YIVVYALLGFgqVAVTFTNSFW-LISSSLHAAKRLHdaMLNSILRA 996
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  911 EISFFDqdSHAPGLLSAHINRDVHLLKTGLVNNIVIFTH--------FIVLFLVSTVMSFYFCPIVAaVLTGTYFIFMrv 982
Cdd:PLN03232  997 PMLFFH--TNPTGRVINRFSKDIGDIDRNVANLMNMFMNqlwqllstFALIGTVSTISLWAIMPLLI-LFYAAYLYYQ-- 1071
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  983 fairariaaNKDVEKKRVnqpgtafvynsdDEIFKDPSF-LIQEAFYNMNTVIIYGLEDYFCTLIEKAID---------- 1051
Cdd:PLN03232 1072 ---------STSREVRRL------------DSVTRSPIYaQFGEALNGLSSIRAYKAYDRMAKINGKSMDnnirftlant 1130
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1052 YSNK--GQKRKTLINSMLWgfsqsaqfFINSFAywfgsfLIRRGTIQVDDFMKSLFTFLFtgSYAGKLMSL-------KG 1122
Cdd:PLN03232 1131 SSNRwlTIRLETLGGVMIW--------LTATFA------VLRNGNAENQAGFASTMGLLL--SYTLNITTLlsgvlrqAS 1194
                         970       980       990      1000      1010      1020      1030      1040
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1123 DSENAKLSFERYyplitrKSLIDVRDNGGIKIKNSNDI-----KGKIEIMDVNFRYlsRPNVP-IYKDLTFSCESKKTTA 1196
Cdd:PLN03232 1195 KAENSLNSVERV------GNYIDLPSEATAIIENNRPVsgwpsRGSIKFEDVHLRY--RPGLPpVLHGLSFFVSPSEKVG 1266
                        1050      1060      1070      1080      1090      1100      1110      1120
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1197 IVGETGSGKSTVMSLLMRFYDLKNdhhivfkneqtgesskeqmqqgdeeqnvgmknanefssskegadgqsstlfknsGK 1276
Cdd:PLN03232 1267 VVGRTGAGKSSMLNALFRIVELEK------------------------------------------------------GR 1292
                        1130      1140      1150      1160      1170      1180      1190      1200
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1277 ILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIK-FGKENATreDVKRACKFAAIDEFIESLPNQYDTNVGPYGK 1355
Cdd:PLN03232 1293 IMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDpFSEHNDA--DLWEALERAHIKDVIDRNPFGLDAEVSEGGE 1370
                        1210      1220      1230      1240      1250      1260      1270      1280
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1356 SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDikDKADKTIITIAHRIASIKRSDKIVVFNNPDrt 1435
Cdd:PLN03232 1371 NFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIRE--EFKSCTMLVIAHRLNTIIDCDKILVLSSGQ-- 1446
                        1290      1300
                  ....*....|....*....|....*
gi 156095386 1436 gsfVQAQGTHEELLSVQDGVYKKYV 1460
Cdd:PLN03232 1447 ---VLEYDSPQELLSRDTSAFFRMV 1468
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
383-656 1.12e-35

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 134.94  E-value: 1.12e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHYDTRKdveIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDShNLKDVNLKWWRSKI 462
Cdd:COG4619     1 LELEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGK-PLSAMPPPEWRRQV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  463 GVVSQDPLLFSNSIKNNIKYSlYSLKDLealseesnedgfssqsdsnsrnscrakcagdlndmiqttdsteliqvRKNYE 542
Cdd:COG4619    77 AYVPQEPALWGGTVRDNLPFP-FQLRER-----------------------------------------------KFDRE 108
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  543 TIEDsevvsvskkvLIHDFvsALPDKYetlVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI 622
Cdd:COG4619   109 RALE----------LLERL--GLPPDI---LDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRVEELL 173
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 156095386  623 NNLKGNENRITIIIAHRLSTI-RYANTIFVLSNRE 656
Cdd:COG4619   174 REYLAEEGRAVLWVSHDPEQIeRVADRVLTLEAGR 208
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
383-663 1.48e-35

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: 143.12  E-value: 1.48e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHYDTRK--DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIIN--DSHNLKDVNLKWW 458
Cdd:COG1123   261 LEVRNLSKRYPVRGkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDgkDLTKLSRRSLREL 340
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  459 RSKIGVVSQDPL--LF-SNSIKNNIKYSLYSLKDLealseesnedgfssqsdsnSRNSCRAKCAgdlndmiqttdstELI 535
Cdd:COG1123   341 RRRVQMVFQDPYssLNpRMTVGDIIAEPLRLHGLL-------------------SRAERRERVA-------------ELL 388
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  536 -QVRknyetiedsevvsvskkvLIHDFVSALPdkYEtlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDnks 614
Cdd:COG1123   389 eRVG------------------LPPDLADRYP--HE---------LSGGQRQRVAIARALALEPKLLILDEPTSALD--- 436
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 156095386  615 eYLVQKTI-NNLKG--NENRITII-IAHRLSTIRY-ANTIFVLSN-R--ENGSTVDV 663
Cdd:COG1123   437 -VSVQAQIlNLLRDlqRELGLTYLfISHDLAVVRYiADRVAVMYDgRivEDGPTEEV 492
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
100-727 4.21e-35

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: 144.50  E-value: 4.21e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   100 IFSLVLIG--IFQFILSFISSFCMDVVTTKILKTLKIEFLKSVFYQDGQFHDNNPGSKLTSDLDFYLEQVNAgIGTKFIT 177
Cdd:TIGR01193  197 IISIGLIIayIIQQILSYIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGEIVSRFTDASSIIDA-LASTILS 275
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   178 IFTYASAFLGLYIWSLFKNARLTLCITCVFPlIYICGVICNKKV--KINKKTslLYNNNTM-SIIEEALVGIRTVVSYCG 254
Cdd:TIGR01193  276 LFLDMWILVIVGLFLVRQNMLLFLLSLLSIP-VYAVIIILFKRTfnKLNHDA--MQANAVLnSSIIEDLNGIETIKSLTS 352
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   255 ENTILKKFNLSEKLYSKYTLKANLMESLHIGMINGFILASYAFGFWYGTRIIISdlsnqqpnNDFHGGSVISilLGVLIS 334
Cdd:TIGR01193  353 EAERYSKIDSEFGDYLNKSFKYQKADQGQQAIKAVTKLILNVVILWTGAYLVMR--------GKLTLGQLIT--FNALLS 422
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   335 MFmlTIILPNITEYMKSLEATNNLYEIINRKPLVENNQDGKKLKDIKK-----IQFKNVRFHYDTRKdvEIYKDLNFTLT 409
Cdd:TIGR01193  423 YF--LTPLENIINLQPKLQAARVANNRLNEVYLVDSEFINKKKRTELNnlngdIVINDVSYSYGYGS--NILSDISLTIK 498
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   410 EGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINdSHNLKDVNLKWWRSKIGVVSQDPLLFSNSIKNNIkyslyslkd 489
Cdd:TIGR01193  499 MNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLN-GFSLKDIDRHTLRQFINYLPQEPYIFSGSILENL--------- 568
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   490 lealseesnedgfssqsdsnsrnscrakcagdlndmiqttdsteLIQVRKNYETIEDSEVVSVSKkvlIHDFVSALPDKY 569
Cdd:TIGR01193  569 --------------------------------------------LLGAKENVSQDEIWAACEIAE---IKDDIENMPLGY 601
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   570 ETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEylvQKTINNLKGNENRITIIIAHRLSTIRYANTI 649
Cdd:TIGR01193  602 QTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITE---KKIVNNLLNLQDKTIIFVAHRLSVAKQSDKI 678
                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156095386   650 FVLSNrengstvdvdvlgedptkdsneknekhdkqekgGKnssanqkignagsyIIEQGTHDALMkNKNGIYYTMINN 727
Cdd:TIGR01193  679 IVLDH---------------------------------GK--------------IIEQGSHDELL-DRNGFYASLIHN 708
NHLM_micro_ABC2 TIGR03797
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ...
382-654 4.66e-35

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: 144.33  E-value: 4.66e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   382 KIQFKNVRFHYdtRKD-VEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGdVIINDSHNLKDVNLKWWRS 460
Cdd:TIGR03797  451 AIEVDRVTFRY--RPDgPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESG-SVFYDGQDLAGLDVQAVRR 527
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   461 KIGVVSQDPLLFSNSIKNNIKYS-LYSLKD-LEALSeesnedgfssqsdsnsrnscRAKCAGDLNDMiqttdsteliqvr 538
Cdd:TIGR03797  528 QLGVVLQNGRLMSGSIFENIAGGaPLTLDEaWEAAR--------------------MAGLAEDIRAM------------- 574
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   539 knyetiedsevvsvskkvlihdfvsalPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLV 618
Cdd:TIGR03797  575 ---------------------------PMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIV 627
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 156095386   619 QKTINNLKGNEnritIIIAHRLSTIRYANTIFVLSN 654
Cdd:TIGR03797  628 SESLERLKVTR----IVIAHRLSTIRNADRIYVLDA 659
type_I_sec_PrtD TIGR01842
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ...
1177-1450 4.89e-35

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: 142.10  E-value: 4.89e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1177 PNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfkneqtgesskeqmqqgdeeqnVGMknanef 1256
Cdd:TIGR01842  329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLI-----------------------------------VGI------ 367
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1257 ssskegadgQSSTlfknSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENI-KFGkENATREDVKRACKFAAI 1335
Cdd:TIGR01842  368 ---------WPPT----SGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENIaRFG-ENADPEKIIEAAKLAGV 433
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1336 DEFIESLPNQYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKdKADKTIITIAH 1415
Cdd:TIGR01842  434 HELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALK-ARGITVVVITH 512
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 156095386  1416 RIASIKRSDKIVVFNNpdrtGSfVQAQGTHEELLS 1450
Cdd:TIGR01842  513 RPSLLGCVDKILVLQD----GR-IARFGERDEVLA 542
ABC_6TM_Pgp_ABCB1_D1_like cd18577
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ...
825-1118 5.24e-35

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: 136.07  E-value: 5.24e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  825 IAIIALSIMVAGGLYPLFALLYAKYVGTLFDFANLEANS-------NKYSLYILVIAIAMFISETLKNYYNNVIGEKVEK 897
Cdd:cd18577     1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFTDFGSGESSPdeflddvNKYALYFVYLGIGSFVLSYIQTACWTITGERQAR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  898 TMKLRLFENIMYQEISFFDQdsHAPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSTVMSFYFCPIVAAVLTGTY- 976
Cdd:cd18577    81 RIRKRYLKALLRQDIAWFDK--NGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLp 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  977 --FIFMRVFAIRARIAANKdvEKKRVNQPGTafvynsddeifkdpsfLIQEAFYNMNTVIIYGLEDYFCTLIEKAIDYSN 1054
Cdd:cd18577   159 liAIVGGIMGKLLSKYTKK--EQEAYAKAGS----------------IAEEALSSIRTVKAFGGEEKEIKRYSKALEKAR 220
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156095386 1055 KGQKRKTLINSMLWGFSQSAQFFINSFAYWFGSFLIRRGTIQVDDFMKSLFTFLFTGSYAGKLM 1118
Cdd:cd18577   221 KAGIKKGLVSGLGLGLLFFIIFAMYALAFWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIA 284
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
1164-1431 1.12e-34

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: 130.80  E-value: 1.12e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYLSRPNvPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfkneqtgesskeqmqqgd 1243
Cdd:cd03246     1 LEVENVSFRYPGAEP-PVLRNVSFSIEPGESLAIIGPSGSGKSTLARLI------------------------------- 48
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 eeqnVGMknanefssskegadgqsstLFKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIkfgkenatr 1323
Cdd:cd03246    49 ----LGL-------------------LRPTSGRVRLDGADISQWDPNELGDHVGYLPQDDELFSGSIAENI--------- 96
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1324 edvkrackfaaidefieslpnqydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIK 1403
Cdd:cd03246    97 ---------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALK 143
                         250       260
                  ....*....|....*....|....*...
gi 156095386 1404 dKADKTIITIAHRIASIKRSDKIVVFNN 1431
Cdd:cd03246   144 -AAGATRIVIAHRPETLASADRILVLED 170
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
1165-1431 1.17e-34

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: 132.21  E-value: 1.17e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1165 EIMDVNFRYlSRPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFydlkndhhivfkneqtgesskeqmqqgde 1244
Cdd:cd03225     1 ELKNLSFSY-PDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGL----------------------------- 50
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1245 eqnvgmknanefssskegadgqsstLFKNSGKILLDGVDICDYNLKDLRNLFSIVSQEP--MLFNMSIYENIKFGKENA- 1321
Cdd:cd03225    51 -------------------------LGPTSGEVLVDGKDLTKLSLKELRRKVGLVFQNPddQFFGPTVEEEVAFGLENLg 105
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1322 -TREDVKRACKFAAIDEFIESLPNQYdtnvgPYgkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIV 1400
Cdd:cd03225   106 lPEEEIEERVEEALELVGLEGLRDRS-----PF--TLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLK 178
                         250       260       270
                  ....*....|....*....|....*....|..
gi 156095386 1401 DIKDKaDKTIITIAHRIASIKR-SDKIVVFNN 1431
Cdd:cd03225   179 KLKAE-GKTIIIVTHDLDLLLElADRVIVLED 209
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
1164-1428 8.02e-34

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: 130.32  E-value: 8.02e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYLSRPN-VPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFydlkndhhivfkneqtgesskeqmqqg 1242
Cdd:cd03257     2 LEVKNLSVSFPTGGGsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGL--------------------------- 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1243 deeqnvgmknanefssskegadgqsstLFKNSGKILLDGVDICDYN---LKDLRNLFSIVSQEPML-FN--MSIYENIKF 1316
Cdd:cd03257    55 ---------------------------LKPTSGSIIFDGKDLLKLSrrlRKIRRKEIQMVFQDPMSsLNprMTIGEQIAE 107
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1317 GKENATREDVKRACKFAAI---------DEFIESLPNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSL 1387
Cdd:cd03257   108 PLRIHGKLSKKEARKEAVLlllvgvglpEEVLNRYPHE-----------LSGGQRQRVAIARALALNPKLLIADEPTSAL 176
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 156095386 1388 DSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVV 1428
Cdd:cd03257   177 DVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKiADRVAV 218
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
384-654 2.58e-33

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: 128.35  E-value: 2.58e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  384 QFKNVRFHYDtRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDShNLKDVNLKWWRSKIG 463
Cdd:cd03225     1 ELKNLSFSYP-DGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGK-DLTKLSLKELRRKVG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  464 VVSQDP--LLFSNSIKNNIKYSLyslkdlealseesnedgfssqsdsnsRNSCRAKcagdlndmiqttdstELIQVRkny 541
Cdd:cd03225    79 LVFQNPddQFFGPTVEEEVAFGL--------------------------ENLGLPE---------------EEIEER--- 114
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  542 etiedseVVSVSKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKT 621
Cdd:cd03225   115 -------VEEALELVGLEGLRDRSP-----------FTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLEL 176
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 156095386  622 INNLKgnENRITIIIA-HRLSTIR-YANTIFVLSN 654
Cdd:cd03225   177 LKKLK--AEGKTIIIVtHDLDLLLeLADRVIVLED 209
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
1164-1431 2.72e-33

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 128.40  E-value: 2.72e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYLSRPnvpIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfkneqtgesskeqmqqgd 1243
Cdd:COG4619     1 LELEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPP------------------------- 52
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 eeqnvgmknanefssskegadgqsstlfkNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFG----KE 1319
Cdd:COG4619    53 -----------------------------TSGEIYLDGKPLSAMPPPEWRRQVAYVPQEPALWGGTVRDNLPFPfqlrER 103
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1320 NATREDVKRAckFAAIDefiesLPNQY-DTNVgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKT 1398
Cdd:COG4619   104 KFDRERALEL--LERLG-----LPPDIlDKPV----ERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRVEEL 172
                         250       260       270
                  ....*....|....*....|....*....|....
gi 156095386 1399 IVDIKDKADKTIITIAHRIASIKR-SDKIVVFNN 1431
Cdd:COG4619   173 LREYLAEEGRAVLWVSHDPEQIERvADRVLTLEA 206
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
383-637 6.52e-33

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: 127.68  E-value: 6.52e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHYDtrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYD-----PTEGDVIINDSH-NLKDVNLK 456
Cdd:cd03260     1 IELRDLNVYYG---DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDiYDLDVDVL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  457 WWRSKIGVVSQDPLLFSNSIKNNIKYSLyslkdleALSEESNEDGFssqsdsnsrnscrakcagdlndmiqttdsteliq 536
Cdd:cd03260    78 ELRRRVGMVFQKPNPFPGSIYDNVAYGL-------RLHGIKLKEEL---------------------------------- 116
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  537 vrknyetieDSEVVSVSKKVLIHDFVSalpDKyetlvgSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEY 616
Cdd:cd03260   117 ---------DERVEEALRKAALWDEVK---DR------LHALGLSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTA 178
                         250       260
                  ....*....|....*....|.
gi 156095386  617 LVQKTINNLKgneNRITIIIA 637
Cdd:cd03260   179 KIEELIAELK---KEYTIVIV 196
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
1164-1431 1.06e-32

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: 126.43  E-value: 1.06e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYLSRPNVPIY--KDLTFSCESKKTTAIVGETGSGKSTVMSLLMrfydlkndhhivfkneqtGEsskeqmqq 1241
Cdd:cd03250     1 ISVEDASFTWDSGEQETSFtlKDINLEVPKGELVAIVGPVGSGKSSLLSALL------------------GE-------- 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1242 gdeeqnvgmknanefssskegadgqsstLFKNSGKILLDGVdicdynlkdlrnlFSIVSQEPMLFNMSIYENIKFGKE-N 1320
Cdd:cd03250    55 ----------------------------LEKLSGSVSVPGS-------------IAYVSQEPWIQNGTIRENILFGKPfD 93
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1321 ATR-EDVKRACkfaAIDEFIESLPNQYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSN-SEKLIEKT 1398
Cdd:cd03250    94 EERyEKVIKAC---ALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHvGRHIFENC 170
                         250       260       270
                  ....*....|....*....|....*....|...
gi 156095386 1399 IVDIKdKADKTIITIAHRIASIKRSDKIVVFNN 1431
Cdd:cd03250   171 ILGLL-LNNKTRILVTHQLQLLPHADQIVVLDN 202
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
402-654 2.41e-32

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: 134.11  E-value: 2.41e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  402 KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIInDSHNLKDvnlkWWRSK----IGVVSQDPLLFSNSIK 477
Cdd:COG4618   349 RGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRL-DGADLSQ----WDREElgrhIGYLPQDVELFDGTIA 423
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  478 NNIkyslyslkdlealseesnedgfssqsdsnsrnsCRakcagdlndmiqttdsteliqvrknYETIEDSEVVSVSKKVL 557
Cdd:COG4618   424 ENI---------------------------------AR-------------------------FGDADPEKVVAAAKLAG 445
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  558 IHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgNENRITIIIA 637
Cdd:COG4618   446 VHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALK-ARGATVVVIT 524
                         250
                  ....*....|....*..
gi 156095386  638 HRLSTIRYANTIFVLSN 654
Cdd:COG4618   525 HRPSLLAAVDKLLVLRD 541
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
337-1463 2.45e-32

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: 137.77  E-value: 2.45e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   337 MLTIILPNITEYMKSLEatnNLYEIINRKPLVENNQDGKKLKD--IKKIQFKNVRFHYdTRKDVEIYKDLNFTLTEGKTY 414
Cdd:TIGR00957  592 ILPMVISSIVQASVSLK---RLRIFLSHEELEPDSIERRTIKPgeGNSITVHNATFTW-ARDLPPTLNGITFSIPEGALV 667
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   415 AFVGESGCGKSTILKLIERLYDPTEGDVIINDShnlkdvnlkwwrskIGVVSQDPLLFSNSIKNNIKyslyslkdleals 494
Cdd:TIGR00957  668 AVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS--------------VAYVPQQAWIQNDSLRENIL------------- 720
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   495 eesnedgFSSQSDSNSRNSCRAKCAgdlndmiqttdsteliqvrknyeTIEDSEVvsvskkvlihdfvsaLPDKYETLVG 574
Cdd:TIGR00957  721 -------FGKALNEKYYQQVLEACA-----------------------LLPDLEI---------------LPSGDRTEIG 755
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   575 SNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNK-SEYLVQKTINNLKGNENRITIIIAHRLSTIRYANTIFVLS 653
Cdd:TIGR00957  756 EKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHvGKHIFEHVIGPEGVLKNKTRILVTHGISYLPQVDVIIVMS 835
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   654 nrengstvdvdvlgedptkdsneknekhdkqekGGKnssanqkignagsyIIEQGTHDALMKnKNGIYYTMInnqkvssk 733
Cdd:TIGR00957  836 ---------------------------------GGK--------------ISEMGSYQELLQ-RDGAFAEFL-------- 859
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   734 sssnndndkdsdmkssiykdseRGYDPDEANGNAKN-----ESASAKKSEKMSDAKASNTNAGGRlaFLRNL-------- 800
Cdd:TIGR00957  860 ----------------------RTYAPDEQQGHLEDswtalVSGEGKEAKLIENGMLVTDVVGKQ--LQRQLsasssdsg 915
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   801 -FKRKPKAPNNLRVV------YREIFSYKKDIAIIALSI----MVAGGLYPLFA--LLY---------AKYVGTLFD--- 855
Cdd:TIGR00957  916 dQSRHHGSSAELQKAeakeetWKLMEADKAQTGQVELSVywdyMKAIGLFITFLsiFLFvcnhvsalaSNYWLSLWTddp 995
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   856 FAN-LEANSN-KYSLY--------ILVIAIAMFISetlknyynnVIGEKVEKTMKLRLFENIMYQEISFFDQDShaPGLL 925
Cdd:TIGR00957  996 MVNgTQNNTSlRLSVYgalgilqgFAVFGYSMAVS---------IGGIQASRVLHQDLLHNKLRSPMSFFERTP--SGNL 1064
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   926 SAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSTVMSFYFCPIVAAV---LTGTYFIFMRVFAIRARiaankdvEKKRVNQ 1002
Cdd:TIGR00957 1065 VNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVIippLGLLYFFVQRFYVASSR-------QLKRLES 1137
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1003 PGTAFVYNSddeifkdpsflIQEAFYNMNTVIIYGLEDYFCTLIEKAIDYSNKGQKRKTLINSMLwgfSQSAQFFINS-- 1080
Cdd:TIGR00957 1138 VSRSPVYSH-----------FNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWL---AVRLECVGNCiv 1203
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1081 -FAYWFGsfLIRRGTIQVDDFMKSLFTFLFTGSYAGKLMSLKGDSENAKLSFERY--YPLITRKSLIDVRdngGIKIKNS 1157
Cdd:TIGR00957 1204 lFAALFA--VISRHSLSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLkeYSETEKEAPWQIQ---ETAPPSG 1278
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1158 NDIKGKIEIMDVNFRYlsRPNVP-IYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFydlkndhhivfkneqtGESSK 1236
Cdd:TIGR00957 1279 WPPRGRVEFRNYCLRY--REDLDlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRI----------------NESAE 1340
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1237 eqmqqgdeeqnvgmknanefssskegadgqsstlfknsGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIK- 1315
Cdd:TIGR00957 1341 --------------------------------------GEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLDp 1382
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1316 FGKenATREDVKRACKFAAIDEFIESLPNQYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLI 1395
Cdd:TIGR00957 1383 FSQ--YSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLI 1460
                         1130      1140      1150      1160      1170      1180
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156095386  1396 EKTIVDIKDkaDKTIITIAHRIASIKRSDKIVVFNNPDrtgsfVQAQGTHEELLSvQDGVYKKYVKLA 1463
Cdd:TIGR00957 1461 QSTIRTQFE--DCTVLTIAHRLNTIMDYTRVIVLDKGE-----VAEFGAPSNLLQ-QRGIFYSMAKDA 1520
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
1164-1416 4.24e-32

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: 132.87  E-value: 4.24e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1164 IEIMDVNFRYlsRPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfkneqtgesskeqmqqgd 1243
Cdd:TIGR02868  335 LELRDLSAGY--PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLD-------------------------- 386
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1244 eeqnvgmknanefssskegadgqsstlfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKENATR 1323
Cdd:TIGR02868  387 ----------------------------PLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATD 438
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1324 EDVKRACKFAAIDEFIESLPNQYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIK 1403
Cdd:TIGR02868  439 EELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAAL 518
                          250
                   ....*....|...
gi 156095386  1404 DKadKTIITIAHR 1416
Cdd:TIGR02868  519 SG--RTVVLITHH 529
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
1182-1385 5.31e-32

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: 122.37  E-value: 5.31e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1182 YKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYdlkndhhivfkneqtgesskeqmqQGDEeqnvgmknanefssske 1261
Cdd:pfam00005    1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLL------------------------SPTE----------------- 39
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1262 gadgqsstlfknsGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFN-MSIYENIKFGKENATREDVKRACKFAAIDEFIe 1340
Cdd:pfam00005   40 -------------GTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPrLTVRENLRLGLLLKGLSKREKDARAEEALEKL- 105
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 156095386  1341 SLPNQYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATS 1385
Cdd:pfam00005  106 GLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
404-654 1.03e-31

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 132.66  E-value: 1.03e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  404 LNFTLTEGKTYAFVGESGCGKSTILKLIerL-YDPTEGDVIINDsHNLKDVNLKWWRSKIGVVSQDPLLFSNSIKNNIky 482
Cdd:PRK11174  369 LNFTLPAGQRIALVGPSGAGKTSLLNAL--LgFLPYQGSLKING-IELRELDPESWRKHLSWVGQNPQLPHGTLRDNV-- 443
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  483 slyslkdleALSEESnedgfssqsdsnsrnscrakcagdlndmiqttdsteliqvrknyetIEDSEVVSVSKKVLIHDFV 562
Cdd:PRK11174  444 ---------LLGNPD----------------------------------------------ASDEQLQQALENAWVSEFL 468
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  563 SALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLST 642
Cdd:PRK11174  469 PLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAAS--RRQTTLMVTHQLED 546
                         250
                  ....*....|..
gi 156095386  643 IRYANTIFVLSN 654
Cdd:PRK11174  547 LAQWDQIWVMQD 558
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
383-654 1.70e-31

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: 121.94  E-value: 1.70e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHYDTRKDvEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIInDSHNLKDVNLKWWRSKI 462
Cdd:cd03246     1 LEVENVSFRYPGAEP-PVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRL-DGADISQWDPNELGDHV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  463 GVVSQDPLLFSNSIKNNIkyslyslkdlealseesnedgfssqsdsnsrnscrakcagdlndmiqttdsteliqvrknye 542
Cdd:cd03246    79 GYLPQDDELFSGSIAENI-------------------------------------------------------------- 96
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  543 tiedsevvsvskkvlihdfvsalpdkyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI 622
Cdd:cd03246    97 -------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAI 139
                         250       260       270
                  ....*....|....*....|....*....|..
gi 156095386  623 NNLKGnENRITIIIAHRLSTIRYANTIFVLSN 654
Cdd:cd03246   140 AALKA-AGATRIVIAHRPETLASADRILVLED 170
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
1164-1431 1.79e-31

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: 122.04  E-value: 1.79e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYLSRpNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRfyDLKndhhivfkneqtgesskeqmqqgd 1243
Cdd:cd03247     1 LSINNVSFSYPEQ-EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTG--DLK------------------------ 53
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 eeqnvgmknanefssskegadgqsstlfKNSGKILLDGVDICDYNlKDLRNLFSIVSQEPMLFNMSIYENIkfgkenatr 1323
Cdd:cd03247    54 ----------------------------PQQGEITLDGVPVSDLE-KALSSLISVLNQRPYLFDTTLRNNL--------- 95
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1324 edvkrackfaaidefieslpnqydtnvgpyGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIK 1403
Cdd:cd03247    96 ------------------------------GRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVL 145
                         250       260
                  ....*....|....*....|....*...
gi 156095386 1404 DkaDKTIITIAHRIASIKRSDKIVVFNN 1431
Cdd:cd03247   146 K--DKTLIWITHHLTGIEHMDKILFLEN 171
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
320-640 5.83e-31

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: 129.40  E-value: 5.83e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   320 HGGSVISILLGVLISMFMLTIILPN----ITEYMKSLEATNNLYEIINRKPLVENNQDGKKLKDIKKIQFKNVRFHYDTr 395
Cdd:TIGR02868  268 LAPVTLAVLVLLPLAAFEAFAALPAaaqqLTRVRAAAERIVEVLDAAGPVAEGSAPAAGAVGLGKPTLELRDLSAGYPG- 346
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   396 kDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDSHnLKDVNLKWWRSKIGVVSQDPLLFSNS 475
Cdd:TIGR02868  347 -APPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVP-VSSLDQDEVRRRVSVCAQDAHLFDTT 424
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   476 IKNNIkyslyslkdlealseesnedgfssqsdsnsrnscrakcagdlndMIQTTDSTeliqvrknyetieDSEVVSVSKK 555
Cdd:TIGR02868  425 VRENL--------------------------------------------RLARPDAT-------------DEELWAALER 447
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   556 VLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTInnLKGNENRITII 635
Cdd:TIGR02868  448 VGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDL--LAALSGRTVVL 525

                   ....*
gi 156095386   636 IAHRL 640
Cdd:TIGR02868  526 ITHHL 530
ECF_ATPase_1 TIGR04520
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
1164-1450 9.47e-31

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: 122.92  E-value: 9.47e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1164 IEIMDVNFRYlsrPN--VPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfkneqtgesskeqmqq 1241
Cdd:TIGR04520    1 IEVENVSFSY---PEseKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLL----------------------------- 48
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1242 gdeeqnvgmknanefssskegaDGQsstLFKNSGKILLDGVDICD-YNLKDLRNLFSIVSQEP--MLFNMSIYENIKFGK 1318
Cdd:TIGR04520   49 ----------------------NGL---LLPTSGKVTVDGLDTLDeENLWEIRKKVGMVFQNPdnQFVGATVEDDVAFGL 103
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1319 ENA------TREDVKRACKFAAIDEFIESLPNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSE 1392
Cdd:TIGR04520  104 ENLgvpreeMRKRVDEALKLVGMEDFRDREPHL-----------LSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGR 172
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 156095386  1393 KLIEKTIVDIKDKADKTIITIAHRIASIKRSDKIVVFNNpdrtGSfVQAQGTHEELLS 1450
Cdd:TIGR04520  173 KEVLETIRKLNKEEGITVISITHDMEEAVLADRVIVMNK----GK-IVAEGTPREIFS 225
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
1155-1431 1.11e-30

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


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 122.45  E-value: 1.11e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1155 KNSNDIKGKIEIMDVNFRYLSRPNVpiyKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDLKNDHHIvfkneqtges 1234
Cdd:COG1117     3 APASTLEPKIEVRNLNVYYGDKQAL---KDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIPGARV---------- 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1235 skeqmqqgdeeqnvgmknanefssskegadgqsstlfknSGKILLDGVDI--CDYNLKDLRNLFSIVSQEPMLFNMSIYE 1312
Cdd:COG1117    70 ---------------------------------------EGEILLDGEDIydPDVDVVELRRRVGMVFQKPNPFPKSIYD 110
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1313 NIKFG-KENATR------EDVKRACKFAAI-DEFIESLpnqyDTNvgpyGKSLSGGQKQRIAIARALLREPKILLLDEAT 1384
Cdd:COG1117   111 NVAYGlRLHGIKskseldEIVEESLRKAALwDEVKDRL----KKS----ALGLSGGQQQRLCIARALAVEPEVLLMDEPT 182
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 156095386 1385 SSLDSNSEKLIEKTIVDIKDkaDKTIITIAHRIASIKR-SDKIVVFNN 1431
Cdd:COG1117   183 SALDPISTAKIEELILELKK--DYTIVIVTHNMQQAARvSDYTAFFYL 228
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
383-654 3.03e-30

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 120.55  E-value: 3.03e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHYdtrKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDsHNLKDvNLKWWRSKI 462
Cdd:COG1131     1 IEVRGLTKRY---GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLG-EDVAR-DPAEVRRRI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  463 GVVSQDPLLFSN-SIKNNIKY--SLYSLKDLEAlseesnedgfssqsdsnsrnscRAKCAgdlndmiqttdstELIqvrk 539
Cdd:COG1131    76 GYVPQEPALYPDlTVRENLRFfaRLYGLPRKEA----------------------RERID-------------ELL---- 116
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  540 nyetiedsevvsvskkvlihDFVSaLPDKYETLVGsnasKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQ 619
Cdd:COG1131   117 --------------------ELFG-LTDAADRKVG----TLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELW 171
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 156095386  620 KTINNLKgnENRITIIIA-HRLSTI-RYANTIFVLSN 654
Cdd:COG1131   172 ELLRELA--AEGKTVLLStHYLEEAeRLCDRVAIIDK 206
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
1164-1450 3.11e-30

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: 126.94  E-value: 3.11e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYLSRPN--VPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfkneqtgesskeqmqq 1241
Cdd:COG1123   261 LEVRNLSKRYPVRGKggVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRP----------------------- 317
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1242 gdeeqnvgmknanefssskegadgqsstlfkNSGKILLDGVDICDYNLKDLRNL---FSIVSQEPML-FN--MSIYENIK 1315
Cdd:COG1123   318 -------------------------------TSGSILFDGKDLTKLSRRSLRELrrrVQMVFQDPYSsLNprMTVGDIIA 366
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1316 FG-------KENATREDVKRACKFAAID-EFIESLPNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSL 1387
Cdd:COG1123   367 EPlrlhgllSRAERRERVAELLERVGLPpDLADRYPHE-----------LSGGQRQRVAIARALALEPKLLILDEPTSAL 435
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156095386 1388 DSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVVFNNpdrtGSFVqAQGTHEELLS 1450
Cdd:COG1123   436 DVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYiADRVAVMYD----GRIV-EDGPTEEVFA 494
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
1164-1432 3.15e-30

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: 118.44  E-value: 3.15e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYlsrPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFydlkndhhivfkneqtgesskeqmqqgd 1243
Cdd:cd03229     1 LELKNVSKRY---GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGL---------------------------- 49
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 EEqnvgmknanefssskegadgqsstlfKNSGKILLDGVDICDYN--LKDLRNLFSIVSQEPMLF-NMSIYENIKFGken 1320
Cdd:cd03229    50 EE--------------------------PDSGSILIDGEDLTDLEdeLPPLRRRIGMVFQDFALFpHLTVLENIALG--- 100
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1321 atredvkrackfaaidefieslpnqydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIV 1400
Cdd:cd03229   101 ------------------------------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLK 144
                         250       260       270
                  ....*....|....*....|....*....|...
gi 156095386 1401 DIKDKADKTIITIAHRIASIKR-SDKIVVFNNP 1432
Cdd:cd03229   145 SLQAQLGITVVLVTHDLDEAARlADRVVVLRDG 177
PLN03130 PLN03130
ABC transporter C family member; Provisional
1162-1461 4.01e-30

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 130.63  E-value: 4.01e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1162 GKIEIMDVNFRYlsRPNVP-IYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDLKndhhivfkneqtgesskeqmq 1240
Cdd:PLN03130 1236 GSIKFEDVVLRY--RPELPpVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELE--------------------- 1292
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1241 qgdeeqnvgmknanefssskegadgqsstlfknSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIK-FGKE 1319
Cdd:PLN03130 1293 ---------------------------------RGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLDpFNEH 1339
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1320 NATreDVKRACKFAAIDEFIESLPNQYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTI 1399
Cdd:PLN03130 1340 NDA--DLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTI 1417
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 156095386 1400 VDikDKADKTIITIAHRIASIKRSDKIVVFNnpdrTGSfVQAQGTHEELLSVQDGVYKKYVK 1461
Cdd:PLN03130 1418 RE--EFKSCTMLIIAHRLNTIIDCDRILVLD----AGR-VVEFDTPENLLSNEGSAFSKMVQ 1472
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
1164-1453 4.23e-30

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: 119.91  E-value: 4.23e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYLSRPnvpIYKDLTFSCESKKTTAIVGETGSGKSTvmslLMRfydlkndhHIVfkneqtgesskeqmqqgd 1243
Cdd:cd03261     1 IELRGLTKSFGGRT---VLKGVDLDVRRGEILAIIGPSGSGKST----LLR--------LIV------------------ 47
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 eeqnvgmknanefssskegadGQsstLFKNSGKILLDGVDICDYN---LKDLRNLFSIVSQEPMLFN-MSIYENIKFG-- 1317
Cdd:cd03261    48 ---------------------GL---LRPDSGEVLIDGEDISGLSeaeLYRLRRRMGMLFQSGALFDsLTVFENVAFPlr 103
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1318 -----KENATREDVKRACKFAAIDEFIESLPNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSE 1392
Cdd:cd03261   104 ehtrlSEEEIREIVLEKLEAVGLRGAEDLYPAE-----------LSGGMKKRVALARALALDPELLLYDEPTAGLDPIAS 172
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 156095386 1393 KLIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVVFNNpdrtgSFVQAQGTHEELLSVQD 1453
Cdd:cd03261   173 GVIDDLIRSLKKELGLTSIMVTHDLDTAFAiADRIAVLYD-----GKIVAEGTPEELRASDD 229
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
383-655 4.52e-30

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: 119.91  E-value: 4.52e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHYDTRKdveIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIIN--DSHNLKDVNLKWWRS 460
Cdd:cd03261     1 IELRGLTKSFGGRT---VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDgeDISGLSEAELYRLRR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  461 KIGVVSQDPLLFSN-SIKNNIKYSLYslkDLEALSEEsnedgfssqsdsnsrnscrakcagdlndMIqttdsTELIQvrk 539
Cdd:cd03261    78 RMGMLFQSGALFDSlTVFENVAFPLR---EHTRLSEE----------------------------EI-----REIVL--- 118
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  540 nyETIEdsevvsvskKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQ 619
Cdd:cd03261   119 --EKLE---------AVGLRGAEDLYP-----------AELSGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVID 176
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 156095386  620 KTINNLKGNENRITIIIAHRLSTIRY-ANTIFVLSNR 655
Cdd:cd03261   177 DLIRSLKKELGLTSIMVTHDLDTAFAiADRIAVLYDG 213
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
1164-1450 4.85e-30

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: 126.56  E-value: 4.85e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYLSRPnVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfkneQTGESSkeqmqqgd 1243
Cdd:COG1123     5 LEVRDLSVRYPGGD-VPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLP------------HGGRIS-------- 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 eeqnvgmknanefssskegadgqsstlfknsGKILLDGVDICDYNLKDLRNLFSIVSQEPM--LFNMSIYENIKFGKEN- 1320
Cdd:COG1123    64 -------------------------------GEVLLDGRDLLELSEALRGRRIGMVFQDPMtqLNPVTVGDQIAEALENl 112
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1321 -----ATREDVKRACKFAAIDEFIESLPNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLI 1395
Cdd:COG1123   113 glsraEARARVLELLEAVGLERRLDRYPHQ-----------LSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAEI 181
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 156095386 1396 EKTIVDIKDKADKTIITIAHRIASIKR-SDKIVVFNNpdrtGSFVqAQGTHEELLS 1450
Cdd:COG1123   182 LDLLRELQRERGTTVLLITHDLGVVAEiADRVVVMDD----GRIV-EDGPPEEILA 232
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
1164-1449 5.25e-30

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 120.87  E-value: 5.25e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYLSRPNvPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfkneqtgesskeqmqqgd 1243
Cdd:PRK13632    8 IKVENVSFSYPNSEN-NALKNVSFEINEGEYVAILGHNGSGKSTISKIL------------------------------- 55
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 eeqnvgmknanefssskegadgqsSTLFK-NSGKILLDGVDICDYNLKDLRNLFSIVSQEP--MLFNMSIYENIKFGKEN 1320
Cdd:PRK13632   56 ------------------------TGLLKpQSGEIKIDGITISKENLKEIRKKIGIIFQNPdnQFIGATVEDDIAFGLEN 111
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1321 A--TREDVKRACKFAA----IDEFIESLPnqydtnvgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKL 1394
Cdd:PRK13632  112 KkvPPKKMKDIIDDLAkkvgMEDYLDKEP-----------QNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKRE 180
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 156095386 1395 IEKTIVDIKDKADKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVqAQGTHEELL 1449
Cdd:PRK13632  181 IKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSE----GKLI-AQGKPKEIL 230
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
383-654 5.41e-30

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: 117.67  E-value: 5.41e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHYdtrKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIIND-SHNLKDVNLKWWRSK 461
Cdd:cd03229     1 LELKNVSKRY---GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGeDLTDLEDELPPLRRR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  462 IGVVSQDPLLFSN-SIKNNIkyslyslkdlealseesnedgfssqsdsnsrnscrakcagdlndmiqttdsteliqvrkn 540
Cdd:cd03229    78 IGMVFQDFALFPHlTVLENI------------------------------------------------------------ 97
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  541 yetiedsevvsvskkvlihdfvsALPdkyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQK 620
Cdd:cd03229    98 -----------------------ALG-------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRA 141
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 156095386  621 TINNLKGNENRITIIIAHRLS-TIRYANTIFVLSN 654
Cdd:cd03229   142 LLKSLQAQLGITVVLVTHDLDeAARLADRVVVLRD 176
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
1164-1453 7.15e-30

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: 119.31  E-value: 7.15e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYLSRPnvpIYKDLTFSCESKKTTAIVGETGSGKSTvmslLMRfydlkndhHIVfkneqtgesskeqmqqgd 1243
Cdd:COG1127     6 IEVRNLTKSFGDRV---VLDGVSLDVPRGEILAIIGGSGSGKSV----LLK--------LII------------------ 52
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 eeqnvgmknanefssskegadGQsstLFKNSGKILLDGVDICDYNLKDLRNL---FSIVSQEPMLF-NMSIYENIKFG-- 1317
Cdd:COG1127    53 ---------------------GL---LRPDSGEILVDGQDITGLSEKELYELrrrIGMLFQGGALFdSLTVFENVAFPlr 108
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1318 -----KENATREDVKRACKFAAIDEFIESLPNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSE 1392
Cdd:COG1127   109 ehtdlSEAEIRELVLEKLELVGLPGAADKMPSE-----------LSGGMRKRVALARALALDPEILLYDEPTAGLDPITS 177
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 156095386 1393 KLIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVVFNNpdrtGSfVQAQGTHEELLSVQD 1453
Cdd:COG1127   178 AVIDELIRELRDELGLTSVVVTHDLDSAFAiADRVAVLAD----GK-IIAEGTPEELLASDD 234
ABCC_SUR2 cd03288
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...
1162-1464 7.70e-30

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: 120.01  E-value: 7.70e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1162 GKIEIMDVNFRYLSRPNvPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhiVFKneqtgesskeqmqq 1241
Cdd:cd03288    18 GEIKIHDLCVRYENNLK-PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVD-------IFD-------------- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1242 gdeeqnvgmknanefssskegadgqsstlfknsGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKfGKENA 1321
Cdd:cd03288    76 ---------------------------------GKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLD-PECKC 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1322 TREDVKRACKFAAIDEFIESLPNQYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIvd 1401
Cdd:cd03288   122 TDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVV-- 199
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 156095386 1402 IKDKADKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQAQgTHEELLSVQDGVYKKYVKLAK 1464
Cdd:cd03288   200 MTAFADRTVVTIAHRVSTILDADLVLVLSR----GILVECD-TPENLLAQEDGVFASLVRTDK 257
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
383-654 3.30e-29

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 117.07  E-value: 3.30e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHYDTRK-DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDS--HNLKDVNL-KWW 458
Cdd:COG1136     5 LELRNLTKSYGTGEgEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQdiSSLSERELaRLR 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  459 RSKIGVVSQDPLLFSN-SIKNNIKYSLYslkdlealseesnedgFSSQSDSNSRNscRAKcagdlndmiqttdstELIqv 537
Cdd:COG1136    85 RRHIGFVFQFFNLLPElTALENVALPLL----------------LAGVSRKERRE--RAR---------------ELL-- 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  538 rknyetiedsevvsvsKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYL 617
Cdd:COG1136   130 ----------------ERVGLGDRLDHRP-----------SQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEE 182
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 156095386  618 VQKTINNLKGNENRITIIIAHRLSTIRYANTIFVLSN 654
Cdd:COG1136   183 VLELLRELNRELGTTIVMVTHDPELAARADRVIRLRD 219
type_I_sec_PrtD TIGR01842
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ...
400-654 3.74e-29

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: 124.38  E-value: 3.74e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIInDSHNLKDVNLKWWRSKIGVVSQDPLLFSNSIKNN 479
Cdd:TIGR01842  333 TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRL-DGADLKQWDRETFGKHIGYLPQDVELFPGTVAEN 411
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   480 IkyslyslkdlealseesnedgfssqsdsnsrnsCRAKcagdlndmiqttdsteliqvrknyETIEDSEVVSVSKKVLIH 559
Cdd:TIGR01842  412 I---------------------------------ARFG------------------------ENADPEKIIEAAKLAGVH 434
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   560 DFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGnENRITIIIAHR 639
Cdd:TIGR01842  435 ELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKA-RGITVVVITHR 513
                          250
                   ....*....|....*
gi 156095386   640 LSTIRYANTIFVLSN 654
Cdd:TIGR01842  514 PSLLGCVDKILVLQD 528
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
384-654 5.22e-29

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: 114.26  E-value: 5.22e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  384 QFKNVRFHYDTRKdveIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDsHNLKDVNLKWWRSKIG 463
Cdd:cd00267     1 EIENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDG-KDIAKLPLEELRRRIG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  464 VVSQdpllfsnsiknnikyslyslkdlealseesnedgfssqsdsnsrnscrakcagdlndmiqttdsteliqvrknyet 543
Cdd:cd00267    77 YVPQ---------------------------------------------------------------------------- 80
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  544 iedsevvsvskkvlihdfvsalpdkyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTIN 623
Cdd:cd00267    81 ------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLR 124
                         250       260       270
                  ....*....|....*....|....*....|..
gi 156095386  624 NLKgNENRITIIIAHRLSTI-RYANTIFVLSN 654
Cdd:cd00267   125 ELA-EEGRTVIIVTHDPELAeLAADRVIVLKD 155
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
383-643 6.95e-29

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: 116.88  E-value: 6.95e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHYdtrKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDSHNLKDVNlkWWRSKI 462
Cdd:COG4555     2 IEVENLSKKY---GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPR--EARRQI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  463 GVVSQDPLLFSN-SIKNNIKYslyslkdlealseesnedgfssqsdsnsrnscrakcAGDLNDMiqttdsteliQVRKNY 541
Cdd:COG4555    77 GVLPDERGLYDRlTVRENIRY------------------------------------FAELYGL----------FDEELK 110
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  542 ETIEDsevvsvskkvLIHDFvsALPDKYETLVGsnasKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKT 621
Cdd:COG4555   111 KRIEE----------LIELL--GLEEFLDRRVG----ELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREI 174
                         250       260
                  ....*....|....*....|..
gi 156095386  622 INNLKgNENRITIIIAHRLSTI 643
Cdd:COG4555   175 LRALK-KEGKTVLFSSHIMQEV 195
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
1164-1427 7.40e-29

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: 115.66  E-value: 7.40e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYLSRPN-VPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfkneqtgesskeqmqqg 1242
Cdd:cd03255     1 IELKNLSKTYGGGGEkVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNIL------------------------------ 50
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1243 deeqnvgmknanefssskegadgqsSTLFK-NSGKILLDGVDICDYNLKDLRNL----FSIVSQEPMLF-NMSIYENIKF 1316
Cdd:cd03255    51 -------------------------GGLDRpTSGEVRVDGTDISKLSEKELAAFrrrhIGFVFQSFNLLpDLTALENVEL 105
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1317 -----GKENATRED-VKRACKFAAIDEFIESLPNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSN 1390
Cdd:cd03255   106 plllaGVPKKERRErAEELLERVGLGDRLNHYPSE-----------LSGGQQQRVAIARALANDPKIILADEPTGNLDSE 174
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 156095386 1391 SEKLIEKTIVDIKDKADKTIITIAH--RIASikRSDKIV 1427
Cdd:cd03255   175 TGKEVMELLRELNKEAGTTIVVVTHdpELAE--YADRII 211
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
383-656 7.63e-29

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: 116.62  E-value: 7.63e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHYDTRKdveIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIIN--DSHNLKDVNLKWWRS 460
Cdd:COG1127     6 IEVRNLTKSFGDRV---VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDgqDITGLSEKELYELRR 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  461 KIGVVSQDPLLFSN-SIKNNIKYSLYSLKDleaLSEEsnedgfssqsdsnsrnscrakcagdlndmiqttdsteliqvrk 539
Cdd:COG1127    83 RIGMLFQGGALFDSlTVFENVAFPLREHTD---LSEA------------------------------------------- 116
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  540 nyetiedsevvsvskkvLIHDFVSalpDKYEtLVG-SNA-----SKLSGGQKQRISIARAIIRNPKILILDEATSSLDNK 613
Cdd:COG1127   117 -----------------EIRELVL---EKLE-LVGlPGAadkmpSELSGGMRKRVALARALALDPEILLYDEPTAGLDPI 175
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 156095386  614 SEYLVQKTINNLKGNENRITIIIAHRLSTIRY-ANTIFVLSNRE 656
Cdd:COG1127   176 TSAVIDELIRELRDELGLTSVVVTHDLDSAFAiADRVAVLADGK 219
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
1164-1464 8.18e-29

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: 116.50  E-value: 8.18e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYlsrPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFydlkndhhivfkneqtgesskeqmqqgd 1243
Cdd:COG4555     2 IEVENLSKKY---GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGL---------------------------- 50
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 eeqnvgmknanefssskegadgqsstLFKNSGKILLDGVDICDYNLKDLRNLFsIVSQEPMLF-NMSIYENIKFgkeNAT 1322
Cdd:COG4555    51 --------------------------LKPDSGSILIDGEDVRKEPREARRQIG-VLPDERGLYdRLTVRENIRY---FAE 100
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1323 REDVKRACKFAAIDEFIES--LPNQYDTNVGpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIV 1400
Cdd:COG4555   101 LYGLFDEELKKRIEELIELlgLEEFLDRRVG----ELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILR 176
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156095386 1401 DIKDKaDKTIITIAHRIASIKR-SDKIVVFNNpdrtGSfVQAQGTHEELLS--VQDGVYKKYVKLAK 1464
Cdd:COG4555   177 ALKKE-GKTVLFSSHIMQEVEAlCDRVVILHK----GK-VVAQGSLDELREeiGEENLEDAFVALIG 237
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
360-725 1.37e-28

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 123.01  E-value: 1.37e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  360 EIINRKPLVENNQDGKKLKDIKKIQFKNVRFHYDTRKDVEIyKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTE 439
Cdd:PRK11160  316 EITEQKPEVTFPTTSTAAADQVSLTLNNVSFTYPDQPQPVL-KGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQ 394
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  440 GDVIINDsHNLKDVNLKWWRSKIGVVSQDPLLFSNSIKNNIKYslyslkdlealseesnedgfssqsdsnsrnscrAKca 519
Cdd:PRK11160  395 GEILLNG-QPIADYSEAALRQAISVVSQRVHLFSATLRDNLLL---------------------------------AA-- 438
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  520 gdlndmiqttdsteliqvrknyETIEDSEVVSVSKKVLIHDFVSAlPDKYETLVGSNASKLSGGQKQRISIARAIIRNPK 599
Cdd:PRK11160  439 ----------------------PNASDEALIEVLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAP 495
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  600 ILILDEATSSLDNKSEylvQKTINNL-KGNENRITIIIAHRLSTIRYANTIFVLsnrENGStvdvdvlgedptkdsnekn 678
Cdd:PRK11160  496 LLLLDEPTEGLDAETE---RQILELLaEHAQNKTVLMITHRLTGLEQFDRICVM---DNGQ------------------- 550
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 156095386  679 ekhdkqekggknssanqkignagsyIIEQGTHDALMKNKNGiYYTMI 725
Cdd:PRK11160  551 -------------------------IIEQGTHQELLAQQGR-YYQLK 571
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
1164-1440 1.88e-28

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: 114.54  E-value: 1.88e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYlsrPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFydlkndhhivfkneqtgesskEQMqqgd 1243
Cdd:cd03259     1 LELKGLSKTY---GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGL---------------------ERP---- 52
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 eeqnvgmknanefssskegadgqsstlfkNSGKILLDGVDICDYNLKDlRNLfSIVSQEPMLF-NMSIYENIKFG----- 1317
Cdd:cd03259    53 -----------------------------DSGEILIDGRDVTGVPPER-RNI-GMVFQDYALFpHLTVAENIAFGlklrg 101
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1318 -KENATREDVKRACKFAAIDEFIESLPNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIE 1396
Cdd:cd03259   102 vPKAEIRARVRELLELVGLEGLLNRYPHE-----------LSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELR 170
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 156095386 1397 KTIVDIKDKADKTIITIAHRIASIKR-SDKIVVFNNpdrtGSFVQ 1440
Cdd:cd03259   171 EELKELQRELGITTIYVTHDQEEALAlADRIAVMNE----GRIVQ 211
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
382-730 2.81e-28

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


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 122.13  E-value: 2.81e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  382 KIQFKNVRFHYdtRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIInDSHNLKDVNLKWWRSK 461
Cdd:PRK10790  340 RIDIDNVSFAY--RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRL-DGRPLSSLSHSVLRQG 416
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  462 IGVVSQDPLLFSNSIKNNIkyslyslkdleALSEESNEDgfssqsdsnsrnscrakcagdlndmiqttdsteliQVRKNY 541
Cdd:PRK10790  417 VAMVQQDPVVLADTFLANV-----------TLGRDISEE-----------------------------------QVWQAL 450
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  542 ETIEdsevvsvskkvlIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKT 621
Cdd:PRK10790  451 ETVQ------------LAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQA 518
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  622 INNLKgnENRITIIIAHRLSTIRYANTIFVLsnrengstvdvdvlgedptkdsneknekHDKQekggknssanqkignag 701
Cdd:PRK10790  519 LAAVR--EHTTLVVIAHRLSTIVEADTILVL----------------------------HRGQ----------------- 551
                         330       340
                  ....*....|....*....|....*....
gi 156095386  702 syIIEQGTHDALMKnKNGIYYTMINNQKV 730
Cdd:PRK10790  552 --AVEQGTHQQLLA-AQGRYWQMYQLQLA 577
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
383-661 3.89e-28

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: 114.52  E-value: 3.89e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHYDTR-KDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDsHNLKDVNLKWWRSK 461
Cdd:COG1124     2 LEVRNLSVSYGQGgRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDG-RPVTRRRRKAFRRR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  462 IGVVSQDPLLfsnSIknNIKYSLYslkdlEALSEEsnedgfssqsdsnsrnscrAKCAGDLNDmiqttdsteliqvrkny 541
Cdd:COG1124    81 VQMVFQDPYA---SL--HPRHTVD-----RILAEP-------------------LRIHGLPDR----------------- 114
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  542 etieDSEVVSVSKKV-LIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDnkseYLVQK 620
Cdd:COG1124   115 ----EERIAELLEQVgLPPSFLDRYP-----------HQLSGGQRQRVAIARALILEPELLLLDEPTSALD----VSVQA 175
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 156095386  621 TINNL----KGNENRITIIIAHRLSTIRY-ANTIFVLsnrENGSTV 661
Cdd:COG1124   176 EILNLlkdlREERGLTYLFVSHDLAVVAHlCDRVAVM---QNGRIV 218
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
383-656 4.59e-28

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: 113.35  E-value: 4.59e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHYDTRKD-VEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIIN--DSHNLKDVNL-KWW 458
Cdd:cd03255     1 IELKNLSKTYGGGGEkVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDgtDISKLSEKELaAFR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  459 RSKIGVVSQDPLLFSN-SIKNNIKYSLYSLKDLEALSEEsnedgfssqsdsnsrnscRAKcagdlndmiqttdstELIqv 537
Cdd:cd03255    81 RRHIGFVFQSFNLLPDlTALENVELPLLLAGVPKKERRE------------------RAE---------------ELL-- 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  538 rknyetiedsevvsvsKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYL 617
Cdd:cd03255   126 ----------------ERVGLGDRLNHYP-----------SELSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKE 178
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 156095386  618 VQKTINNLKGNENRITIIIAHRLSTIRYANTIFVLSNRE 656
Cdd:cd03255   179 VMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGK 217
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
1164-1429 5.54e-28

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 113.60  E-value: 5.54e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYLSRPN-VPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfkneqtgesskeqmqqg 1242
Cdd:COG1136     5 LELRNLTKSYGTGEGeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNIL------------------------------ 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1243 deeqnvgmknanefssskegadgqsSTLFK-NSGKILLDGVDICDYNLKDL----RNLFSIVSQEPMLF-NMSIYENIKF 1316
Cdd:COG1136    55 -------------------------GGLDRpTSGEVLIDGQDISSLSERELarlrRRHIGFVFQFFNLLpELTALENVAL 109
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1317 G------KENATREDVKRACKFAAIDEFIESLPNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSN 1390
Cdd:COG1136   110 PlllagvSRKERRERARELLERVGLGDRLDHRPSQ-----------LSGGQQQRVAIARALVNRPKLILADEPTGNLDSK 178
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 156095386 1391 SEKLIEKTIVDIKDKADKTIITIAH--RIASikRSDKIVVF 1429
Cdd:COG1136   179 TGEEVLELLRELNRELGTTIVMVTHdpELAA--RADRVIRL 217
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
383-668 6.69e-28

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 113.22  E-value: 6.69e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHYdtRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIIN--DSHNLKDVNLKWWRS 460
Cdd:COG2884     2 IRFENVSKRY--PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNgqDLSRLKRREIPYLRR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  461 KIGVVSQD-PLLFSNSIKNNIKYSLyslkdlEALSEESNEdgfssqsdsnsrnscrakcagdlndmiqttdstelIQVRk 539
Cdd:COG2884    80 RIGVVFQDfRLLPDRTVYENVALPL------RVTGKSRKE-----------------------------------IRRR- 117
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  540 nyetiedseVVSVSKKVLIHDFVSALPDKyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDnksEYLVQ 619
Cdd:COG2884   118 ---------VREVLDLVGLSDKAKALPHE-----------LSGGEQQRVAIARALVNRPELLLADEPTGNLD---PETSW 174
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 156095386  620 KTINNLKG-NENRITIIIA-HRLSTI-RYANTIFVLsnrENGSTVDVDVLGE 668
Cdd:COG2884   175 EIMELLEEiNRRGTTVLIAtHDLELVdRMPKRVLEL---EDGRLVRDEARGV 223
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
1274-1450 1.03e-27

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: 113.20  E-value: 1.03e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1274 SGKILLDGVDICdyNLKDLRNLFSIVSQEPMLF-NMSIYENIKFGKENATREDVKRACKFAAIDEF--IESLPNQYDtnv 1350
Cdd:cd03299    53 SGKILLNGKDIT--NLPPEKRDISYVPQNYALFpHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMlgIDHLLNRKP--- 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1351 gpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNS-EKLIEKtIVDIKDKADKTIITIAHRIASIKR-SDKIVV 1428
Cdd:cd03299   128 ----ETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTkEKLREE-LKKIRKEFGVTVLHVTHDFEEAWAlADKVAI 202
                         170       180
                  ....*....|....*....|..
gi 156095386 1429 FNNpdrtGSFVQAqGTHEELLS 1450
Cdd:cd03299   203 MLN----GKLIQV-GKPEEVFK 219
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
382-653 1.25e-27

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: 111.74  E-value: 1.25e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  382 KIQFKNVRFHYdtRKDV-EIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIInDSHNLKDVNLKWWRS 460
Cdd:cd03369     6 EIEVENLSVRY--APDLpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEI-DGIDISTIPLEDLRS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  461 KIGVVSQDPLLFSNSIKNNIkyslyslkdlealseesneDGFSSQSDsnsrnscrakcagdlndmiqttdsteliqvRKN 540
Cdd:cd03369    83 SLTIIPQDPTLFSGTIRSNL-------------------DPFDEYSD------------------------------EEI 113
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  541 YETIEDSEVvsvskkvlihdfvsalpdkyetlvGSNaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQK 620
Cdd:cd03369   114 YGALRVSEG------------------------GLN---LSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQK 166
                         250       260       270
                  ....*....|....*....|....*....|...
gi 156095386  621 TINNLKGNENriTIIIAHRLSTIRYANTIFVLS 653
Cdd:cd03369   167 TIREEFTNST--ILTIAHRLRTIIDYDKILVMD 197
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
383-661 2.47e-27

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: 110.10  E-value: 2.47e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHYDtRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDSHNLKDVNLKwwRSKI 462
Cdd:cd03247     1 LSINNVSFSYP-EQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKAL--SSLI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  463 GVVSQDPLLFSNSIKNNIkyslyslkdlealseesnedgfssqsdsnsrnscrakcagdlndmiqttdsteliqvrknye 542
Cdd:cd03247    78 SVLNQRPYLFDTTLRNNL-------------------------------------------------------------- 95
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  543 tiedsevvsvskkvlihdfvsalpdkyetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI 622
Cdd:cd03247    96 ----------------------------------GRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLI 141
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 156095386  623 nnLKGNENRITIIIAHRLSTIRYANTIFVLsnrENGSTV 661
Cdd:cd03247   142 --FEVLKDKTLIWITHHLTGIEHMDKILFL---ENGKII 175
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
386-654 3.42e-27

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: 109.83  E-value: 3.42e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  386 KNVRFHYDTRkdvEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDsHNLKDVNLKWWRSKIGVV 465
Cdd:cd03214     3 ENLSVGYGGR---TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDG-KDLASLSPKELARKIAYV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  466 SQdpllfsnsiknnikyslyslkdlealseesnedgfssqsdsnsrnscrakcagdlndMIQTTDSTELIQvrKNYETie 545
Cdd:cd03214    79 PQ---------------------------------------------------------ALELLGLAHLAD--RPFNE-- 97
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  546 dsevvsvskkvlihdfvsalpdkyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNL 625
Cdd:cd03214    98 ----------------------------------LSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRL 143
                         250       260       270
                  ....*....|....*....|....*....|
gi 156095386  626 KGNENRITIIIAHRLS-TIRYANTIFVLSN 654
Cdd:cd03214   144 ARERGKTVVMVLHDLNlAARYADRVILLKD 173
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
1164-1450 3.93e-27

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: 112.06  E-value: 3.93e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYlsrPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFydLKNDhhivfkneqtgesskeqmqqgd 1243
Cdd:COG1120     2 LEAENLSVGY---GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGL--LKPS---------------------- 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 eeqnvgmknanefssskegadgqsstlfknSGKILLDGVDICDYNLKDLRNLFSIVSQEPML-FNMSIYENIKFGK---- 1318
Cdd:COG1120    55 ------------------------------SGEVLLDGRDLASLSRRELARRIAYVPQEPPApFGLTVRELVALGRyphl 104
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1319 ---ENATREDVKRAckFAAIDEF-IESLPNQydtnvgPYGkSLSGGQKQRIAIARALLREPKILLLDEATSSLD-SNSEK 1393
Cdd:COG1120   105 glfGRPSAEDREAV--EEALERTgLEHLADR------PVD-ELSGGERQRVLIARALAQEPPLLLLDEPTSHLDlAHQLE 175
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 156095386 1394 LIEkTIVDIKDKADKTII------TIAHRIAsikrsDKIVVFNNpdrtGSfVQAQGTHEELLS 1450
Cdd:COG1120   176 VLE-LLRRLARERGRTVVmvlhdlNLAARYA-----DRLVLLKD----GR-IVAQGPPEEVLT 227
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
383-663 4.25e-27

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: 111.13  E-value: 4.25e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHY-DTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIIN--DSHNLKDVNLKWWR 459
Cdd:cd03258     2 IELKNVSKVFgDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDgtDLTLLSGKELRKAR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  460 SKIGVVSQDPLLFSN-SIKNNIKYSLyslkdlealseesnEDGFSSQSDSNSRnscrakcagdlndmiqttdSTELIqvr 538
Cdd:cd03258    82 RRIGMIFQHFNLLSSrTVFENVALPL--------------EIAGVPKAEIEER-------------------VLELL--- 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  539 knyetiedsEVVSVSKKVlihdfvsalpDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS---- 614
Cdd:cd03258   126 ---------ELVGLEDKA----------DAY-------PAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETtqsi 179
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 156095386  615 -EYLvqKTINnlkgNENRITI-IIAHRLSTIR-YANTIFVLSNR---ENGSTVDV 663
Cdd:cd03258   180 lALL--RDIN----RELGLTIvLITHEMEVVKrICDRVAVMEKGevvEEGTVEEV 228
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
1165-1431 5.99e-27

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: 108.10  E-value: 5.99e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1165 EIMDVNFRYlsrPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFydlkndhhivfkneqtgesskeqmqqgde 1244
Cdd:cd00267     1 EIENLSFRY---GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGL----------------------------- 48
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1245 eqnvgmknanefssskegadgqsstLFKNSGKILLDGVDICDYNLKDLRNLFSIVSQepmlfnmsiyenikfgkenatre 1324
Cdd:cd00267    49 -------------------------LKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ----------------------- 80
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1325 dvkrackfaaidefieslpnqydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKD 1404
Cdd:cd00267    81 --------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAE 128
                         250       260
                  ....*....|....*....|....*...
gi 156095386 1405 KaDKTIITIAHRIASIKR-SDKIVVFNN 1431
Cdd:cd00267   129 E-GRTVIIVTHDPELAELaADRVIVLKD 155
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
382-636 6.49e-27

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


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 111.28  E-value: 6.49e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  382 KIQFKNVRFHYDTRKdveIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYD--P---TEGDVIINDsHNL--KDVN 454
Cdd:COG1117    11 KIEVRNLNVYYGDKQ---ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPgarVEGEILLDG-EDIydPDVD 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  455 LKWWRSKIGVVSQDPLLFSNSIKNNIKYSL-----YSLKDLEALSEESnedgfssqsdsnsrnscrakcagdlndmiqtt 529
Cdd:COG1117    87 VVELRRRVGMVFQKPNPFPKSIYDNVAYGLrlhgiKSKSELDEIVEES-------------------------------- 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  530 dsteLIQVrknyetiedsevvsvskkvlihdfvsALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSS 609
Cdd:COG1117   135 ----LRKA--------------------------ALWDEVKDRLKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSA 184
                         250       260
                  ....*....|....*....|....*..
gi 156095386  610 LDNKSEYLVQKTINNLKgneNRITIII 636
Cdd:COG1117   185 LDPISTAKIEELILELK---KDYTIVI 208
ECF_ATPase_1 TIGR04520
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
383-654 8.04e-27

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: 111.37  E-value: 8.04e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   383 IQFKNVRFHYDTRKDVEIyKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDSHNLKDVNLKWWRSKI 462
Cdd:TIGR04520    1 IEVENVSFSYPESEKPAL-KNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENLWEIRKKV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   463 GVVSQDPllfSNSIKNNIkyslyslkdLEalseesnED-GFssqsdsnsrnscrakcaGDLNDMIqttdSTELIQVRkny 541
Cdd:TIGR04520   80 GMVFQNP---DNQFVGAT---------VE-------DDvAF-----------------GLENLGV----PREEMRKR--- 116
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   542 etiedseVVSVSKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKT 621
Cdd:TIGR04520  117 -------VDEALKLVGMEDFRDREP-----------HLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLET 178
                          250       260       270
                   ....*....|....*....|....*....|....
gi 156095386   622 INNLKgNENRITII-IAHRLSTIRYANTIFVLSN 654
Cdd:TIGR04520  179 IRKLN-KEEGITVIsITHDMEEAVLADRVIVMNK 211
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
1164-1450 1.46e-26

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: 110.28  E-value: 1.46e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYLSRP-NVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFydLKNDhhivfkneqtgesskeqmqqg 1242
Cdd:COG1124     2 LEVRNLSVSYGQGGrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGL--ERPW--------------------- 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1243 deeqnvgmknanefssskegadgqsstlfknSGKILLDGVDICDYNLKDLRNLFSIVSQEPML-FN------MSIYENIK 1315
Cdd:COG1124    59 -------------------------------SGEVTFDGRPVTRRRRKAFRRRVQMVFQDPYAsLHprhtvdRILAEPLR 107
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1316 FGKENATREDVKRACKFAAID-EFIESLPNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKL 1394
Cdd:COG1124   108 IHGLPDREERIAELLEQVGLPpSFLDRYPHQ-----------LSGGQRQRVAIARALILEPELLLLDEPTSALDVSVQAE 176
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 156095386 1395 IEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVVFNNpdrtGSFVqAQGTHEELLS 1450
Cdd:COG1124   177 ILNLLKDLREERGLTYLFVSHDLAVVAHlCDRVAVMQN----GRIV-EELTVADLLA 228
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
1164-1450 2.19e-26

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 109.38  E-value: 2.19e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYlsrPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFydlkndhhivfkneqtgesskeqmqqgd 1243
Cdd:COG1131     1 IEVRGLTKRY---GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGL---------------------------- 49
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 eeqnvgmknanefssskegadgqsstLFKNSGKILLDGVDICDyNLKDLRNLFSIVSQEPMLF-NMSIYENIKF-----G 1317
Cdd:COG1131    50 --------------------------LRPTSGEVRVLGEDVAR-DPAEVRRRIGYVPQEPALYpDLTVRENLRFfarlyG 102
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1318 KENATREdvkrackfAAIDEFIE--SLPNQYDTNVGpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLI 1395
Cdd:COG1131   103 LPRKEAR--------ERIDELLElfGLTDAADRKVG----TLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARREL 170
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 156095386 1396 EKTIVDIKDKaDKTIITIAHRIASIKR-SDKIVVFNNpdrtGSFVqAQGTHEELLS 1450
Cdd:COG1131   171 WELLRELAAE-GKTVLLSTHYLEEAERlCDRVAIIDK----GRIV-ADGTPDELKA 220
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
383-655 2.31e-26

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: 108.71  E-value: 2.31e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHYDTRKD-VEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDshnlKDVNLKwwRSK 461
Cdd:cd03293     1 LEVRNVSKTYGGGGGaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG----EPVTGP--GPD 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  462 IGVVSQDPLLFS-NSIKNNIKYSLyslkdlealseesnedgfssqsdsnsrnscraKCAGdlndmIQTTDSTEliqvrkn 540
Cdd:cd03293    75 RGYVFQQDALLPwLTVLDNVALGL--------------------------------ELQG-----VPKAEARE------- 110
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  541 yetiedsEVVSVSKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQK 620
Cdd:cd03293   111 -------RAEELLELVGLSGFENAYP-----------HQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLQE 172
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 156095386  621 TINNLKgNENRITII-IAHRLS-TIRYANTIFVLSNR 655
Cdd:cd03293   173 ELLDIW-RETGKTVLlVTHDIDeAVFLADRVVVLSAR 208
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
383-659 3.64e-26

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: 107.56  E-value: 3.64e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHYDTRKDVEIY--KDLNFTLTEGKTYAFVGESGCGKSTILKLI--ErlYDPTEGDVIINDShnlkdvnlkww 458
Cdd:cd03250     1 ISVEDASFTWDSGEQETSFtlKDINLEVPKGELVAIVGPVGSGKSSLLSALlgE--LEKLSGSVSVPGS----------- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  459 rskIGVVSQDPLLFSNSIKNNIKyslyslkdlealseesnedgFSSQSDSnsrnscrakcagdlndmiqttdsteliqvr 538
Cdd:cd03250    68 ---IAYVSQEPWIQNGTIRENIL--------------------FGKPFDE------------------------------ 94
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  539 KNYEtiedsEVVSVSkkVLIHDFvSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNK-SEYL 617
Cdd:cd03250    95 ERYE-----KVIKAC--ALEPDL-EILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHvGRHI 166
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 156095386  618 VQKTINNLkGNENRITIIIAHRLSTIRYANTIFVLsnrENGS 659
Cdd:cd03250   167 FENCILGL-LLNNKTRILVTHQLQLLPHADQIVVL---DNGR 204
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
383-654 4.20e-26

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: 108.98  E-value: 4.20e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHYDTRkdvEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDsHNLKDVNLKWWRSKI 462
Cdd:COG1120     2 LEAENLSVGYGGR---PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDG-RDLASLSRRELARRI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  463 GVVSQDPLL-FSnsiknnikyslYSLKDL---------EALSEESNEDgfssqsdsnsrnscRAKCAgdlnDMIQTTDST 532
Cdd:COG1120    78 AYVPQEPPApFG-----------LTVRELvalgryphlGLFGRPSAED--------------REAVE----EALERTGLE 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  533 ELIQvrKNYETiedsevvsvskkvlihdfvsalpdkyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDN 612
Cdd:COG1120   129 HLAD--RPVDE------------------------------------LSGGERQRVLIARALAQEPPLLLLDEPTSHLDL 170
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 156095386  613 KSEYLVQKTINNLKGNENRITIIIAHRLS-TIRYANTIFVLSN 654
Cdd:COG1120   171 AHQLEVLELLRRLARERGRTVVMVLHDLNlAARYADRLVLLKD 213
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
403-645 4.27e-26

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


Pssm-ID: 443658 [Multi-domain]  Cd Length: 329  Bit Score: 110.98  E-value: 4.27e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  403 DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIIN--DSHNLKDVNLKWWRSKIGVVSQDPllfsnsiknni 480
Cdd:COG4608    36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDgqDITGLSGRELRPLRRRMQMVFQDP----------- 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  481 kYSlySLkdlealseesnedgfssqsdsNSRnscrakcagdlndMiqttdsteliqvrknyeTIEDsevvSVSKKVLIHD 560
Cdd:COG4608   105 -YA--SL---------------------NPR-------------M-----------------TVGD----IIAEPLRIHG 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  561 FVSA--LPDKYETL---VGSNAS-------KLSGGQKQRISIARAIIRNPKILILDEATSSLDnKSeylVQKTINNLKG- 627
Cdd:COG4608   127 LASKaeRRERVAELlelVGLRPEhadryphEFSGGQRQRIGIARALALNPKLIVCDEPVSALD-VS---IQAQVLNLLEd 202
                         250       260
                  ....*....|....*....|.
gi 156095386  628 --NENRIT-IIIAHRLSTIRY 645
Cdd:COG4608   203 lqDELGLTyLFISHDLSVVRH 223
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
1164-1432 4.60e-26

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: 107.94  E-value: 4.60e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRY-LSRPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfkneqtgesskeqmqqg 1242
Cdd:cd03293     1 LEVRNVSKTYgGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRII------------------------------ 50
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1243 deeqnvgmknAnefssskeGADGQSStlfknsGKILLDGVDICDYNLKdlrnlFSIVSQEPMLFN-MSIYENIKFGKENA 1321
Cdd:cd03293    51 ----------A--------GLERPTS------GEVLVDGEPVTGPGPD-----RGYVFQQDALLPwLTVLDNVALGLELQ 101
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1322 ------TREDVKRACKFAAIDEFIESLPNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLI 1395
Cdd:cd03293   102 gvpkaeARERAEELLELVGLSGFENAYPHQ-----------LSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQL 170
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 156095386 1396 EKTIVDIKDKADKTIITIAHRIA-SIKRSDKIVVFNNP 1432
Cdd:cd03293   171 QEELLDIWRETGKTVLLVTHDIDeAVFLADRVVVLSAR 208
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
383-654 6.09e-26

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: 105.94  E-value: 6.09e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHYdtrKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDsHNLKDvNLKWWRSKI 462
Cdd:cd03230     1 IEVRNLSKRY---GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLG-KDIKK-EPEEVKRRI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  463 GVVSQDPLLFSNsiknnikyslyslkdlealseesnedgfssqsdsnsrnscrakcagdlndmiqttdsteliqvrknye 542
Cdd:cd03230    76 GYLPEEPSLYEN-------------------------------------------------------------------- 87
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  543 tiedsevVSVskkvlihdfvsalpdkYETLvgsnasKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI 622
Cdd:cd03230    88 -------LTV----------------RENL------KLSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELL 138
                         250       260       270
                  ....*....|....*....|....*....|....
gi 156095386  623 NNLKgnENRITIIIA-HRLSTI-RYANTIFVLSN 654
Cdd:cd03230   139 RELK--KEGKTILLSsHILEEAeRLCDRVAILNN 170
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
383-654 1.11e-25

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: 106.45  E-value: 1.11e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHYDtrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDshnlKDV-NLKWWRSK 461
Cdd:cd03259     1 LELKGLSKTYG---SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDG----RDVtGVPPERRN 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  462 IGVVSQDPLLFSN-SIKNNIKYSLYSLKDLEAlseesnedgfssqsdsnsrnscrakcagdlndmiqttdsteliQVRKN 540
Cdd:cd03259    74 IGMVFQDYALFPHlTVAENIAFGLKLRGVPKA-------------------------------------------EIRAR 110
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  541 yetiedseVVSVSKKVLIHDFVSALPDkyetlvgsnasKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQK 620
Cdd:cd03259   111 --------VRELLELVGLEGLLNRYPH-----------ELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELRE 171
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 156095386  621 TINNLKGNENRITIIIAHRLS-TIRYANTIFVLSN 654
Cdd:cd03259   172 ELKELQRELGITTIYVTHDQEeALALADRIAVMNE 206
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
1164-1448 1.35e-25

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 110.19  E-value: 1.35e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYlsrPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfkneqtgesskeqmqqgd 1243
Cdd:COG3842     6 LELENVSKRY---GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETP------------------------- 57
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 eeqnvgmknanefssskegadgqsstlfkNSGKILLDGVDIcdynlKDL----RNlFSIVSQEPMLF-NMSIYENIKFG- 1317
Cdd:COG3842    58 -----------------------------DSGRILLDGRDV-----TGLppekRN-VGMVFQDYALFpHLTVAENVAFGl 102
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1318 -----KENATREDVKRACKFAAIDEFIESLPNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSnse 1392
Cdd:COG3842   103 rmrgvPKAEIRARVAELLELVGLEGLADRYPHQ-----------LSGGQQQRVALARALAPEPRVLLLDEPLSALDA--- 168
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156095386 1393 KLIEKTIVDIKD---KADKTIITIAH------RIasikrSDKIVVFNNpdrtGSFVQaQGTHEEL 1448
Cdd:COG3842   169 KLREEMREELRRlqrELGITFIYVTHdqeealAL-----ADRIAVMND----GRIEQ-VGTPEEI 223
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
1165-1431 1.97e-25

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: 104.82  E-value: 1.97e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1165 EIMDVNFRYlsrPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFydLKNDhhivfkneqtgesskeqmqqgde 1244
Cdd:cd03214     1 EVENLSVGY---GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGL--LKPS----------------------- 52
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1245 eqnvgmknanefssskegadgqsstlfknSGKILLDGVDICDYNLKDLRNLFSIVSQepmlfnmsiyenikfgkenatre 1324
Cdd:cd03214    53 -----------------------------SGEILLDGKDLASLSPKELARKIAYVPQ----------------------- 80
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1325 dvkrACKFAAIDEFIESlpnQYDTnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKD 1404
Cdd:cd03214    81 ----ALELLGLAHLADR---PFNE--------LSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLAR 145
                         250       260
                  ....*....|....*....|....*...
gi 156095386 1405 KADKTIITIAHRIASIKR-SDKIVVFNN 1431
Cdd:cd03214   146 ERGKTVVMVLHDLNLAARyADRVILLKD 173
ABC_6TM_Pgp_ABCB1 cd18558
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ...
64-361 3.00e-25

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: 108.13  E-value: 3.00e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   64 VSFVCATISGGTLPFFVSVFG--------VIMKNMN---------------LGENVNDIIFSLVLIGIFQFILSFISSFC 120
Cdd:cd18558     3 VGILCAIIHGGLLPAFMVIFGdmtdsftnGGMTNITgnssglnssagpfekLEEEMTLYAYYYLIIGAIVLITAYIQGSF 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  121 MDVVTTKILKTLKIEFLKSVFYQDGQFHDNNPGSKLTSDLDFYLEQVNAGIGTKFITIFTYASAFLGLYIWSLFKNARLT 200
Cdd:cd18558    83 WGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRGWKLT 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  201 LCITCVFPLIYICGVICNKKVKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGENTILKKFNLSEKLYSKYTLKANLME 280
Cdd:cd18558   163 LVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKKAITF 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  281 SLHIGMINGFILASYAFGFWYGTRIIISdlsnqqpnNDFHGGSVISILLGVLISMFMLTIILPNITEYMKsleATNNLYE 360
Cdd:cd18558   243 NISMGAAFLLIYASYALAFWYGTYLVTQ--------QEYSIGEVLTVFFSVLIGAFSAGQQVPSIEAFAN---ARGAAYH 311

                  .
gi 156095386  361 I 361
Cdd:cd18558   312 I 312
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
383-663 4.21e-25

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 108.24  E-value: 4.21e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHYDTRK-DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIIN--DSHNLKDVNLKWWR 459
Cdd:COG1135     2 IELENLSKTFPTKGgPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDgvDLTALSERELRAAR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  460 SKIGVVSQDP-LLFSNSIKNNIKYSLyslkdlealseesnedgfssqsdsnsrnscraKCAGdlndmiqttdsteliqVR 538
Cdd:COG1135    82 RKIGMIFQHFnLLSSRTVAENVALPL--------------------------------EIAG----------------VP 113
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  539 KnyETIEdsevvsvsKKV--LIhDFVSaLPDKyetlvgSNA--SKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS 614
Cdd:COG1135   114 K--AEIR--------KRVaeLL-ELVG-LSDK------ADAypSQLSGGQKQRVGIARALANNPKVLLCDEATSALDPET 175
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 156095386  615 -----EYLvqKTINnlkgNENRITI-IIAHRLSTIRY-ANTIFVLSN-R--ENGSTVDV 663
Cdd:COG1135   176 trsilDLL--KDIN----RELGLTIvLITHEMDVVRRiCDRVAVLENgRivEQGPVLDV 228
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
391-654 4.49e-25

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: 104.65  E-value: 4.49e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  391 HYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDshnlKDVNLKWWRSKIGVVSQDP- 469
Cdd:cd03226     6 SFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG----KPIKAKERRKSIGYVMQDVd 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  470 -LLFSNSIKNNIkysLYSLKDLEAlseesnedgfssqsdsnsrnscrakcagdlndmiqttdsteliqvrkNYETIEDse 548
Cdd:cd03226    82 yQLFTDSVREEL---LLGLKELDA-----------------------------------------------GNEQAET-- 109
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  549 vvsVSKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGn 628
Cdd:cd03226   110 ---VLKDLDLYALKERHP-----------LSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAA- 174
                         250       260
                  ....*....|....*....|....*..
gi 156095386  629 ENRITIIIAHRLSTI-RYANTIFVLSN 654
Cdd:cd03226   175 QGKAVIVITHDYEFLaKVCDRVLLLAN 201
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
383-663 7.16e-25

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: 110.76  E-value: 7.16e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHYDTRkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPT---EGDVIINDsHNLKDVNLKWWR 459
Cdd:COG1123     5 LEVRDLSVRYPGG-DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDG-RDLLELSEALRG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  460 SKIGVVSQDPL--LFSNSIKNNIkyslyslkdLEALseesnedgfssqsdsnsRNSCRAKcagdlndmiqttdstELIQV 537
Cdd:COG1123    83 RRIGMVFQDPMtqLNPVTVGDQI---------AEAL-----------------ENLGLSR---------------AEARA 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  538 RknyetiedseVVSVSKKVLIHDFVSALPDKyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYL 617
Cdd:COG1123   122 R----------VLELLEAVGLERRLDRYPHQ-----------LSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQAE 180
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 156095386  618 VQKTINNLKGNENRITIIIAHRLSTI-RYANTIFVLSN---RENGSTVDV 663
Cdd:COG1123   181 ILDLLRELQRERGTTVLLITHDLGVVaEIADRVVVMDDgriVEDGPPEEI 230
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
382-655 7.42e-25

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


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 105.56  E-value: 7.42e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  382 KIQFKNVRFHYDTRK-DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDshnlKDVNLKwwRS 460
Cdd:COG1116     7 ALELRGVSKRFPTGGgGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDG----KPVTGP--GP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  461 KIGVVSQDPLLFS-NSIKNNIkysLYSLKDLEALSEESNEdgfssqsdsnsrnscRAkcagdlndmiqttdsTELIqvrk 539
Cdd:COG1116    81 DRGVVFQEPALLPwLTVLDNV---ALGLELRGVPKAERRE---------------RA---------------RELL---- 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  540 nyetiedsevvsvsKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQ 619
Cdd:COG1116   124 --------------ELVGLAGFEDAYP-----------HQLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRERLQ 178
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 156095386  620 KTINNLKGNENRITIIIAH------RLstiryANTIFVLSNR 655
Cdd:COG1116   179 DELLRLWQETGKTVLFVTHdvdeavFL-----ADRVVVLSAR 215
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
383-654 1.46e-24

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 105.07  E-value: 1.46e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHYDTRKDVEIyKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIInDSHNLKDVNLKWWRSKI 462
Cdd:PRK13632    8 IKVENVSFSYPNSENNAL-KNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKI-DGITISKENLKEIRKKI 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  463 GVVSQDP--LLFSNSIKNNIKYSLyslkdlealsEESNEDgfssqsdsnsrnscrakcagdlndmiqttdsteliqvRKN 540
Cdd:PRK13632   86 GIIFQNPdnQFIGATVEDDIAFGL----------ENKKVP-------------------------------------PKK 118
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  541 YETIedseVVSVSKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQK 620
Cdd:PRK13632  119 MKDI----IDDLAKKVGMEDYLDKEP-----------QNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKK 183
                         250       260       270
                  ....*....|....*....|....*....|....
gi 156095386  621 TINNLKGNENRITIIIAHRLSTIRYANTIFVLSN 654
Cdd:PRK13632  184 IMVDLRKTRKKTLISITHDMDEAILADKVIVFSE 217
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
1184-1428 1.53e-24

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: 106.29  E-value: 1.53e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1184 DLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfKNEQTgesskeqmqqgdeeqnvgmknanefssskega 1263
Cdd:COG0444    23 GVSFDVRRGETLGLVGESGSGKSTLARAILGLLP---------PPGIT-------------------------------- 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1264 dgqsstlfknSGKILLDGVDICDYNLKDLRNL----FSIVSQEPML-FN--MSIYENI-------KFGKENATREDVK-- 1327
Cdd:COG0444    62 ----------SGEILFDGEDLLKLSEKELRKIrgreIQMIFQDPMTsLNpvMTVGDQIaeplrihGGLSKAEARERAIel 131
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1328 -RACKFAAIDEFIESLPNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKA 1406
Cdd:COG0444   132 lERVGLPDPERRLDRYPHE-----------LSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQREL 200
                         250       260
                  ....*....|....*....|...
gi 156095386 1407 DKTIITIAHRIASIKR-SDKIVV 1428
Cdd:COG0444   201 GLAILFITHDLGVVAEiADRVAV 223
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
1164-1449 2.40e-24

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: 103.53  E-value: 2.40e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYLSRPnvPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYdlkndhhivfknEQTgesskeqmqqgd 1243
Cdd:cd03295     1 IEFENVTKRYGGGK--KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLI------------EPT------------ 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 eeqnvgmknanefssskegadgqsstlfknSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLF-NMSIYENIKFgkeNAT 1322
Cdd:cd03295    55 ------------------------------SGEIFIDGEDIREQDPVELRRKIGYVIQQIGLFpHMTVEENIAL---VPK 101
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1323 REDVKRACKFAAIDEFIESL---PNQYdtnVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTI 1399
Cdd:cd03295   102 LLKWPKEKIRERADELLALVgldPAEF---ADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLQEEF 178
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 156095386 1400 VDIKDKADKTIITIAHRI-ASIKRSDKIVVFNNpdrtGSFVQaQGTHEELL 1449
Cdd:cd03295   179 KRLQQELGKTIVFVTHDIdEAFRLADRIAIMKN----GEIVQ-VGTPDEIL 224
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
383-613 2.53e-24

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


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 106.31  E-value: 2.53e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHYDtrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDshnlKDVN-LKWWRSK 461
Cdd:COG3839     4 LELENVSKSYG---GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGG----RDVTdLPPKDRN 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  462 IGVVSQDPLLFSN-SIKNNIKYSLyslkdlealseesnedgfssqsdsnsrnscraKCAGdlndmiqttdsteliqVRKn 540
Cdd:COG3839    77 IAMVFQSYALYPHmTVYENIAFPL--------------------------------KLRK----------------VPK- 107
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 156095386  541 yETIeDSEVVSVSKKVLIHDFVsalpDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNK 613
Cdd:COG3839   108 -AEI-DRRVREAAELLGLEDLL----DRK-------PKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLDAK 167
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
383-613 2.91e-24

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 105.95  E-value: 2.91e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHYDtrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDshnlKDV-NLKWWRSK 461
Cdd:COG3842     6 LELENVSKRYG---DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDG----RDVtGLPPEKRN 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  462 IGVVSQDPLLFSN-SIKNNIKYSLySLKDLEAlsEEsnedgfssqsdsnsrnscRAKCAGDLNDMIQttdsteliqvrkn 540
Cdd:COG3842    79 VGMVFQDYALFPHlTVAENVAFGL-RMRGVPK--AE------------------IRARVAELLELVG------------- 124
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 156095386  541 yetiedsevvsvskkvlihdfVSALPDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNK 613
Cdd:COG3842   125 ---------------------LEGLADRY-------PHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAK 169
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
1273-1448 3.07e-24

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: 103.09  E-value: 3.07e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1273 NSGKILLDGVDIcdYNLKDLRNLFSIVSQEPMLF-NMSIYENIKFG------KENATREDVKRACKFAAIDEFIESLPNQ 1345
Cdd:cd03300    53 TSGEILLDGKDI--TNLPPHKRPVNTVFQNYALFpHLTVFENIAFGlrlkklPKAEIKERVAEALDLVQLEGYANRKPSQ 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1346 ydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSnseKLIEKTIVDIKDKADK---TIITIAH-RIASIK 1421
Cdd:cd03300   131 -----------LSGGQQQRVAIARALVNEPKVLLLDEPLGALDL---KLRKDMQLELKRLQKElgiTFVFVTHdQEEALT 196
                         170       180
                  ....*....|....*....|....*..
gi 156095386 1422 RSDKIVVFNNpdrtGSFVQAqGTHEEL 1448
Cdd:cd03300   197 MSDRIAVMNK----GKIQQI-GTPEEI 218
cbiO PRK13650
energy-coupling factor transporter ATPase;
1164-1450 3.33e-24

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 104.04  E-value: 3.33e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYLSRPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfkneqtgesskeqmqqgd 1243
Cdd:PRK13650    5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLI------------------------------- 53
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 eeqnvgmknanefssskegaDGqssTLFKNSGKILLDGVDICDYNLKDLRNLFSIVSQEP--MLFNMSIYENIKFGKENA 1321
Cdd:PRK13650   54 --------------------DG---LLEAESGQIIIDGDLLTEENVWDIRHKIGMVFQNPdnQFVGATVEDDVAFGLENK 110
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1322 ------TREDVKRACKFAAIDEFIESLPNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLI 1395
Cdd:PRK13650  111 gipheeMKERVNEALELVGMQDFKEREPAR-----------LSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLEL 179
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 156095386 1396 EKTIVDIKDKADKTIITIAHRIASIKRSDKIVVFNNPDrtgsfVQAQGTHEELLS 1450
Cdd:PRK13650  180 IKTIKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQ-----VESTSTPRELFS 229
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
1164-1450 8.18e-24

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: 101.89  E-value: 8.18e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYLSRPN-VPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfkneqtgesskeqmqqg 1242
Cdd:cd03258     2 IELKNVSKVFGDTGGkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCI------------------------------ 51
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1243 deeqnvgmkNANEFSSSkegadgqsstlfknsGKILLDGVDICDYNLKDLRNL---FSIVSQEPMLFN-MSIYENIKFGK 1318
Cdd:cd03258    52 ---------NGLERPTS---------------GSVLVDGTDLTLLSGKELRKArrrIGMIFQHFNLLSsRTVFENVALPL 107
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1319 ENATREDVKRACKfaaIDEFIEsLPNQYDtNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKT 1398
Cdd:cd03258   108 EIAGVPKAEIEER---VLELLE-LVGLED-KADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILAL 182
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 156095386 1399 IVDIKDKADKTIITIAHRIASIKR-SDKIVVFNNpdrtGSFVQaQGTHEELLS 1450
Cdd:cd03258   183 LRDINRELGLTIVLITHEMEVVKRiCDRVAVMEK----GEVVE-EGTVEEVFA 230
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
1165-1431 1.15e-23

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: 100.69  E-value: 1.15e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1165 EIMDVNFRYlsrPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMrfydlkndhhivfkneqtgesskeqmqqgde 1244
Cdd:cd03235     1 EVEDLTVSY---GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAIL------------------------------- 46
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1245 eqnvgmknanefssskegadGQsstLFKNSGKILLDGvdicdYNLKDLRNLFSIVSQEPML---FNMSIYENIKFGKEN- 1320
Cdd:cd03235    47 --------------------GL---LKPTSGSIRVFG-----KPLEKERKRIGYVPQRRSIdrdFPISVRDVVLMGLYGh 98
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1321 ---------ATREDVKRACKFAAIDEFIeslpnqyDTNVGpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNS 1391
Cdd:cd03235    99 kglfrrlskADKAKVDEALERVGLSELA-------DRQIG----ELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKT 167
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 156095386 1392 EKLIEKTIVDIKDKaDKTIITIAHRI-ASIKRSDKIVVFNN 1431
Cdd:cd03235   168 QEDIYELLRELRRE-GMTILVVTHDLgLVLEYFDRVLLLNR 207
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
383-652 1.29e-23

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: 103.59  E-value: 1.29e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHYDTRK-DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDP---TEGDVIIN--DSHNLKDVNLK 456
Cdd:COG0444     2 LEVRNLKVYFPTRRgVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDgeDLLKLSEKELR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  457 WWRSK-IGVVSQDPllfsnsiknnikyslyslkdlealseesnedgFSSqsdsnsrnscrakcagdLN------DMIqtt 529
Cdd:COG0444    82 KIRGReIQMIFQDP--------------------------------MTS-----------------LNpvmtvgDQI--- 109
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  530 dsTELIQVRKNYETIE-DSEVVSVSKKVLIHDFVSALpDKY--EtlvgsnaskLSGGQKQRISIARAIIRNPKILILDEA 606
Cdd:COG0444   110 --AEPLRIHGGLSKAEaRERAIELLERVGLPDPERRL-DRYphE---------LSGGMRQRVMIARALALEPKLLIADEP 177
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 156095386  607 TSSLDnkseYLVQKTI----NNLKgNENRITII-IAHRLSTIRY-ANTIFVL 652
Cdd:COG0444   178 TTALD----VTIQAQIlnllKDLQ-RELGLAILfITHDLGVVAEiADRVAVM 224
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
1164-1431 1.35e-23

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


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 104.07  E-value: 1.35e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYlsrPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfkneqtgesskeqmqqgd 1243
Cdd:COG1118     3 IEVRNISKRF---GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRII------------------------------- 48
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 eeqnVGMknanefssskEGADgqsstlfknSGKILLDGVDIcDYNL--KDlRNL-FsiVSQEPMLF-NMSIYENIKFG-- 1317
Cdd:COG1118    49 ----AGL----------ETPD---------SGRIVLNGRDL-FTNLppRE-RRVgF--VFQHYALFpHMTVAENIAFGlr 101
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1318 ----KENATREDVKRACKFAAIDEFIESLPNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEK 1393
Cdd:COG1118   102 vrppSKAEIRARVEELLELVQLEGLADRYPSQ-----------LSGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRK 170
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 156095386 1394 LIEKTIVDIKDKADKTIITIAH------RIAsikrsDKIVVFNN 1431
Cdd:COG1118   171 ELRRWLRRLHDELGGTTVFVTHdqeealELA-----DRVVVMNQ 209
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
383-664 1.59e-23

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: 101.11  E-value: 1.59e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHYDTrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDS--HNLKDVNLKWWRS 460
Cdd:cd03256     1 IEVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTdiNKLKGKALRQLRR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  461 KIGVVSQDPLLFSNS--IKNnikyslyslkdleALSeesnedgfssqsdsnsrnscrakcaGDLNDMiqttdstELIQVR 538
Cdd:cd03256    79 QIGMIFQQFNLIERLsvLEN-------------VLS-------------------------GRLGRR-------STWRSL 113
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  539 KNYETIEDSEV-VSVSKKVLIHDFVSAlpdkyetlvgsNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYL 617
Cdd:cd03256   114 FGLFPKEEKQRaLAALERVGLLDKAYQ-----------RADQLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQ 182
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 156095386  618 VQKTINNLKGNENRITIIIAHRLSTIR-YANTIFVLSNRE---NGSTVDVD 664
Cdd:cd03256   183 VMDLLKRINREEGITVIVSLHQVDLAReYADRIVGLKDGRivfDGPPAELT 233
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
1164-1431 2.66e-23

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: 98.24  E-value: 2.66e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYlsrPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFydLKNDhhivfkneqtgesskeqmqqgd 1243
Cdd:cd03230     1 IEVRNLSKRY---GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGL--LKPD---------------------- 53
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 eeqnvgmknanefssskegadgqsstlfknSGKILLDGVDICDyNLKDLRNLFSIVSQEPMLF-NMSIYENIKfgkenat 1322
Cdd:cd03230    54 ------------------------------SGEIKVLGKDIKK-EPEEVKRRIGYLPEEPSLYeNLTVRENLK------- 95
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1323 redvkrackfaaidefieslpnqydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDI 1402
Cdd:cd03230    96 ----------------------------------LSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLREL 141
                         250       260       270
                  ....*....|....*....|....*....|
gi 156095386 1403 KDKaDKTIITIAHRIASI-KRSDKIVVFNN 1431
Cdd:cd03230   142 KKE-GKTILLSSHILEEAeRLCDRVAILNN 170
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
1163-1450 3.68e-23

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 101.25  E-value: 3.68e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1163 KIEIMDVNFRY--LSRPNVpiyKDLTFSCESKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfkneqtgesskeqmq 1240
Cdd:PRK13635    5 IIRVEHISFRYpdAATYAL---KDVSFSVYEGEWVAIVGHNGSGKSTLAKLL---------------------------- 53
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1241 qgdeeqnvgmknanefssskegaDGqssTLFKNSGKILLDGVDICDYNLKDLRNLFSIVSQEP--MLFNMSIYENIKFGK 1318
Cdd:PRK13635   54 -----------------------NG---LLLPEAGTITVGGMVLSEETVWDVRRQVGMVFQNPdnQFVGATVQDDVAFGL 107
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1319 EN--ATRED----VKRACKFAAIDEFIESLPNqydtnvgpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSE 1392
Cdd:PRK13635  108 ENigVPREEmverVDQALRQVGMEDFLNREPH-----------RLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGR 176
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 156095386 1393 KLIEKTIVDIKDKADKTIITIAHRIASIKRSDKIVVFNNPDrtgsfVQAQGTHEELLS 1450
Cdd:PRK13635  177 REVLETVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGE-----ILEEGTPEEIFK 229
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
1164-1431 7.11e-23

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: 98.48  E-value: 7.11e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYlsrPNVPIYKDLTFSCESKKTTAIVGETGSGKSTvmslLMRfydlkndhhivfkneqtgesskeqMQQGD 1243
Cdd:cd03301     1 VELENVTKRF---GNVTALDDLNLDIADGEFVVLLGPSGCGKTT----TLR------------------------MIAGL 49
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 EEqnvgmknanefssskegadgqsstlfKNSGKILLDGVDICDYNLKDlRNLfSIVSQEPMLF-NMSIYENIKFG----- 1317
Cdd:cd03301    50 EE--------------------------PTSGRIYIGGRDVTDLPPKD-RDI-AMVFQNYALYpHMTVYDNIAFGlklrk 101
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1318 -KENATREDVKRACKFAAIDEFIESLPNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSnseKLIE 1396
Cdd:cd03301   102 vPKDEIDERVREVAELLQIEHLLDRKPKQ-----------LSGGQRQRVALGRAIVREPKVFLMDEPLSNLDA---KLRV 167
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 156095386 1397 KT---IVDIKDKADKTIITIAH-RIASIKRSDKIVVFNN 1431
Cdd:cd03301   168 QMraeLKRLQQRLGTTTIYVTHdQVEAMTMADRIAVMND 206
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
383-611 7.73e-23

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


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 98.91  E-value: 7.73e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHYDtrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDSH-NLKDVNLKWWRSK 461
Cdd:COG1126     2 IEIENLHKSFG---DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDlTDSKKDINKLRRK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  462 IGVVSQDPLLFSN-SIKNNIkyslyslkdLEALseesnedgfssqsdsnsrnscrakcagdlndmiqttdstelIQVRKn 540
Cdd:COG1126    79 VGMVFQQFNLFPHlTVLENV---------TLAP-----------------------------------------IKVKK- 107
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156095386  541 yetIEDSEVVSVSKKVL----IHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:COG1126   108 ---MSKAEAEERAMELLervgLADKADAYP-----------AQLSGGQQQRVAIARALAMEPKVMLFDEPTSALD 168
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
1163-1434 1.03e-22

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


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 99.39  E-value: 1.03e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1163 KIEIMDVNFRYLSRPN-VPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMrfydlkndhhivfkneqtgesskeqmqq 1241
Cdd:COG1116     7 ALELRGVSKRFPTGGGgVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIA---------------------------- 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1242 gdeeqnvgmknanefssskeGADGQSStlfknsGKILLDGVDIcdynlKDLRNLFSIVSQEPMLFN-MSIYENIKFGKEN 1320
Cdd:COG1116    59 --------------------GLEKPTS------GEVLVDGKPV-----TGPGPDRGVVFQEPALLPwLTVLDNVALGLEL 107
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1321 A---TREDVKRACKFAAI---DEFIESLPNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKL 1394
Cdd:COG1116   108 RgvpKAERRERARELLELvglAGFEDAYPHQ-----------LSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRER 176
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 156095386 1395 IEKTIVDIKDKADKTIITIAHRIA-SIKRSDKIVVF-NNPDR 1434
Cdd:COG1116   177 LQDELLRLWQETGKTVLFVTHDVDeAVFLADRVVVLsARPGR 218
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
1164-1450 1.14e-22

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 98.62  E-value: 1.14e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYlsrPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFydLKNDhhivfkneqtgesskeqmqqgd 1243
Cdd:COG1121     7 IELENLTVSY---GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGL--LPPT---------------------- 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 eeqnvgmknanefssskegadgqsstlfknSGKILLDGVDIcdynlKDLRNLFSIVSQE-------PM----LFNMSIYE 1312
Cdd:COG1121    60 ------------------------------SGTVRLFGKPP-----RRARRRIGYVPQRaevdwdfPItvrdVVLMGRYG 104
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1313 NIKFGKeNATREDVKRAckFAAIDEF-IESLPNQydtnvgPYGkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNS 1391
Cdd:COG1121   105 RRGLFR-RPSRADREAV--DEALERVgLEDLADR------PIG-ELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAAT 174
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1392 EKLIEKTIVDIKdKADKTIITIAHRIASIKR-SDKIVVFNnpdRTgsfVQAQGTHEELLS 1450
Cdd:COG1121   175 EEALYELLRELR-REGKTILVVTHDLGAVREyFDRVLLLN---RG---LVAHGPPEEVLT 227
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
398-652 1.37e-22

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: 97.75  E-value: 1.37e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  398 VEIYKDL-NFTL-----TEGKTYAFVGESGCGKSTILKLIERLYDPTEG-----DVIINDSHnlKDVNLKWWRSKIGVVS 466
Cdd:cd03297     4 VDIEKRLpDFTLkidfdLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGtivlnGTVLFDSR--KKINLPPQQRKIGLVF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  467 QDPLLFSN-SIKNNIKYSLYSLKDLEalseesnedgfssqsdsnsrnscrakcagdlnDMIQTTDSTELIQVrknyetie 545
Cdd:cd03297    82 QQYALFPHlNVRENLAFGLKRKRNRE--------------------------------DRISVDELLDLLGL-------- 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  546 dsevvsvskkvlihdfvsalpdkyETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNL 625
Cdd:cd03297   122 ------------------------DHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQI 177
                         250       260
                  ....*....|....*....|....*...
gi 156095386  626 KGNENRITIIIAHRLSTIRY-ANTIFVL 652
Cdd:cd03297   178 KKNLNIPVIFVTHDLSEAEYlADRIVVM 205
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
383-611 1.47e-22

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: 97.60  E-value: 1.47e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHYDTRkdvEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIIND-SHNLKDVNLKWWRSK 461
Cdd:cd03262     1 IEIKNLHKSFGDF---HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGlKLTDDKKNINELRQK 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  462 IGVVSQDPLLFSN-SIKNNIKYSlyslkdlealseesnedgfssqsdsnsrnscrakcagdlndmiqttdsteLIQVRKn 540
Cdd:cd03262    78 VGMVFQQFNLFPHlTVLENITLA--------------------------------------------------PIKVKG- 106
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156095386  541 yetIEDSEVVSVS----KKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:cd03262   107 ---MSKAEAEERAlellEKVGLADKADAYP-----------AQLSGGQQQRVAIARALAMNPKVMLFDEPTSALD 167
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
383-638 1.47e-22

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: 97.33  E-value: 1.47e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHYDTRKDVeiyKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDshnlKDVN-LKWWRSK 461
Cdd:cd03301     1 VELENVTKRFGNVTAL---DDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGG----RDVTdLPPKDRD 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  462 IGVVSQDPLLFSN-SIKNNIKYSLyslkdlealseesnedgfssqsdsnsrnscrakcagdlndmiqttdsteliQVRKN 540
Cdd:cd03301    74 IAMVFQNYALYPHmTVYDNIAFGL---------------------------------------------------KLRKV 102
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  541 YETIEDSEVVSVSKKVLIhdfvSALPDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQK 620
Cdd:cd03301   103 PKDEIDERVREVAELLQI----EHLLDRK-------PKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQMRA 171
                         250
                  ....*....|....*...
gi 156095386  621 TINNLKGNENRITIIIAH 638
Cdd:cd03301   172 ELKRLQQRLGTTTIYVTH 189
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
1274-1449 1.49e-22

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: 99.26  E-value: 1.49e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1274 SGKILLDGVDICDYNLKDLRNL----FSIVSQEPMLF-NMSIYENIKFGKE------NATREDVKRACKFAAIDEFIESL 1342
Cdd:cd03294    78 SGKVLIDGQDIAAMSRKELRELrrkkISMVFQSFALLpHRTVLENVAFGLEvqgvprAEREERAAEALELVGLEGWEHKY 157
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1343 PNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIA-SIK 1421
Cdd:cd03294   158 PDE-----------LSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDeALR 226
                         170       180
                  ....*....|....*....|....*...
gi 156095386 1422 RSDKIVVFnnpdRTGSFVQAqGTHEELL 1449
Cdd:cd03294   227 LGDRIAIM----KDGRLVQV-GTPEEIL 249
cbiO PRK13640
energy-coupling factor transporter ATPase;
1164-1450 1.54e-22

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 99.49  E-value: 1.54e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYLSRPnVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMrfydlkndhhivfkneqtgesskeqmqqgd 1243
Cdd:PRK13640    6 VEFKHVSFTYPDSK-KPALNDISFSIPRGSWTALIGHNGSGKSTISKLIN------------------------------ 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 eeqnvGMKNANEFSSSKegadgqsstlfknsgkILLDGVDICDYNLKDLRNLFSIVSQEP--MLFNMSIYENIKFGKEN- 1320
Cdd:PRK13640   55 -----GLLLPDDNPNSK----------------ITVDGITLTAKTVWDIREKVGIVFQNPdnQFVGATVGDDVAFGLENr 113
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1321 -ATREDVKRACKFAAID----EFIESLPnqydtnvgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLI 1395
Cdd:PRK13640  114 aVPRPEMIKIVRDVLADvgmlDYIDSEP-----------ANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQI 182
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 156095386 1396 EKTIVDIKDKADKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVqAQGTHEELLS 1450
Cdd:PRK13640  183 LKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDD----GKLL-AQGSPVEIFS 232
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
384-655 1.88e-22

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: 97.22  E-value: 1.88e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  384 QFKNVRFHYDTRkdvEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDSHNLKDvnlkwwRSKIG 463
Cdd:cd03235     1 EVEDLTVSYGGH---PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE------RKRIG 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  464 VVSQdpllfsnsiknnikySLYSLKDLEALSEESNEDGFSSQSDSNSRNSCRAKCAGDlnDMIQTTDSTELIQvrknyet 543
Cdd:cd03235    72 YVPQ---------------RRSIDRDFPISVRDVVLMGLYGHKGLFRRLSKADKAKVD--EALERVGLSELAD------- 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  544 iedsevvsvskkvlihdfvsalpdkyetlvgSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTIN 623
Cdd:cd03235   128 -------------------------------RQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLR 176
                         250       260       270
                  ....*....|....*....|....*....|...
gi 156095386  624 NLKGnENRITIIIAHRLSTI-RYANTIFVLSNR 655
Cdd:cd03235   177 ELRR-EGMTILVVTHDLGLVlEYFDRVLLLNRT 208
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
1183-1439 3.31e-22

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 97.54  E-value: 3.31e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1183 KDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDLKNDHHIvfkneqTGEsskeqmqqgdeeqnVGMKNANEFSSSKeg 1262
Cdd:PRK14239   22 NSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTI------TGS--------------IVYNGHNIYSPRT-- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1263 adgqsstlfknsgkillDGVDicdynlkdLRNLFSIVSQEPMLFNMSIYENIKFG------KENAT-REDVKRACKFAAI 1335
Cdd:PRK14239   80 -----------------DTVD--------LRKEIGMVFQQPNPFPMSIYENVVYGlrlkgiKDKQVlDEAVEKSLKGASI 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1336 -DEFIESLpnqYDTNVGpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkaDKTIITIA 1414
Cdd:PRK14239  135 wDEVKDRL---HDSALG-----LSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKD--DYTMLLVT 204
                         250       260
                  ....*....|....*....|....*
gi 156095386 1415 HriaSIKRSDKIvvfnnPDRTGSFV 1439
Cdd:PRK14239  205 R---SMQQASRI-----SDRTGFFL 221
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
1162-1448 4.70e-22

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


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 99.38  E-value: 4.70e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1162 GKIEIMDVNFRYlsrPNVPIYKDLTFSCESKKTTAIVGETGSGKSTvmslLMRfydlkndhhivfkneqtgesskeqMQQ 1241
Cdd:COG3839     2 ASLELENVSKSY---GGVEALKDIDLDIEDGEFLVLLGPSGCGKST----LLR------------------------MIA 50
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1242 GDEEQNvgmknanefssskegadgqsstlfknSGKILLDGVDICDYNLKDlRNLfSIVSQEPMLF-NMSIYENIKFGKEN 1320
Cdd:COG3839    51 GLEDPT--------------------------SGEILIGGRDVTDLPPKD-RNI-AMVFQSYALYpHMTVYENIAFPLKL 102
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1321 A--TREDVKRACKFAA----IDEFIESLPNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSnseKL 1394
Cdd:COG3839   103 RkvPKAEIDRRVREAAellgLEDLLDRKPKQ-----------LSGGQRQRVALGRALVREPKVFLLDEPLSNLDA---KL 168
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156095386 1395 IEKTIVDIKD---KADKTII----------TIAhriasikrsDKIVVFNNpdrtGSFVQaQGTHEEL 1448
Cdd:COG3839   169 RVEMRAEIKRlhrRLGTTTIyvthdqveamTLA---------DRIAVMND----GRIQQ-VGTPEEL 221
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
383-655 9.70e-22

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 95.93  E-value: 9.70e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHYDTRkdvEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDSHNLKDvnlkwwRSKI 462
Cdd:COG1121     7 IELENLTVSYGGR---PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA------RRRI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  463 GVVSQdpllfsnsiknnikyslyslkdlealSEESNED--------------------GFSSQSDsnsrnscRAKCAgdl 522
Cdd:COG1121    78 GYVPQ--------------------------RAEVDWDfpitvrdvvlmgrygrrglfRRPSRAD-------REAVD--- 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  523 nDMIQTTDSTELiqvrknyetiedsevvsvsKKVLIhdfvsalpdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILI 602
Cdd:COG1121   122 -EALERVGLEDL-------------------ADRPI-------------------GELSGGQQQRVLLARALAQDPDLLL 162
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 156095386  603 LDEATSSLDNKSEYLVQKTINNLkgNENRITIIIA-HRLSTIR-YANTIFVLSNR 655
Cdd:COG1121   163 LDEPFAGVDAATEEALYELLREL--RREGKTILVVtHDLGAVReYFDRVLLLNRG 215
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
1183-1439 1.04e-21

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 100.48  E-value: 1.04e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1183 KDLTFSCESKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfkneqTGesskeqMQQGDeeqnvgmknanefssskeg 1262
Cdd:COG1129    21 DGVSLELRPGEVHALLGENGAGKSTLMKIL------------------SG------VYQPD------------------- 57
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1263 adgqsstlfknSGKILLDGVDICDYNLKDLRNL-FSIVSQEPMLF-NMSIYENIKFGKENATREDVKRACKFAAIDEFIE 1340
Cdd:COG1129    58 -----------SGEILLDGEPVRFRSPRDAQAAgIAIIHQELNLVpNLSVAENIFLGREPRRGGLIDWRAMRRRARELLA 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1341 SL-----PnqyDTNVGpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSN-SEKLIEkTIVDIKDKaDKTIITIA 1414
Cdd:COG1129   127 RLgldidP---DTPVG----DLSVAQQQLVEIARALSRDARVLILDEPTASLTEReVERLFR-IIRRLKAQ-GVAIIYIS 197
                         250       260
                  ....*....|....*....|....*.
gi 156095386 1415 HRIASIKR-SDKIVVFnnpdRTGSFV 1439
Cdd:COG1129   198 HRLDEVFEiADRVTVL----RDGRLV 219
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
386-663 1.07e-21

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: 100.91  E-value: 1.07e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  386 KNVRFHYDTRK--------DVEIYKDLNFTLTEGKTYAFVGESGCGKST----ILKLIerlydPTEGDVIINDS--HNLK 451
Cdd:COG4172   279 RDLKVWFPIKRglfrrtvgHVKAVDGVSLTLRRGETLGLVGESGSGKSTlglaLLRLI-----PSEGEIRFDGQdlDGLS 353
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  452 DVNLKWWRSKIGVVSQDPllfsnsiknnikyslYSlkdleALS-----EESNEDGFSSQSDSNSRNSCRAKCAgdlndmi 526
Cdd:COG4172   354 RRALRPLRRRMQVVFQDP---------------FG-----SLSprmtvGQIIAEGLRVHGPGLSAAERRARVA------- 406
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  527 qttdsteliqvrknyETIEDsevVSVSKKVL---IHDFvsalpdkyetlvgsnasklSGGQKQRISIARAIIRNPKILIL 603
Cdd:COG4172   407 ---------------EALEE---VGLDPAARhryPHEF-------------------SGGQRQRIAIARALILEPKLLVL 449
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156095386  604 DEATSSLDnKSeylVQKTINNLKGN---ENRIT-IIIAHRLSTIRY-ANTIFVLSN-R--ENGSTVDV 663
Cdd:COG4172   450 DEPTSALD-VS---VQAQILDLLRDlqrEHGLAyLFISHDLAVVRAlAHRVMVMKDgKvvEQGPTEQV 513
cbiO PRK13637
energy-coupling factor transporter ATPase;
1164-1431 1.29e-21

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 96.66  E-value: 1.29e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYLsrPNVPIYK----DLTFSCESKKTTAIVGETGSGKSTVMsllmrfydlkndHHIvfkneqtgesskeqm 1239
Cdd:PRK13637    3 IKIENLTHIYM--EGTPFEKkaldNVNIEIEDGEFVGLIGHTGSGKSTLI------------QHL--------------- 53
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1240 qqgdeeqnvgmknanefssskegadgqSSTLFKNSGKILLDGVDICD--YNLKDLRNLFSIVSQEP--MLFNMSIYENIK 1315
Cdd:PRK13637   54 ---------------------------NGLLKPTSGKIIIDGVDITDkkVKLSDIRKKVGLVFQYPeyQLFEETIEKDIA 106
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1316 FGKENATRED------VKRACKFAAIDefieslpnqYDT--NVGPYgkSLSGGQKQRIAIARALLREPKILLLDEATSSL 1387
Cdd:PRK13637  107 FGPINLGLSEeeienrVKRAMNIVGLD---------YEDykDKSPF--ELSGGQKRRVAIAGVVAMEPKILILDEPTAGL 175
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 156095386 1388 DSNSEKLIEKTIVDIKDKADKTIITIAHRIASI-KRSDKIVVFNN 1431
Cdd:PRK13637  176 DPKGRDEILNKIKELHKEYNMTIILVSHSMEDVaKLADRIIVMNK 220
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
383-656 1.61e-21

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: 95.45  E-value: 1.61e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHY-DTRKDVeiyKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDShNLKDVNLKWWRSK 461
Cdd:cd03295     1 IEFENVTKRYgGGKKAV---NNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGE-DIREQDPVELRRK 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  462 IGVVSQDPLLFSN-SIKNNIKyslySLKDLEALSEESNEDgfssqsdsnsrnscRAKcagdlndmiqttdstELIQvrkn 540
Cdd:cd03295    77 IGYVIQQIGLFPHmTVEENIA----LVPKLLKWPKEKIRE--------------RAD---------------ELLA---- 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  541 yetiedsevvsvskkvLIHdfvsaLPDkyETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQK 620
Cdd:cd03295   120 ----------------LVG-----LDP--AEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLQE 176
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 156095386  621 TINNLKGNENRITIIIAHRL-STIRYANTIFVLSNRE 656
Cdd:cd03295   177 EFKRLQQELGKTIVFVTHDIdEAFRLADRIAIMKNGE 213
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
1156-1455 1.88e-21

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 95.97  E-value: 1.88e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1156 NSNDIkgkIEIMDVNFRYLSRPNVPIyKDLTFSCESKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfkneqtgess 1235
Cdd:PRK13648    3 DKNSI---IVFKNVSFQYQSDASFTL-KDVSFNIPKGQWTSIVGHNGSGKSTIAKLM----------------------- 55
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1236 keqmqqgdeeqnVGMKNANEfssskegadgqsstlfknsGKILLDGVDICDYNLKDLRNLFSIVSQEP-MLFNMSIYE-N 1313
Cdd:PRK13648   56 ------------IGIEKVKS-------------------GEIFYNNQAITDDNFEKLRKHIGIVFQNPdNQFVGSIVKyD 104
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1314 IKFGKENAT------REDVKRACKFAAIDEFIESLPNqydtnvgpygkSLSGGQKQRIAIARALLREPKILLLDEATSSL 1387
Cdd:PRK13648  105 VAFGLENHAvpydemHRRVSEALKQVDMLERADYEPN-----------ALSGGQKQRVAIAGVLALNPSVIILDEATSML 173
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156095386 1388 DSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKRSDKIVVFNNPDrtgsfVQAQGTHEELLSVQDGV 1455
Cdd:PRK13648  174 DPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGT-----VYKEGTPTEIFDHAEEL 236
PTZ00243 PTZ00243
ABC transporter; Provisional
1162-1431 2.26e-21

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 101.78  E-value: 2.26e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1162 GKIEIMDVNFRYlsRPNVP-IYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfkneqtgesskeqmq 1240
Cdd:PTZ00243 1307 GSLVFEGVQMRY--REGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEV---------------------- 1362
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1241 qgdeeqnvgmknanefssskegadgqsstlfkNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEn 1320
Cdd:PTZ00243 1363 --------------------------------CGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVDPFLE- 1409
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1321 ATREDVKRACKFAAIDEFIESLPNQYDTNVGPYGKSLSGGQKQRIAIARALL-REPKILLLDEATSSLDSNSEKLIEKTI 1399
Cdd:PTZ00243 1410 ASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLkKGSGFILMDEATANIDPALDRQIQATV 1489
                         250       260       270
                  ....*....|....*....|....*....|..
gi 156095386 1400 vdIKDKADKTIITIAHRIASIKRSDKIVVFNN 1431
Cdd:PTZ00243 1490 --MSAFSAYTVITIAHRLHTVAQYDKIIVMDH 1519
cbiO PRK13650
energy-coupling factor transporter ATPase;
383-660 2.56e-21

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 95.57  E-value: 2.56e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIInDSHNLKDVNLKWWRSKI 462
Cdd:PRK13650    5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIII-DGDLLTEENVWDIRHKI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  463 GVVSQDPllfSNSIknnikyslyslkdLEALSEESNEDGFSSQsdsnsrnscrakcAGDLNDMIQTTDsteliqvrknye 542
Cdd:PRK13650   84 GMVFQNP---DNQF-------------VGATVEDDVAFGLENK-------------GIPHEEMKERVN------------ 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  543 tiEDSEVVSVSkkvlihDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI 622
Cdd:PRK13650  123 --EALELVGMQ------DFKEREP-----------ARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTI 183
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 156095386  623 NNLKgNENRITII-IAHRLSTIRYANTIFVLSNRENGST 660
Cdd:PRK13650  184 KGIR-DDYQMTVIsITHDLDEVALSDRVLVMKNGQVEST 221
ABC_6TM_TAP_ABCB8_10_like cd18557
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ...
826-1125 4.99e-21

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: 94.93  E-value: 4.99e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  826 AIIALSIMVAGGL-YPLFALLYAKYVGTLFDFANLeansNKYSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMKLRLF 904
Cdd:cd18557     1 GLLFLLISSAAQLlLPYLIGRLIDTIIKGGDLDVL----NELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLF 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  905 ENIMYQEISFFDQdsHAPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSTVMSFYFCPIVAAVLTGT---YFIFMR 981
Cdd:cd18557    77 SSLLRQEIAFFDK--HKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLViplLLIASK 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  982 VFAIRARiAANKDVEKK--RVNQpgtafvynsddeifkdpsfLIQEAFYNMNTVIIYGLEDY----FCTLIEKAIDYSnk 1055
Cdd:cd18557   155 IYGRYIR-KLSKEVQDAlaKAGQ-------------------VAEESLSNIRTVRSFSAEEKeirrYSEALDRSYRLA-- 212
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 156095386 1056 gqKRKTLINSMLWGFSQSAQFFINSFAYWFGSFLIRRGTIQVDD---FMksLFTFLFTGSYAG------KLMSLKGDSE 1125
Cdd:cd18557   213 --RKKALANALFQGITSLLIYLSLLLVLWYGGYLVLSGQLTVGEltsFI--LYTIMVASSVGGlssllaDIMKALGASE 287
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
383-637 5.43e-21

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: 92.86  E-value: 5.43e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHYDTrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIIN--DSHNLKDVNLKWWRS 460
Cdd:cd03292     1 IEFINVTKTYPN--GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNgqDVSDLRGRAIPYLRR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  461 KIGVVSQDPLLFSN-SIKNNIKYSLyslkdlealseesnedgfssqsdsnsrnscrakcagdlndmiqttdsteliqvrk 539
Cdd:cd03292    79 KIGVVFQDFRLLPDrNVYENVAFAL------------------------------------------------------- 103
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  540 nyetiedsEVVSVSKKvLIHDFVSA------LPDKYETLvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNK 613
Cdd:cd03292   104 --------EVTGVPPR-EIRKRVPAalelvgLSHKHRAL----PAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPD 170
                         250       260
                  ....*....|....*....|....
gi 156095386  614 SEYLVQKTINnlKGNENRITIIIA 637
Cdd:cd03292   171 TTWEIMNLLK--KINKAGTTVVVA 192
PLN03232 PLN03232
ABC transporter C family member; Provisional
100-653 5.85e-21

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 100.44  E-value: 5.85e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  100 IFSLVLIGIFQFILSFISSFCMDVVTTKILKTLKIEFLKSVFYQDGQFHDNNPGSKLtsdldfyLEQVNAGIGTKFITIF 179
Cdd:PLN03232  953 IVVYALLGFGQVAVTFTNSFWLISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRV-------INRFSKDIGDIDRNVA 1025
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  180 TYASAFLGLyIWSLFKNARL-----TLCITCVFPLI---YICGVICNKKVKINKKTSLLYNNNTMSIIEEALVGIRTVVS 251
Cdd:PLN03232 1026 NLMNMFMNQ-LWQLLSTFALigtvsTISLWAIMPLLilfYAAYLYYQSTSREVRRLDSVTRSPIYAQFGEALNGLSSIRA 1104
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  252 YcgentilKKFNLSEKLYSKYtlkanlmeslhigMING--FILASYAFGFWYGTRII------------ISDLSNQQPNN 317
Cdd:PLN03232 1105 Y-------KAYDRMAKINGKS-------------MDNNirFTLANTSSNRWLTIRLEtlggvmiwltatFAVLRNGNAEN 1164
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  318 DFHGGSVISILLGVLISmfmLTIILPNITEY-------MKSLEATNNLYEIINRKP-LVENNQDGKKLKDIKKIQFKNVR 389
Cdd:PLN03232 1165 QAGFASTMGLLLSYTLN---ITTLLSGVLRQaskaensLNSVERVGNYIDLPSEATaIIENNRPVSGWPSRGSIKFEDVH 1241
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  390 FHYdtRKDVE-IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDsHNLKDVNLKWWRSKIGVVSQD 468
Cdd:PLN03232 1242 LRY--RPGLPpVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDD-CDVAKFGLTDLRRVLSIIPQS 1318
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  469 PLLFSNSIKNNIkyslyslkdlealseesneDGFSSQSDSnsrnscrakcagDLndmiqttdsteliqvrknYETIEDSE 548
Cdd:PLN03232 1319 PVLFSGTVRFNI-------------------DPFSEHNDA------------DL------------------WEALERAH 1349
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  549 vvsvskkvlIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINnlkgN 628
Cdd:PLN03232 1350 ---------IKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIR----E 1416
                         570       580
                  ....*....|....*....|....*..
gi 156095386  629 ENR--ITIIIAHRLSTIRYANTIFVLS 653
Cdd:PLN03232 1417 EFKscTMLVIAHRLNTIIDCDKILVLS 1443
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
1164-1460 6.17e-21

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 94.33  E-value: 6.17e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYLSRPnvpIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDLKNDHHIvfkneqtgESSKEQMQQGD 1243
Cdd:PRK14258    8 IKVNNLSFYYDTQK---ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRV--------EGRVEFFNQNI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 EEQNVgmknanefssskegadgqsstlfknsgkilldgvdicdyNLKDLRNLFSIVSQEPMLFNMSIYENIKFG-KENAT 1322
Cdd:PRK14258   77 YERRV---------------------------------------NLNRLRRQVSMVHPKPNLFPMSVYDNVAYGvKIVGW 117
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1323 REDVKrackfaaIDEFIES------LPNQYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIE 1396
Cdd:PRK14258  118 RPKLE-------IDDIVESalkdadLWDEIKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVE 190
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156095386 1397 KTIVDIKDKADKTIITIAHRIASIKRSDKIVVF--NNPDRTGSFVQAQGTHEELLSVQDGVYKKYV 1460
Cdd:PRK14258  191 SLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFfkGNENRIGQLVEFGLTKKIFNSPHDSRTREYV 256
ABC_6TM_MsbA_like cd18552
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ...
62-309 9.29e-21

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: 94.41  E-value: 9.29e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   62 LGVSFVCATISGGTLPFFVSVFGVIMKNMNLGENVNDIIF-SLVLIGIF--QFILSFISSFCMDVVTTKILKTLKIEFLK 138
Cdd:cd18552     1 LALAILGMILVAATTAALAWLLKPLLDDIFVEKDLEALLLvPLAIIGLFllRGLASYLQTYLMAYVGQRVVRDLRNDLFD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  139 SVFYQDGQFHDNNPG----SKLTSDldfyLEQVNAGIGTKFITIFTYASAFLGLYIWSLFKNARLTLCITCVFPLIYICG 214
Cdd:cd18552    81 KLLRLPLSFFDRNSSgdliSRITND----VNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  215 VICNKKVKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGENTILKKFNLSEKLYSKYTLKANLMESLHIGMINgfILAS 294
Cdd:cd18552   157 RRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLME--LLGA 234
                         250
                  ....*....|....*..
gi 156095386  295 YAFGF--WYGTRIIISD 309
Cdd:cd18552   235 IAIALvlWYGGYQVISG 251
PhnC COG3638
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ...
383-636 1.17e-20

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


Pssm-ID: 442855 [Multi-domain]  Cd Length: 249  Bit Score: 92.81  E-value: 1.17e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHYDTrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIIN--DSHNLKDVNLKWWRS 460
Cdd:COG3638     3 LELRNLSKRYPG--GTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDgqDVTALRGRALRRLRR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  461 KIGVVSQDPLLFSNS--IKN----NIKY--------SLYSLKD----LEALSEesnedgfssqsdsnsrnscrakcagdl 522
Cdd:COG3638    81 RIGMIFQQFNLVPRLsvLTNvlagRLGRtstwrsllGLFPPEDreraLEALER--------------------------- 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  523 ndmiqttdsteliqvrknyetiedsevVSVSKKVLIHdfvsalpdkyetlvgsnASKLSGGQKQRISIARAIIRNPKILI 602
Cdd:COG3638   134 ---------------------------VGLADKAYQR-----------------ADQLSGGQQQRVAIARALVQEPKLIL 169
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 156095386  603 LDEATSSLDNKS-----EYLvqKTINnlkgNENRITIII 636
Cdd:COG3638   170 ADEPVASLDPKTarqvmDLL--RRIA----REDGITVVV 202
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
383-663 1.61e-20

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 94.87  E-value: 1.61e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHYDT-RKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIIN--DSHNLKDVNLKWWR 459
Cdd:PRK11153    2 IELKNISKVFPQgGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDgqDLTALSEKELRKAR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  460 SKIGVVSQD-PLLFSNSIKNNIKYSLyslkdlealseesnedgfssqsdsnsrnscraKCAGDLNDMIQTTdSTELIqvr 538
Cdd:PRK11153   82 RQIGMIFQHfNLLSSRTVFDNVALPL--------------------------------ELAGTPKAEIKAR-VTELL--- 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  539 knyetiedsEVVSVSKKVlihdfvsalpDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSeylv 618
Cdd:PRK11153  126 ---------ELVGLSDKA----------DRY-------PAQLSGGQKQRVAIARALASNPKVLLCDEATSALDPAT---- 175
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 156095386  619 QKTINNLKGNENR---ITII-IAHRLSTI-RYANTIFVLSNR---ENGSTVDV 663
Cdd:PRK11153  176 TRSILELLKDINRelgLTIVlITHEMDVVkRICDRVAVIDAGrlvEQGTVSEV 228
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
1165-1415 2.20e-20

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: 90.78  E-value: 2.20e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1165 EIMDVNFRYlsRPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMrfydlkndhhivfkneqtgesskeqmqqgde 1244
Cdd:cd03226     1 RIENISFSY--KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILA------------------------------- 47
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1245 eqnvGMKNanefssskegadgqsstlfKNSGKILLDGVDICdynLKDLRNLFSIVSQEP--MLFNMSIYENIKFGKENAT 1322
Cdd:cd03226    48 ----GLIK-------------------ESSGSILLNGKPIK---AKERRKSIGYVMQDVdyQLFTDSVREELLLGLKELD 101
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1323 R--EDVKRACKFAAIDEFIESLPnqydtnvgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIV 1400
Cdd:cd03226   102 AgnEQAETVLKDLDLYALKERHP-----------LSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIR 170
                         250
                  ....*....|....*
gi 156095386 1401 DIKdKADKTIITIAH 1415
Cdd:cd03226   171 ELA-AQGKAVIVITH 184
ABC_6TM_TAP_ABCB8_10_like cd18557
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ...
64-355 2.42e-20

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: 93.01  E-value: 2.42e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   64 VSFVCATISGGTLPFFVS-VFGVIMKNMNLgENVNDIIFSLVLIGIFQFILSFISSFCMDVVTTKILKTLKIEFLKSVFY 142
Cdd:cd18557     3 LFLLISSAAQLLLPYLIGrLIDTIIKGGDL-DVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  143 QDGQFHD-NNPG---SKLTSDLdfylEQVNAGIGTKFITIFTYASAFLGLYIWSLFKNARLTLCITCVFPLIYICGVICN 218
Cdd:cd18557    82 QEIAFFDkHKTGeltSRLSSDT----SVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  219 KKVKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGENTILKKFnlSEKLYSKYTL--KANLMESLHIGMINGFILASYA 296
Cdd:cd18557   158 RYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRY--SEALDRSYRLarKKALANALFQGITSLLIYLSLL 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 156095386  297 FGFWYGTRIIISdlsnqqpnNDFHGGSVISILLGVLISMFMLTIILPNITEYMKSLEAT 355
Cdd:cd18557   236 LVLWYGGYLVLS--------GQLTVGELTSFILYTIMVASSVGGLSSLLADIMKALGAS 286
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
385-619 3.06e-20

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 96.29  E-value: 3.06e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  385 FKNVRFHYDTRKdveIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINdshnlKDVnlkwwrsKIGV 464
Cdd:COG0488     1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP-----KGL-------RIGY 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  465 VSQDPLLFSN-SIKNNIKYSLYSLKDLEALSEESNEDGFSSQSDSNSrnscrakcAGDLNDMIQTTDSTELiqvrknyet 543
Cdd:COG0488    66 LPQEPPLDDDlTVLDTVLDGDAELRALEAELEELEAKLAEPDEDLER--------LAELQEEFEALGGWEA--------- 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  544 ieDSEVvsvsKKVLihdfvSAL---PDKYETLVGSnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS-----E 615
Cdd:COG0488   129 --EARA----EEIL-----SGLgfpEEDLDRPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESiewleE 193

                  ....
gi 156095386  616 YLVQ 619
Cdd:COG0488   194 FLKN 197
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
1164-1388 3.72e-20

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 90.97  E-value: 3.72e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYLSRPnvpiykdLTFSCESKK--TTAIVGETGSGKSTVMSLLMRFydlkndhhivfkneqtgesskeqmqq 1241
Cdd:COG3840     2 LRLDDLTYRYGDFP-------LRFDLTIAAgeRVAILGPSGAGKSTLLNLIAGF-------------------------- 48
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1242 gdeeqnvgmknanefssskegadgqsstLFKNSGKILLDGVDICDYNlKDLRnLFSIVSQEPMLFN-MSIYENIKFG--- 1317
Cdd:COG3840    49 ----------------------------LPPDSGRILWNGQDLTALP-PAER-PVSMLFQENNLFPhLTVAQNIGLGlrp 98
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156095386 1318 --KENAT-REDVKRACKFAAIDEFIESLPNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLD 1388
Cdd:COG3840    99 glKLTAEqRAQVEQALERVGLAGLLDRLPGQ-----------LSGGQRQRVALARCLVRKRPILLLDEPFSALD 161
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
1274-1432 5.99e-20

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 92.83  E-value: 5.99e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1274 SGKILLDGVDICDYNLKDLRNL---FSIVSQEpmlFN-MS---IYENIKF-----GKENATREdvKRackfaaIDEFIE- 1340
Cdd:COG1135    59 SGSVLVDGVDLTALSERELRAArrkIGMIFQH---FNlLSsrtVAENVALpleiaGVPKAEIR--KR------VAELLEl 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1341 --------SLPNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTI-- 1410
Cdd:COG1135   128 vglsdkadAYPSQ-----------LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIvl 196
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 156095386 1411 IT--------IAHRIASIKRSdKIV-------VFNNP 1432
Cdd:COG1135   197 IThemdvvrrICDRVAVLENG-RIVeqgpvldVFANP 232
ABCC_SUR2 cd03288
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...
382-664 6.58e-20

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: 91.12  E-value: 6.58e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  382 KIQFKNVRFHYDTRKDvEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIInDSHNLKDVNLKWWRSK 461
Cdd:cd03288    19 EIKIHDLCVRYENNLK-PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVI-DGIDISKLPLHTLRSR 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  462 IGVVSQDPLLFSNSIKNNIkyslyslkDLEAlseesnedgfssqsdsnsrnscraKCagdlndmiqtTDSTEliqvrknY 541
Cdd:cd03288    97 LSIILQDPILFSGSIRFNL--------DPEC------------------------KC----------TDDRL-------W 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  542 ETIEDSEvvsvskkvlIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKT 621
Cdd:cd03288   128 EALEIAQ---------LKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKV 198
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 156095386  622 InnLKGNENRITIIIAHRLSTIRYANTIFVLSnreNGSTVDVD 664
Cdd:cd03288   199 V--MTAFADRTVVTIAHRVSTILDADLVLVLS---RGILVECD 236
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
1164-1429 6.81e-20

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: 89.86  E-value: 6.81e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYlsrPNVPIYKDLTFscESKKTTAIVGETGSGKSTVMSLLMRFydlkndhhivfkneqtgesskeqmqqgd 1243
Cdd:cd03298     1 VRLDKIRFSY---GEQPMHFDLTF--AQGEITAIVGPSGSGKSTLLNLIAGF---------------------------- 47
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 eeqnvgmknanefssskegadgqsstLFKNSGKILLDGVDICdyNLKDLRNLFSIVSQEPMLF-NMSIYENIKFG----- 1317
Cdd:cd03298    48 --------------------------ETPQSGRVLINGVDVT--AAPPADRPVSMLFQENNLFaHLTVEQNVGLGlspgl 99
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1318 KENAT-REDVKRACKFAAIDEFIESLPNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIE 1396
Cdd:cd03298   100 KLTAEdRQAIEVALARVGLAGLEKRLPGE-----------LSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEML 168
                         250       260       270
                  ....*....|....*....|....*....|...
gi 156095386 1397 KTIVDIKDKADKTIITIAHRIASIKRSDKIVVF 1429
Cdd:cd03298   169 DLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVF 201
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
381-656 7.52e-20

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 91.23  E-value: 7.52e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  381 KKIQFKNVRFHYDTRKDVEIyKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIIN----DSHNLKDVnlk 456
Cdd:PRK13635    4 EIIRVEHISFRYPDAATYAL-KDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGgmvlSEETVWDV--- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  457 wwRSKIGVVSQDPllfsnsikNNiKYSLYSLKDLEALSEESNedGFSSQsdsnsrnscrakcagdlnDMIQTTDSTeLIQ 536
Cdd:PRK13635   80 --RRQVGMVFQNP--------DN-QFVGATVQDDVAFGLENI--GVPRE------------------EMVERVDQA-LRQ 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  537 VRknyetiedsevvsvskkvlIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEY 616
Cdd:PRK13635  128 VG-------------------MEDFLNREP-----------HRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRR 177
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 156095386  617 LVQKTINNLKgNENRITII-IAHRLSTIRYANTIFVLSNRE 656
Cdd:PRK13635  178 EVLETVRQLK-EQKGITVLsITHDLDEAAQADRVIVMNKGE 217
PLN03130 PLN03130
ABC transporter C family member; Provisional
351-653 7.79e-20

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 96.73  E-value: 7.79e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  351 SLEATNNLYEIINRKPLV-ENNQDGKKLKDIKKIQFKNVRFHYdtRKDVE-IYKDLNFTLTEGKTYAFVGESGCGKSTIL 428
Cdd:PLN03130 1205 AVERVGTYIDLPSEAPLViENNRPPPGWPSSGSIKFEDVVLRY--RPELPpVLHGLSFEISPSEKVGIVGRTGAGKSSML 1282
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  429 KLIERLYDPTEGDVIInDSHNLKDVNLKWWRSKIGVVSQDPLLFSNSIKNNIkyslyslkdlealseesneDGFSSQSDS 508
Cdd:PLN03130 1283 NALFRIVELERGRILI-DGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNL-------------------DPFNEHNDA 1342
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  509 NSRNSC-RAKcagdLNDMIqttdsteliqvRKNYETIeDSEVvsvskkvlihdfvsalpdkyeTLVGSNaskLSGGQKQR 587
Cdd:PLN03130 1343 DLWESLeRAH----LKDVI-----------RRNSLGL-DAEV---------------------SEAGEN---FSVGQRQL 1382
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156095386  588 ISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINnlkgNENR--ITIIIAHRLSTIRYANTIFVLS 653
Cdd:PLN03130 1383 LSLARALLRRSKILVLDEATAAVDVRTDALIQKTIR----EEFKscTMLIIAHRLNTIIDCDRILVLD 1446
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
383-653 1.10e-19

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 89.39  E-value: 1.10e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHYDTRKdveIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIInDSHNLKDVNLKWWRSKI 462
Cdd:PRK10247    8 LQLQNVGYLAGDAK---ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLF-EGEDISTLKPEIYRQQV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  463 GVVSQDPLLFSNSIKNNIKYSLyslkdlealseesnedgfssqsdsnsrnscrakcagdlndmiqttdsteliQVRKNye 542
Cdd:PRK10247   84 SYCAQTPTLFGDTVYDNLIFPW---------------------------------------------------QIRNQ-- 110
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  543 tiedsevvSVSKKVLIHDFVS-ALPdkyETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKT 621
Cdd:PRK10247  111 --------QPDPAIFLDDLERfALP---DTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEI 179
                         250       260       270
                  ....*....|....*....|....*....|..
gi 156095386  622 INNLKGNENRITIIIAHRLSTIRYANTIFVLS 653
Cdd:PRK10247  180 IHRYVREQNIAVLWVTHDKDEINHADKVITLQ 211
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
378-643 1.38e-19

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 90.10  E-value: 1.38e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  378 KDIKKIQFKNVRFHYDTRKDVEiykDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYD-----PTEGDV-IINDSHNLK 451
Cdd:PRK14258    3 KLIPAIKVNNLSFYYDTQKILE---GVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElesevRVEGRVeFFNQNIYER 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  452 DVNLKWWRSKIGVVSQDPLLFSNSIKNNIKYSLYSLkdlealseesnedgfssqsdsnsrnSCRAKCagDLNDMIQTtds 531
Cdd:PRK14258   80 RVNLNRLRRQVSMVHPKPNLFPMSVYDNVAYGVKIV-------------------------GWRPKL--EIDDIVES--- 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  532 teliqvrknyeTIEDSEvvsvskkvlihdfvsaLPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:PRK14258  130 -----------ALKDAD----------------LWDEIKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLD 182
                         250       260       270
                  ....*....|....*....|....*....|..
gi 156095386  612 NKSEYLVQKTINNLKGNENRITIIIAHRLSTI 643
Cdd:PRK14258  183 PIASMKVESLIQSLRLRSELTMVIVSHNLHQV 214
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
1154-1437 1.49e-19

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 90.23  E-value: 1.49e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1154 IKNSNDIKGKIEIMDVNFRYLSRPNVpiyKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDLKNDhhivfkneqtge 1233
Cdd:PRK14243    1 TSTLNGTETVLRTENLNVYYGSFLAV---KNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIPG------------ 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1234 sskeqmqqgdeeqnvgmknanefssskegadgqsstlFKNSGKILLDGVDICDYNLK--DLRNLFSIVSQEPMLFNMSIY 1311
Cdd:PRK14243   66 -------------------------------------FRVEGKVTFHGKNLYAPDVDpvEVRRRIGMVFQKPNPFPKSIY 108
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1312 ENIKFG-KENATRED----VKRACKFAAI-DEFIESLPNQydtnvgpyGKSLSGGQKQRIAIARALLREPKILLLDEATS 1385
Cdd:PRK14243  109 DNIAYGaRINGYKGDmdelVERSLRQAALwDEVKDKLKQS--------GLSLSGGQQQRLCIARAIAVQPEVILMDEPCS 180
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 156095386 1386 SLDSNSEKLIEKTIVDIKDkaDKTIITIAHRIASIKR-SDKIVVFN-NPDRTGS 1437
Cdd:PRK14243  181 ALDPISTLRIEELMHELKE--QYTIIIVTHNMQQAARvSDMTAFFNvELTEGGG 232
cbiO PRK13646
energy-coupling factor transporter ATPase;
382-663 1.77e-19

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 90.61  E-value: 1.77e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  382 KIQFKNVRFHYD--TRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIIND---SHNLKDVNLK 456
Cdd:PRK13646    2 TIRFDNVSYTYQkgTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitiTHKTKDKYIR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  457 WWRSKIGVVSQDP--LLFSNSIKNNIkysLYSLKDLEALSEESNEDGFssqsdsnsrnscrakcagDLndmiqttdsteL 534
Cdd:PRK13646   82 PVRKRIGMVFQFPesQLFEDTVEREI---IFGPKNFKMNLDEVKNYAH------------------RL-----------L 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  535 IQvrknyetiedsevVSVSKKVLihdfvsalpdkyetlvGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS 614
Cdd:PRK13646  130 MD-------------LGFSRDVM----------------SQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQS 180
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 156095386  615 EYLVQKTINNLKGNENRITIIIAHRLSTI-RYANTIFVLsnrENGSTVDV 663
Cdd:PRK13646  181 KRQVMRLLKSLQTDENKTIILVSHDMNEVaRYADEVIVM---KEGSIVSQ 227
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
1178-1427 1.77e-19

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: 89.16  E-value: 1.77e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1178 NVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfkneqtgesskeqmqqgdeeqnvgmknanefs 1257
Cdd:cd03256    13 GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEP--------------------------------------- 53
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1258 sskegadgqsstlfkNSGKILLDGVDICDYNLKDLRnlfSIVSQEPMLF-------NMSIYENIKFGKENA--------- 1321
Cdd:cd03256    54 ---------------TSGSVLIDGTDINKLKGKALR---QLRRQIGMIFqqfnlieRLSVLENVLSGRLGRrstwrslfg 115
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1322 --TREDVKRAckFAAIDEF-IESLPNQY-DTnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEK 1397
Cdd:cd03256   116 lfPKEEKQRA--LAALERVgLLDKAYQRaDQ--------LSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMD 185
                         250       260       270
                  ....*....|....*....|....*....|.
gi 156095386 1398 TIVDIKDKADKTIITIAHRIASIKR-SDKIV 1427
Cdd:cd03256   186 LLKRINREEGITVIVSLHQVDLAREyADRIV 216
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
383-613 1.94e-19

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: 88.83  E-value: 1.94e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHYDtrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDshnlKDV-NLKWWRSK 461
Cdd:cd03300     1 IELENVSKFYG---GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDG----KDItNLPPHKRP 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  462 IGVVSQDPLLFSN-SIKNNIKYSLySLKDLealseesnedgfssqsdsnSRNSCRAKCAGDLnDMIQttdsteliqvrkn 540
Cdd:cd03300    74 VNTVFQNYALFPHlTVFENIAFGL-RLKKL-------------------PKAEIKERVAEAL-DLVQ------------- 119
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 156095386  541 yetiedsevvsvskkvlihdfVSALPDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNK 613
Cdd:cd03300   120 ---------------------LEGYANRK-------PSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLK 164
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
383-613 2.05e-19

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


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 91.36  E-value: 2.05e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHYDTRKdveIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDshnlKDV--NLKWWRS 460
Cdd:COG1118     3 IEVRNISKRFGSFT---LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNG----RDLftNLPPRER 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  461 KIGVVSQDPLLFSN-SIKNNIKYSLYSLKdleaLSEESnedgfssqsdsnsrnscRAKCAGDLNDMIQttdsteliqvrk 539
Cdd:COG1118    76 RVGFVFQHYALFPHmTVAENIAFGLRVRP----PSKAE-----------------IRARVEELLELVQ------------ 122
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156095386  540 nyetiedsevvsvskkvlihdfVSALPDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNK 613
Cdd:COG1118   123 ----------------------LEGLADRY-------PSQLSGGQRQRVALARALAVEPEVLLLDEPFGALDAK 167
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
1163-1460 2.16e-19

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 89.20  E-value: 2.16e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1163 KIEIMDVNfryLSRPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDLKNDHHIvfkneqtgesskeqmqqg 1242
Cdd:PRK14247    3 KIEIRDLK---VSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYPEARV------------------ 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1243 deeqnvgmknanefssskegadgqsstlfknSGKILLDGVDICDYNLKDLRNLFSIVSQEPM-LFNMSIYENIKFG---- 1317
Cdd:PRK14247   62 -------------------------------SGEVYLDGQDIFKMDVIELRRRVQMVFQIPNpIPNLSIFENVALGlkln 110
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1318 ----KENATREDVKRACKFAaidEFIESLPNQYDtnvGPYGKsLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEK 1393
Cdd:PRK14247  111 rlvkSKKELQERVRWALEKA---QLWDEVKDRLD---APAGK-LSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTA 183
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156095386 1394 LIEKTIVDIKDkaDKTIITIAHRIASIKRSDKIVVFNnpdRTGSFVQAQGTHEELLSVQDGVYKKYV 1460
Cdd:PRK14247  184 KIESLFLELKK--DMTIVLVTHFPQQAARISDYVAFL---YKGQIVEWGPTREVFTNPRHELTEKYV 245
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
1164-1415 5.55e-19

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 87.42  E-value: 5.55e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYlsRPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRfydlkndhhivfkneqtgesskeqmqqgd 1243
Cdd:COG2884     2 IRFENVSKRY--PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYG----------------------------- 50
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 EEQNvgmknanefssskegadgqsstlfkNSGKILLDGVDICDYNLKDLRNL---FSIVSQE-PMLFNMSIYENIKF--- 1316
Cdd:COG2884    51 EERP-------------------------TSGQVLVNGQDLSRLKRREIPYLrrrIGVVFQDfRLLPDRTVYENVALplr 105
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1317 --GKENAT-REDVKRACKFAAIDEFIESLPNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLD-SNSE 1392
Cdd:COG2884   106 vtGKSRKEiRRRVREVLDLVGLSDKAKALPHE-----------LSGGEQQRVAIARALVNRPELLLADEPTGNLDpETSW 174
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 156095386 1393 KLIE---------KTIV------DIKDKADKTIITIAH 1415
Cdd:COG2884   175 EIMElleeinrrgTTVLiathdlELVDRMPKRVLELED 212
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
383-652 6.51e-19

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 88.27  E-value: 6.51e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHYDTRKDVEIyKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIIND----SHNLKDVnlkww 458
Cdd:PRK13648    8 IVFKNVSFQYQSDASFTL-KDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNqaitDDNFEKL----- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  459 RSKIGVVSQDPL-LFSNSIknnIKYSLyslkdleALSEEsnedgfssqsdsnsrnscrakcagdlNDMIQTTDSTEliqv 537
Cdd:PRK13648   82 RKHIGIVFQNPDnQFVGSI---VKYDV-------AFGLE--------------------------NHAVPYDEMHR---- 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  538 rknyetiedsEVVSVSKKVLIHDFVSALPDKyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYL 617
Cdd:PRK13648  122 ----------RVSEALKQVDMLERADYEPNA-----------LSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQN 180
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 156095386  618 VQKTINNLKGNENrITII-IAHRLSTIRYANTIFVL 652
Cdd:PRK13648  181 LLDLVRKVKSEHN-ITIIsITHDLSEAMEADHVIVM 215
SapF COG4167
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
389-611 1.03e-18

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


Pssm-ID: 443328 [Multi-domain]  Cd Length: 265  Bit Score: 87.59  E-value: 1.03e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  389 RFHYDT----RKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDsHNLKDVNLKWwRSK-IG 463
Cdd:COG4167    13 TFKYRTglfrRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILING-HKLEYGDYKY-RCKhIR 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  464 VVSQDPllfSNSIknNIKYSLYSLkdLEA-LSeesnedgfssqsdsnsrnscrakcagdLNdmiqtTDSTELIQVRKNYE 542
Cdd:COG4167    91 MIFQDP---NTSL--NPRLNIGQI--LEEpLR---------------------------LN-----TDLTAEEREERIFA 131
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 156095386  543 TIEdsevvsvskkvlihdFVSALPDKYETlvgsNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:COG4167   132 TLR---------------LVGLLPEHANF----YPHMLSSGQKQRVALARALILQPKIIIADEALAALD 181
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
1273-1388 1.25e-18

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


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 86.59  E-value: 1.25e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1273 NSGKILLDGVDICD--YNLKDLRNLFSIVSQEPMLF-NMSIYENI--------KFGKENATredvKRACKFAA---IDEF 1338
Cdd:COG1126    54 DSGTITVDGEDLTDskKDINKLRRKVGMVFQQFNLFpHLTVLENVtlapikvkKMSKAEAE----ERAMELLErvgLADK 129
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 156095386 1339 IESLPNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLD 1388
Cdd:COG1126   130 ADAYPAQ-----------LSGGQQQRVAIARALAMEPKVMLFDEPTSALD 168
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
1273-1431 1.43e-18

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 89.62  E-value: 1.43e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1273 NSGKILLDGVDICDYNLKDlRNLfSIVSQEPMLF-NMSIYENIKFG--------KENATRedVKRACKFAAIDEFIESLP 1343
Cdd:PRK09452   67 DSGRIMLDGQDITHVPAEN-RHV-NTVFQSYALFpHMTVFENVAFGlrmqktpaAEITPR--VMEALRMVQLEEFAQRKP 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1344 NQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH-RIASIKR 1422
Cdd:PRK09452  143 HQ-----------LSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHdQEEALTM 211

                  ....*....
gi 156095386 1423 SDKIVVFNN 1431
Cdd:PRK09452  212 SDRIVVMRD 220
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
1268-1429 1.58e-18

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: 85.81  E-value: 1.58e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1268 STLFKN--------SGKILLDGVDICDYNLK-DL---RNLFSIVSQEPMLF-NMSIYENIKFG-KENATREDVKRAckfa 1333
Cdd:cd03297    37 STLLRCiaglekpdGGTIVLNGTVLFDSRKKiNLppqQRKIGLVFQQYALFpHLNVRENLAFGlKRKRNREDRISV---- 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1334 aiDEFIESLpnQYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITI 1413
Cdd:cd03297   113 --DELLDLL--GLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKKNLNIPVIFV 188
                         170
                  ....*....|....*..
gi 156095386 1414 AHRIASIKR-SDKIVVF 1429
Cdd:cd03297   189 THDLSEAEYlADRIVVM 205
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
1174-1388 1.69e-18

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


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 85.61  E-value: 1.69e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1174 LSRPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMrfydlkndhhivfkneqtgesskeqmqqgdeeqnvgmkna 1253
Cdd:COG4136     9 ITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIA---------------------------------------- 48
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1254 nefssskegadGQSSTLFKNSGKILLDGVDICDYNLkDLRNLfSIVSQEPMLF-NMSIYENIKFgkenATREDVKRACKF 1332
Cdd:COG4136    49 -----------GTLSPAFSASGEVLLNGRRLTALPA-EQRRI-GILFQDDLLFpHLSVGENLAF----ALPPTIGRAQRR 111
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 156095386 1333 AAIDEFIES--LPNQYDTNVGpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLD 1388
Cdd:COG4136   112 ARVEQALEEagLAGFADRDPA----TLSGGQRARVALLRALLAEPRALLLDEPFSKLD 165
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
402-636 2.05e-18

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 86.76  E-value: 2.05e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  402 KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYD--PT---EGDVIINDsHNL--KDVNLKWWRSKIGVVSQDPLLFSN 474
Cdd:PRK14243   27 KNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGfrvEGKVTFHG-KNLyaPDVDPVEVRRRIGMVFQKPNPFPK 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  475 SIKNNIKYSlyslkdlealseeSNEDGFSsqsdsnsrnscrakcaGDLNDMIQTTdsteLIQvrknyetiedsevvsvsk 554
Cdd:PRK14243  106 SIYDNIAYG-------------ARINGYK----------------GDMDELVERS----LRQ------------------ 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  555 kvlihdfvSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgneNRITI 634
Cdd:PRK14243  135 --------AALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELK---EQYTI 203

                  ..
gi 156095386  635 II 636
Cdd:PRK14243  204 II 205
cbiO PRK13637
energy-coupling factor transporter ATPase;
402-652 2.32e-18

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 87.03  E-value: 2.32e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  402 KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDShNL--KDVNLKWWRSKIGVVSQDP--LLFSNSIK 477
Cdd:PRK13637   24 DNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGV-DItdKKVKLSDIRKKVGLVFQYPeyQLFEETIE 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  478 NNIKYSLYSLkdleALSEESNEDgfssqsdsnsrnscRAKCAGDLndmiqttdsteliqVRKNYETIEDSevvsvskkvl 557
Cdd:PRK13637  103 KDIAFGPINL----GLSEEEIEN--------------RVKRAMNI--------------VGLDYEDYKDK---------- 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  558 ihdfvsalpdkyetlvgsNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIA 637
Cdd:PRK13637  141 ------------------SPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVS 202
                         250
                  ....*....|....*.
gi 156095386  638 HRLSTI-RYANTIFVL 652
Cdd:PRK13637  203 HSMEDVaKLADRIIVM 218
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
1274-1431 2.51e-18

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: 85.85  E-value: 2.51e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1274 SGKILLDGVDICDYNLKDlRNLfSIVSQEPMLF-NMSIYENIKFG----------KENATREDVKRACKFAAIDEFIESL 1342
Cdd:cd03296    56 SGTILFGGEDATDVPVQE-RNV-GFVFQHYALFrHMTVFDNVAFGlrvkprserpPEAEIRAKVHELLKLVQLDWLADRY 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1343 PNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIA-SIK 1421
Cdd:cd03296   134 PAQ-----------LSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEeALE 202
                         170
                  ....*....|
gi 156095386 1422 RSDKIVVFNN 1431
Cdd:cd03296   203 VADRVVVMNK 212
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
356-664 2.82e-18

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: 86.54  E-value: 2.82e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  356 NNLYEIINRKPlvennqdGKKLKDIKKIQFKNvrfhydtrkdvEIYK---------DLNFTLTEGKTYAFVGESGCGKST 426
Cdd:cd03294     4 KGLYKIFGKNP-------QKAFKLLAKGKSKE-----------EILKktgqtvgvnDVSLDVREGEIFVIMGLSGSGKST 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  427 ILKLIERLYDPTEGDVIIN--DSHNLKDVNLKWWRSK-IGVVSQDPLLFSN-SIKNNIKYSLyslkDLEALSEESNEdgf 502
Cdd:cd03294    66 LLRCINRLIEPTSGKVLIDgqDIAAMSRKELRELRRKkISMVFQSFALLPHrTVLENVAFGL----EVQGVPRAERE--- 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  503 ssqsdsnsrnscrakcagdlndmiqttdsteliqvRKNYETIEdsevvsvskKVLIHDFVSALPDKyetlvgsnaskLSG 582
Cdd:cd03294   139 -----------------------------------ERAAEALE---------LVGLEGWEHKYPDE-----------LSG 163
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  583 GQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLS-TIRYANTIFVLsnrENGSTV 661
Cdd:cd03294   164 GMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDeALRLGDRIAIM---KDGRLV 240

                  ...
gi 156095386  662 DVD 664
Cdd:cd03294   241 QVG 243
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
402-677 2.91e-18

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: 85.47  E-value: 2.91e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  402 KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDshnlKDV-NLKWWRSKIGVVSQDPLLFSN-SIKNN 479
Cdd:cd03299    16 KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNG----KDItNLPPEKRDISYVPQNYALFPHmTVYKN 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  480 IKYSLyslkdlealseesnedgfssqsdsnsrnscrakcagdlndmiqttdsteliQVRKNYETIEDSEVVSVSKKVLIh 559
Cdd:cd03299    92 IAYGL---------------------------------------------------KKRKVDKKEIERKVLEIAEMLGI- 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  560 dfvsalpdkyETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEylvQKTINNLK--GNENRITII-I 636
Cdd:cd03299   120 ----------DHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTK---EKLREELKkiRKEFGVTVLhV 186
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 156095386  637 AHRLSTIRyantifVLSNR----ENGSTVDVDVLGEDPTKDSNEK 677
Cdd:cd03299   187 THDFEEAW------ALADKvaimLNGKLIQVGKPEEVFKKPKNEF 225
cbiO PRK13644
energy-coupling factor transporter ATPase;
1274-1450 3.01e-18

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 86.58  E-value: 3.01e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1274 SGKILLDGVDICDYN-LKDLRNLFSIVSQEP--MLFNMSIYENIKFGKEN------ATREDVKRACKFAAIDEFIESLPn 1344
Cdd:PRK13644   56 KGKVLVSGIDTGDFSkLQGIRKLVGIVFQNPetQFVGRTVEEDLAFGPENlclppiEIRKRVDRALAEIGLEKYRHRSP- 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1345 qydtnvgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTIITIAHRIASIKRSD 1424
Cdd:PRK13644  135 ----------KTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKG-KTIVYITHNLEELHDAD 203
                         170       180
                  ....*....|....*....|....*.
gi 156095386 1425 KIVVFnnpDRtgSFVQAQGTHEELLS 1450
Cdd:PRK13644  204 RIIVM---DR--GKIVLEGEPENVLS 224
ABC_6TM_exporters cd07346
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ...
61-307 3.11e-18

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: 86.84  E-value: 3.11e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   61 LLGVSFVCATISGGTLPFFVSV---FGVIMKNMNLgenVNDIIFSLVLIGIFQFILSFISSFCMDVVTTKILKTLKIEFL 137
Cdd:cd07346     3 LALLLLLLATALGLALPLLTKLlidDVIPAGDLSL---LLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  138 KSVFYQDGQFHDNNP-G---SKLTSDLDfyleQVNAGIGTKFITIFTYASAFLGLYIWSLFKNARLTLCITCVFPLIYIC 213
Cdd:cd07346    80 RHLQRLSLSFFDRNRtGdlmSRLTSDVD----AVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLI 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  214 GVICNKKVK-----INKKTSLLYNNntmsiIEEALVGIRTVVSYCGENTILKKFNLSEKLYSKYTLKANLMESLHIGMIN 288
Cdd:cd07346   156 LRYFRRRIRkasreVRESLAELSAF-----LQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIG 230
                         250
                  ....*....|....*....
gi 156095386  289 GFILASYAFGFWYGTRIII 307
Cdd:cd07346   231 LLTALGTALVLLYGGYLVL 249
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
1274-1448 3.44e-18

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 87.93  E-value: 3.44e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1274 SGKILLDGVDICDYNLKDLR-------------NLFSivSQepmlfnmSIYENIKFGKE--NATREDVKrackfAAIDEF 1338
Cdd:PRK11153   59 SGRVLVDGQDLTALSEKELRkarrqigmifqhfNLLS--SR-------TVFDNVALPLElaGTPKAEIK-----ARVTEL 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1339 IE--SLPNQYDTnvgpYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHR 1416
Cdd:PRK11153  125 LElvGLSDKADR----YPAQLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHE 200
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 156095386 1417 IASIKR---------SDKIV-------VFNNP--DRTGSFVQAQgTHEEL 1448
Cdd:PRK11153  201 MDVVKRicdrvavidAGRLVeqgtvseVFSHPkhPLTREFIQST-LHLDL 249
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
1273-1427 5.08e-18

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: 84.12  E-value: 5.08e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1273 NSGKILLDGVDICD--YNLKDLRNLFSIVSQEPMLF-NMSIYENIKFGKENATREDVKRACKFA-------AIDEFIESL 1342
Cdd:cd03262    53 DSGTIIIDGLKLTDdkKNINELRQKVGMVFQQFNLFpHLTVLENITLAPIKVKGMSKAEAEERAlellekvGLADKADAY 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1343 PNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKdKADKTIITIAHRIASIKR 1422
Cdd:cd03262   133 PAQ-----------LSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLA-EEGMTMVVVTHEMGFARE 200

                  ....*.
gi 156095386 1423 -SDKIV 1427
Cdd:cd03262   201 vADRVI 206
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
383-637 6.16e-18

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: 84.09  E-value: 6.16e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHYDTRKDVEIyKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDsHNLKDvNLKWWRSKI 462
Cdd:cd03263     1 LQIRNLTKTYKKGTKPAV-DDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYING-YSIRT-DRKAARQSL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  463 GVVSQDPLLFSNsiknnikyslysLKDLEALseesnedgfssqsdsnsRNSCRAKCagdlndmiqttdsteliqvrknye 542
Cdd:cd03263    78 GYCPQFDALFDE------------LTVREHL-----------------RFYARLKG------------------------ 104
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  543 tIEDSEVVSVSKKVLIHDfvsALPDKYETLvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI 622
Cdd:cd03263   105 -LPKSEIKEEVELLLRVL---GLTDKANKR----ARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLI 176
                         250
                  ....*....|....*
gi 156095386  623 NNLKgnENRiTIIIA 637
Cdd:cd03263   177 LEVR--KGR-SIILT 188
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
383-643 1.45e-17

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: 83.98  E-value: 1.45e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHYDTRKdveIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEG-DVIINDsHNLKDVNLKWWRSK 461
Cdd:COG1119     4 LELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFG-ERRGGEDVWELRKR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  462 IGVVSQDpllfsnsiknnikyslyslkdlealseesnedgfsSQSDSNSRNSCRakcagdlnDMIQT--TDSTELiqvrk 539
Cdd:COG1119    80 IGLVSPA-----------------------------------LQLRFPRDETVL--------DVVLSgfFDSIGL----- 111
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  540 nYETIEDSEVVSVskKVLIHDF-VSALPDK-YETLvgsnasklSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYL 617
Cdd:COG1119   112 -YREPTDEQRERA--RELLELLgLAHLADRpFGTL--------SQGEQRRVLIARALVKDPELLILDEPTAGLDLGAREL 180
                         250       260
                  ....*....|....*....|....*.
gi 156095386  618 VQKTINNLKGNENRITIIIAHRLSTI 643
Cdd:COG1119   181 LLALLDKLAAEGAPTLVLVTHHVEEI 206
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
1270-1450 1.99e-17

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 84.37  E-value: 1.99e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1270 LFKNSGKILLDGVDICDY-NLKDLRNLFSIVSQEP--MLFNMSIYENIKFGKEN------ATREDVKRACKFAAIDEFIE 1340
Cdd:PRK13633   60 LIPSEGKVYVDGLDTSDEeNLWDIRNKAGMVFQNPdnQIVATIVEEDVAFGPENlgippeEIRERVDESLKKVGMYEYRR 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1341 SLPNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASI 1420
Cdd:PRK13633  140 HAPHL-----------LSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEA 208
                         170       180       190
                  ....*....|....*....|....*....|
gi 156095386 1421 KRSDKIVVFNnpdrTGSFVQaQGTHEELLS 1450
Cdd:PRK13633  209 VEADRIIVMD----SGKVVM-EGTPKEIFK 233
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
402-676 2.30e-17

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 87.00  E-value: 2.30e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  402 KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIIN----DSHNLKDVnlkwWRSKIGVVSQDPLLFSN-SI 476
Cdd:COG1129    21 DGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDgepvRFRSPRDA----QAAGIAIIHQELNLVPNlSV 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  477 KNNIkyslyslkdleALSEESNEDGFSsqsdsnsrnscrakcagDLNDMIQTTdsTELIqvrknyETIEdsevVSVSkkv 556
Cdd:COG1129    97 AENI-----------FLGREPRRGGLI-----------------DWRAMRRRA--RELL------ARLG----LDID--- 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  557 lihdfvsalPDkyeTLVGSnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNK-SEYLVqKTINNLKgnENRITII 635
Cdd:COG1129   134 ---------PD---TPVGD----LSVAQQQLVEIARALSRDARVLILDEPTASLTEReVERLF-RIIRRLK--AQGVAII 194
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 156095386  636 -IAHRLSTIRY-ANTIFVLsnReNGSTVdvdvlGEDPTKDSNE 676
Cdd:COG1129   195 yISHRLDEVFEiADRVTVL--R-DGRLV-----GTGPVAELTE 229
PhnC COG3638
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ...
1164-1415 2.48e-17

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


Pssm-ID: 442855 [Multi-domain]  Cd Length: 249  Bit Score: 83.18  E-value: 2.48e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYLSrpNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfkneqtgesskeqmqqgd 1243
Cdd:COG3638     3 LELRNLSKRYPG--GTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEP------------------------- 55
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 eeqnvgmknanefssskegadgqsstlfkNSGKILLDGVDICDYNLKDLRNLFS---IVSQEPMLF-NMSIYENI---KF 1316
Cdd:COG3638    56 -----------------------------TSGEILVDGQDVTALRGRALRRLRRrigMIFQQFNLVpRLSVLTNVlagRL 106
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1317 GKENA--------TREDVKRAckFAAIDEFieSLPNQYDTNVGpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLD 1388
Cdd:COG3638   107 GRTSTwrsllglfPPEDRERA--LEALERV--GLADKAYQRAD----QLSGGQQQRVAIARALVQEPKLILADEPVASLD 178
                         250       260
                  ....*....|....*....|....*...
gi 156095386 1389 -SNSEKLIEkTIVDIKDKADKTIITIAH 1415
Cdd:COG3638   179 pKTARQVMD-LLRRIAREDGITVVVNLH 205
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
1164-1450 2.71e-17

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 83.92  E-value: 2.71e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYlsRPNVPIYK----DLTFSCESKKTTAIVGETGSGKSTVM----SLLMrfydlkndhhivfkneqtgeSS 1235
Cdd:PRK13634    3 ITFQKVEHRY--QYKTPFERralyDVNVSIPSGSYVAIIGHTGSGKSTLLqhlnGLLQ--------------------PT 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1236 KEQMQQGDEEQNVGMKNANefssskegadgqsstlfknsgkilldgvdicdynLKDLRNLFSIVSQ--EPMLFNMSIYEN 1313
Cdd:PRK13634   61 SGTVTIGERVITAGKKNKK----------------------------------LKPLRKKVGIVFQfpEHQLFEETVEKD 106
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1314 IKFGKEN--ATREDVKRACKfaaidEFIE--SLPNQYDTNvGPYgkSLSGGQKQRIAIARALLREPKILLLDEATSSLDS 1389
Cdd:PRK13634  107 ICFGPMNfgVSEEDAKQKAR-----EMIElvGLPEELLAR-SPF--ELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDP 178
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 156095386 1390 NSEKLIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVVFNNpdrtGSfVQAQGTHEELLS 1450
Cdd:PRK13634  179 KGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARyADQIVVMHK----GT-VFLQGTPREIFA 235
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
1177-1431 2.73e-17

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: 82.38  E-value: 2.73e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1177 PNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMrfydlkndhhivfkneqtGEsskeqMQQgdeeqnvgMKNANEF 1256
Cdd:cd03290    12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAIL------------------GE-----MQT--------LEGKVHW 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1257 SSSKEGADGQSSTLFKNSGKIlldgvdicdynlkdlrnlfSIVSQEPMLFNMSIYENIKFGKE-NATR-EDVKRACkfaA 1334
Cdd:cd03290    61 SNKNESEPSFEATRSRNRYSV-------------------AYAAQKPWLLNATVEENITFGSPfNKQRyKAVTDAC---S 118
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1335 IDEFIESLPNQYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSN-SEKLIEKTIVDIKDKADKTIITI 1413
Cdd:cd03290   119 LQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHlSDHLMQEGILKFLQDDKRTLVLV 198
                         250
                  ....*....|....*...
gi 156095386 1414 AHRIASIKRSDKIVVFNN 1431
Cdd:cd03290   199 THKLQYLPHADWIIAMKD 216
cbiO PRK13640
energy-coupling factor transporter ATPase;
383-663 2.77e-17

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 84.08  E-value: 2.77e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHY-DTRKDVeiYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGD--VIINDSHNLKDVNLKWWR 459
Cdd:PRK13640    6 VEFKHVSFTYpDSKKPA--LNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnsKITVDGITLTAKTVWDIR 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  460 SKIGVVSQDPllfsnsiknnikyslyslkDLEALSEESNED-GFSSQSDSNSRNscrakcagdlndmiqttdstELIQVr 538
Cdd:PRK13640   84 EKVGIVFQNP-------------------DNQFVGATVGDDvAFGLENRAVPRP--------------------EMIKI- 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  539 knyetiedseVVSVSKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLV 618
Cdd:PRK13640  124 ----------VRDVLADVGMLDYIDSEP-----------ANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQI 182
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 156095386  619 QKTINNLKgNENRITII-IAHRLSTIRYANTIFVLSNRE---NGSTVDV 663
Cdd:PRK13640  183 LKLIRKLK-KKNNLTVIsITHDIDEANMADQVLVLDDGKllaQGSPVEI 230
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
390-611 3.44e-17

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 83.30  E-value: 3.44e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  390 FHYDT----RKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDsHNLKDVNLKWWRSKIGVV 465
Cdd:PRK15112   14 FRYRTgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDD-HPLHFGDYSYRSQRIRMI 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  466 SQDPllfSNSIknNIKYSLYSLKDLEALseesnedgfssqsdsnsrnscrakcagdLNDMIQTTDSTELIqvrknYETIE 545
Cdd:PRK15112   93 FQDP---STSL--NPRQRISQILDFPLR----------------------------LNTDLEPEQREKQI-----IETLR 134
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156095386  546 DsevvsvskkvlihdfVSALPDKyetlVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:PRK15112  135 Q---------------VGLLPDH----ASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLD 181
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
383-654 5.02e-17

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: 81.47  E-value: 5.02e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHYDTRKDVeiyKDLNFTLTEGkTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDSHNLKDVNlkWWRSKI 462
Cdd:cd03264     1 LQLENLTKRYGKKRAL---DGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQ--KLRRRI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  463 GVVSQDPLLFSNsiknnikyslysLKDLEALseesnedgfssqsdsnsRNSCRAKcagdlnDMIQTTdsteliqvrknye 542
Cdd:cd03264    75 GYLPQEFGVYPN------------FTVREFL-----------------DYIAWLK------GIPSKE------------- 106
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  543 tiEDSEVVSVSKKVLIHDFVsalpDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI 622
Cdd:cd03264   107 --VKARVDEVLELVNLGDRA----KKK-------IGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLL 173
                         250       260       270
                  ....*....|....*....|....*....|...
gi 156095386  623 NNLkgNENRITIIIAHRLSTIRY-ANTIFVLSN 654
Cdd:cd03264   174 SEL--GEDRIVILSTHIVEDVESlCNQVAVLNK 204
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
383-639 5.97e-17

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 82.13  E-value: 5.97e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHYDTRKDVeiyKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYD-----PTEGDVIINdSHNL-----KD 452
Cdd:PRK14239    6 LQVSDLSVYYNKKKAL---NSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYN-GHNIysprtDT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  453 VNLkwwRSKIGVVSQDPLLFSNSIKNNIKYSLY--SLKDLEALseesnedgfssqsDSNSRNSCRAKCAGDlndmiqttd 530
Cdd:PRK14239   82 VDL---RKEIGMVFQQPNPFPMSIYENVVYGLRlkGIKDKQVL-------------DEAVEKSLKGASIWD--------- 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  531 steliqvrknyetiedsEVvsvskKVLIHDfvsalpdkyetlvgsNASKLSGGQKQRISIARAIIRNPKILILDEATSSL 610
Cdd:PRK14239  137 -----------------EV-----KDRLHD---------------SALGLSGGQQQRVCIARVLATSPKIILLDEPTSAL 179
                         250       260
                  ....*....|....*....|....*....
gi 156095386  611 DNKSEYLVQKTINNLKgneNRITIIIAHR 639
Cdd:PRK14239  180 DPISAGKIEETLLGLK---DDYTMLLVTR 205
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
1164-1415 6.51e-17

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: 81.30  E-value: 6.51e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYlsRPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRfydlkndhhivfkneqtgesskeqmqqgd 1243
Cdd:cd03292     1 IEFINVTKTY--PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYK----------------------------- 49
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 EEQnvgmknanefssskegadgqsstlfKNSGKILLDGVDICDYN---LKDLRNLFSIVSQE-PMLFNMSIYENIKFGKE 1319
Cdd:cd03292    50 EEL-------------------------PTSGTIRVNGQDVSDLRgraIPYLRRKIGVVFQDfRLLPDRNVYENVAFALE 104
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1320 ------NATREDVKRACKFAAIDEFIESLPNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEK 1393
Cdd:cd03292   105 vtgvppREIRKRVPAALELVGLSHKHRALPAE-----------LSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTW 173
                         250       260
                  ....*....|....*....|..
gi 156095386 1394 LIEKTIVDIkDKADKTIITIAH 1415
Cdd:cd03292   174 EIMNLLKKI-NKAGTTVVVATH 194
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
1162-1420 7.23e-17

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: 82.59  E-value: 7.23e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1162 GKIEIMDVNFRYLSRPNVpIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRfydlkndhhivfkneqtgesskeqmqq 1241
Cdd:cd03289     1 GQMTVKDLTAKYTEGGNA-VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLR--------------------------- 52
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1242 gdeeqnvgmknanefssskegadgqsstLFKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIK-FGKEN 1320
Cdd:cd03289    53 ----------------------------LLNTEGDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTFRKNLDpYGKWS 104
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1321 atREDVKRACKFAAIDEFIESLPNQYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIV 1400
Cdd:cd03289   105 --DEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLK 182
                         250       260
                  ....*....|....*....|
gi 156095386 1401 diKDKADKTIITIAHRIASI 1420
Cdd:cd03289   183 --QAFADCTVILSEHRIEAM 200
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
1179-1450 8.35e-17

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: 80.94  E-value: 8.35e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1179 VPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDLKndhhivfkneqtgesskeqmqqgdeeqnvgmknanefss 1258
Cdd:cd03224    13 SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPR--------------------------------------- 53
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1259 skegadgqsstlfknSGKILLDGVDIcdynlkDLRNLFSI-------VSQEPMLF-NMSIYENIKFGKENATREDVKRAc 1330
Cdd:cd03224    54 ---------------SGSIRFDGRDI------TGLPPHERaragigyVPEGRRIFpELTVEENLLLGAYARRRAKRKAR- 111
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1331 kfaaIDEFIESLP------NQYdtnvgpyGKSLSGGQKQRIAIARALLREPKILLLDEATSSLdsnSEKLIE---KTIVD 1401
Cdd:cd03224   112 ----LERVYELFPrlkerrKQL-------AGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGL---APKIVEeifEAIRE 177
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 156095386 1402 IKDKaDKTIITI---AHRIASIkrSDKIVVFnnpdRTGSFVqAQGTHEELLS 1450
Cdd:cd03224   178 LRDE-GVTILLVeqnARFALEI--ADRAYVL----ERGRVV-LEGTAAELLA 221
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
1164-1419 8.43e-17

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


Pssm-ID: 443326 [Multi-domain]  Cd Length: 242  Bit Score: 81.60  E-value: 8.43e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYLSrpnVPIYKDLTFSCESKKTTAIVGETGSGKST---VMSLLmrfyDLKNDHHIVFKNEQTGESSKEQMQ 1240
Cdd:COG4161     3 IQLKNINCFYGS---HQALFDINLECPSGETLVLLGPSGAGKSSllrVLNLL----ETPDSGQLNIAGHQFDFSQKPSEK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1241 QGDE-EQNVGMknanefssskegadgqsstLFKNsgkilldgvdicdYNL----KDLRNLFsivsQEPM-LFNMSiyeni 1314
Cdd:COG4161    76 AIRLlRQKVGM-------------------VFQQ-------------YNLwphlTVMENLI----EAPCkVLGLS----- 114
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1315 kfgKENAtredVKRACKFAA---IDEFIESLPNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNs 1391
Cdd:COG4161   115 ---KEQA----REKAMKLLArlrLTDKADRFPLH-----------LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPE- 175
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 156095386 1392 eklIEKTIVDIKDKADKTIIT---------IAHRIAS 1419
Cdd:COG4161   176 ---ITAQVVEIIRELSQTGITqvivtheveFARKVAS 209
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
1183-1450 1.21e-16

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: 80.94  E-value: 1.21e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1183 KDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfkneqtgesskeqmqqgdeeqnvgmknanefssskeg 1262
Cdd:cd03219    17 DDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRP-------------------------------------------- 52
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1263 adgqsstlfkNSGKILLDGVDICdyNLK-DLRNLFSIVS--QEPMLF-NMSIYENIKFGKENATREDVKRACKFAAIDEF 1338
Cdd:cd03219    53 ----------TSGSVLFDGEDIT--GLPpHEIARLGIGRtfQIPRLFpELTVLENVMVAAQARTGSGLLLARARREEREA 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1339 IES---------LPNQYDTNVGpygkSLSGGQKQRIAIARALLREPKILLLDEATSSL-DSNSEKLIEkTIVDIKDKaDK 1408
Cdd:cd03219   121 RERaeellervgLADLADRPAG----ELSYGQQRRLEIARALATDPKLLLLDEPAAGLnPEETEELAE-LIRELRER-GI 194
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 156095386 1409 TIITIAHRIASIKR-SDKIVVFNNpdrtGSfVQAQGTHEELLS 1450
Cdd:cd03219   195 TVLLVEHDMDVVMSlADRVTVLDQ----GR-VIAEGTPDEVRN 232
cbiO PRK13642
energy-coupling factor transporter ATPase;
1243-1455 1.39e-16

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 81.68  E-value: 1.39e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1243 DEEQNVGMKNANEFSSSK--------EGADGQSST------LFKN-SGKILLDGVDICDYNLKDLRNLFSIVSQEP--ML 1305
Cdd:PRK13642   15 EKESDVNQLNGVSFSITKgewvsiigQNGSGKSTTarlidgLFEEfEGKVKIDGELLTAENVWNLRRKIGMVFQNPdnQF 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1306 FNMSIYENIKFGKENatrEDVKRACKFAAIDEFIESLpNQYDTNVGPYGKsLSGGQKQRIAIARALLREPKILLLDEATS 1385
Cdd:PRK13642   95 VGATVEDDVAFGMEN---QGIPREEMIKRVDEALLAV-NMLDFKTREPAR-LSGGQKQRVAVAGIIALRPEIIILDESTS 169
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1386 SLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKRSDKIVVFnnpdRTGSFVQAQGTHEELLSVQDGV 1455
Cdd:PRK13642  170 MLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVM----KAGEIIKEAAPSELFATSEDMV 235
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
383-613 1.82e-16

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 83.07  E-value: 1.82e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHYDTRkdvEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDshnlKDVN-LKWWRSK 461
Cdd:PRK09452   15 VELRGISKSFDGK---EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDG----QDIThVPAENRH 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  462 IGVVSQDPLLFSN-SIKNNIKYSLyslkdlealseesnedgfssqsdsnsrnscraKCAGDLNDMIQTTDSTELIQVRkn 540
Cdd:PRK09452   88 VNTVFQSYALFPHmTVFENVAFGL--------------------------------RMQKTPAAEITPRVMEALRMVQ-- 133
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 156095386  541 yetiedsevvsvskkvlihdfvsalpdkYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNK 613
Cdd:PRK09452  134 ----------------------------LEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYK 178
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
403-614 2.42e-16

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: 82.46  E-value: 2.42e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  403 DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIIN-----DSHnlKDVNLKWWRSKIGVVSQDPLLFSN-SI 476
Cdd:COG4148    17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGgevlqDSA--RGIFLPPHRRRIGYVFQEARLFPHlSV 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  477 KNNIKYSLyslkdlealseesnedgfssqsdsnsRNSCRAKCAGDLNDMIQTTDsteliqvrknyetIEDsevvsvskkv 556
Cdd:COG4148    95 RGNLLYGR--------------------------KRAPRAERRISFDEVVELLG-------------IGH---------- 125
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 156095386  557 lihdfvsalpdkyetLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS 614
Cdd:COG4148   126 ---------------LLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLAR 168
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
1274-1448 2.67e-16

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 82.07  E-value: 2.67e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1274 SGKILLDGVDICDYNLKDlRNLfSIVSQEPMLF-NMSIYENIKFG-------KENaTREDVKRACKFAAIDEFIESLPNQ 1345
Cdd:PRK11432   60 EGQIFIDGEDVTHRSIQQ-RDI-CMVFQSYALFpHMSLGENVGYGlkmlgvpKEE-RKQRVKEALELVDLAGFEDRYVDQ 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1346 ydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH-RIASIKRSD 1424
Cdd:PRK11432  137 -----------ISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHdQSEAFAVSD 205
                         170       180
                  ....*....|....*....|....
gi 156095386 1425 KIVVFNNpdrtGSFVQaQGTHEEL 1448
Cdd:PRK11432  206 TVIVMNK----GKIMQ-IGSPQEL 224
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
1161-1460 3.05e-16

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 80.48  E-value: 3.05e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1161 KGKIEIMDVNFRYLSRPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDLKNDHhivfkneqtgesskeqmq 1240
Cdd:PRK14246    5 KSAEDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSK------------------ 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1241 qgdeeqnvgmknanefssskegadgqsstlFKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLF-NMSIYENIKFGKE 1319
Cdd:PRK14246   67 ------------------------------IKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNPFpHLSIYDNIAYPLK 116
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1320 NATREDvKRACKfAAIDEFIESL---PNQYDTNVGPyGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIE 1396
Cdd:PRK14246  117 SHGIKE-KREIK-KIVEECLRKVglwKEVYDRLNSP-ASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIE 193
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156095386 1397 KTIVDIKDKAdkTIITIAHRIASIKRSDKIVVFNnpdRTGSFVQAQGTHEELLSVQDGVYKKYV 1460
Cdd:PRK14246  194 KLITELKNEI--AIVIVSHNPQQVARVADYVAFL---YNGELVEWGSSNEIFTSPKNELTEKYV 252
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
383-681 3.44e-16

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 81.68  E-value: 3.44e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHYDTR----------KDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINdSHNLKD 452
Cdd:PRK15079    9 LEVADLKVHFDIKdgkqwfwqppKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWL-GKDLLG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  453 VNLKWW---RSKIGVVSQDPLLfsnsiknnikySLyslkdlealseesnedgfssqsdsNSRNScrakcagdLNDMIQTT 529
Cdd:PRK15079   88 MKDDEWravRSDIQMIFQDPLA-----------SL------------------------NPRMT--------IGEIIAEP 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  530 dsteliqVRKNYETIEDSEVVSVSKKVLIHdfVSALPDkyetLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSS 609
Cdd:PRK15079  125 -------LRTYHPKLSRQEVKDRVKAMMLK--VGLLPN----LINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSA 191
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156095386  610 LDNKSEYLVqktINNLKG--NENRITII-IAHRLSTIRYantifvLSNRengstVDVDVLG---EDPTKDSNEKNEKH 681
Cdd:PRK15079  192 LDVSIQAQV---VNLLQQlqREMGLSLIfIAHDLAVVKH------ISDR-----VLVMYLGhavELGTYDEVYHNPLH 255
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
1357-1431 3.64e-16

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: 77.47  E-value: 3.64e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156095386 1357 LSGGQKQRIAIARALLREPKILLLDEATSSLDSN-SEKLIeKTIVDIKDKaDKTIITIAHRIASIKR-SDKIVVFNN 1431
Cdd:cd03216    83 LSVGERQMVEIARALARNARLLILDEPTAALTPAeVERLF-KVIRRLRAQ-GVAVIFISHRLDEVFEiADRVTVLRD 157
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
1319-1416 3.64e-16

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 83.70  E-value: 3.64e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1319 ENATREDVKRACKFAAIDEFIESLpnqyDTnVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKT 1398
Cdd:COG4178   453 EAFSDAELREALEAVGLGHLAERL----DE-EADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQL 527
                          90
                  ....*....|....*...
gi 156095386 1399 IVDIKDKAdkTIITIAHR 1416
Cdd:COG4178   528 LREELPGT--TVISVGHR 543
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
1275-1429 4.09e-16

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 79.89  E-value: 4.09e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1275 GKILLDGVDI--CDYNLKDLRNLFSIVSQEPMLF-NMSIYENIKFG--------KENATREDVKRACKFAAIDEFIESLP 1343
Cdd:PRK14267   64 GEVRLFGRNIysPDVDPIEVRREVGMVFQYPNPFpHLTIYDNVAIGvklnglvkSKKELDERVEWALKKAALWDEVKDRL 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1344 NQYDTNvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkaDKTIITIAHRIASIKRS 1423
Cdd:PRK14267  144 NDYPSN-------LSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKK--EYTIVLVTHSPAQAARV 214

                  ....*.
gi 156095386 1424 DKIVVF 1429
Cdd:PRK14267  215 SDYVAF 220
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
383-654 4.20e-16

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: 77.08  E-value: 4.20e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHYDtrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIIN----DSHNLKDVnlkwW 458
Cdd:cd03216     1 LELRGITKRFG---GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDgkevSFASPRDA----R 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  459 RSKIGVVSQdpllfsnsiknnikyslyslkdlealseesnedgfssqsdsnsrnscrakcagdlndmiqttdsteliqvr 538
Cdd:cd03216    74 RAGIAMVYQ----------------------------------------------------------------------- 82
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  539 knyetiedsevvsvskkvlihdfvsalpdkyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLV 618
Cdd:cd03216    83 -----------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERL 121
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 156095386  619 QKTINNLKgnENRITII-IAHRLSTI-RYANTIFVLSN 654
Cdd:cd03216   122 FKVIRRLR--AQGVAVIfISHRLDEVfEIADRVTVLRD 157
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
1268-1427 5.05e-16

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 78.99  E-value: 5.05e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1268 STLFK--------NSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEnaTREDVKRACKFAA-IDEF 1338
Cdd:PRK10247   47 STLLKivaslispTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTVYDNLIFPWQ--IRNQQPDPAIFLDdLERF 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1339 ieSLPNQ-YDTNVgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRI 1417
Cdd:PRK10247  125 --ALPDTiLTKNI----AELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDK 198
                         170
                  ....*....|
gi 156095386 1418 ASIKRSDKIV 1427
Cdd:PRK10247  199 DEINHADKVI 208
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
1268-1453 5.59e-16

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 79.85  E-value: 5.59e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1268 STLFKN--------SGKILLDGVDICDYNLKDLRNLFSIVSQEP--MLFNMSIYENIKFG------KENATREDVKRACK 1331
Cdd:PRK13652   44 STLFRHfngilkptSGSVLIRGEPITKENIREVRKFVGLVFQNPddQIFSPTVEQDIAFGpinlglDEETVAHRVSSALH 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1332 FAAIDEFIESLPNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTII 1411
Cdd:PRK13652  124 MLGLEELRDRVPHH-----------LSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVI 192
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 156095386 1412 TIAHRIASI-KRSDKIVVFNNpdrtGSFVqAQGTHEELLSVQD 1453
Cdd:PRK13652  193 FSTHQLDLVpEMADYIYVMDK----GRIV-AYGTVEEIFLQPD 230
ABC_6TM_exporters cd07346
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ...
825-1119 6.19e-16

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: 79.90  E-value: 6.19e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  825 IAIIALSIMVAgglypLFALLYAKYVGTLFDFANLEANS---NKYSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMKL 901
Cdd:cd07346     2 LLALLLLLLAT-----ALGLALPLLTKLLIDDVIPAGDLsllLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRR 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  902 RLFENIMYQEISFFDQdsHAPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSTVMSFYFCPIVAAVLTGT---YFI 978
Cdd:cd07346    77 DLFRHLQRLSLSFFDR--NRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLlplYVL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  979 FMRVFAIRARiAANKDVEKKRvnqpgtafvynsdDEIFKdpsfLIQEAFYNMNTVIIYGLEDYFctliEKAIDYSNKGQK 1058
Cdd:cd07346   155 ILRYFRRRIR-KASREVRESL-------------AELSA----FLQESLSGIRVVKAFAAEERE----IERFREANRDLR 212
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156095386 1059 RKTLINSMLWGFSQSAQFFINSFA----YWFGSFLIRRGTIQVDDfmksLFTFLftgSYAGKLMS 1119
Cdd:cd07346   213 DANLRAARLSALFSPLIGLLTALGtalvLLYGGYLVLQGSLTIGE----LVAFL---AYLGMLFG 270
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
395-638 6.41e-16

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: 78.47  E-value: 6.41e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  395 RKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDP---TEGDVIINDSHNLKDVnlkwWRSKIGVVSQDPLL 471
Cdd:cd03234    17 NKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPRKPDQ----FQKCVAYVRQDDIL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  472 FSN-SIKNNIKYSLYSlkdleALSEESNEdgfssqsdsnsrnscrakcagdlndmiqttdsteliqvrknyetiedsevv 550
Cdd:cd03234    93 LPGlTVRETLTYTAIL-----RLPRKSSD--------------------------------------------------- 116
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  551 SVSKKVlihDFVSALPDKYETLVGSNASK-LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLkGNE 629
Cdd:cd03234   117 AIRKKR---VEDVLLRDLALTRIGGNLVKgISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQL-ARR 192

                  ....*....
gi 156095386  630 NRITIIIAH 638
Cdd:cd03234   193 NRIVILTIH 201
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
402-644 6.54e-16

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 82.83  E-value: 6.54e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  402 KDLNFTLTEGKTYAFVGESGCGKST----ILKLIerlydPTEGDVIINDS--HNLKDVNLKWWRSKIGVVSQDPllfsNS 475
Cdd:PRK15134  303 KNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQplHNLNRRQLLPVRHRIQVVFQDP----NS 373
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  476 iknnikyslySLkdlealseesnedgfssqsdsNSRnscrakcagdLNdMIQTTDstELIQVRKNYETIEDSE--VVSVS 553
Cdd:PRK15134  374 ----------SL---------------------NPR----------LN-VLQIIE--EGLRVHQPTLSAAQREqqVIAVM 409
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  554 KKVLIHdfvSALPDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKseylVQKTI-NNLKG--NEN 630
Cdd:PRK15134  410 EEVGLD---PETRHRY-------PAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKT----VQAQIlALLKSlqQKH 475
                         250
                  ....*....|....*
gi 156095386  631 RIT-IIIAHRLSTIR 644
Cdd:PRK15134  476 QLAyLFISHDLHVVR 490
ABC_6TM_YknU_like cd18542
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ...
99-343 6.66e-16

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: 80.17  E-value: 6.66e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   99 IIFSLVLIGIFQFILSFISSFCMDVVTTKILKTLKIEFLKSVFYQDGQFHDNNP-G---SKLTSDLDfyleQVNAGIGTK 174
Cdd:cd18542    41 LALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYDHLQRLSFSFHDKARtGdlmSRCTSDVD----TIRRFLAFG 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  175 FITIFtYASAFLGLYIWSLFK-NARLTLCITCVFPLIYICGVICNKKV-----KINKKTSLLynnNTMsiIEEALVGIRT 248
Cdd:cd18542   117 LVELV-RAVLLFIGALIIMFSiNWKLTLISLAIIPFIALFSYVFFKKVrpafeEIREQEGEL---NTV--LQENLTGVRV 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  249 VVSYCGENTILKKFNLSEKLYSKYTLKANLMESLHIGMINGFILASYAFGFWYGTRIIISDlsnqqpnndfhggsviSIL 328
Cdd:cd18542   191 VKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVLVLWVGGYLVING----------------EIT 254
                         250
                  ....*....|....*..
gi 156095386  329 LGVLI--SMFMLTIILP 343
Cdd:cd18542   255 LGELVafISYLWMLIWP 271
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
383-613 7.32e-16

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: 78.54  E-value: 7.32e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHYDTRKDVEiykDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDshnlKDV-NLKWWRSK 461
Cdd:cd03296     3 IEVRNVSKRFGDFVALD---DVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGG----EDAtDVPVQERN 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  462 IGVVSQDPLLFSN-SIKNNIKYSLYSLKDLEALSEesnedgfssqsdsnsrNSCRAKcAGDLNDMIQttdsteliqvrkn 540
Cdd:cd03296    76 VGFVFQHYALFRHmTVFDNVAFGLRVKPRSERPPE----------------AEIRAK-VHELLKLVQ------------- 125
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 156095386  541 yetiedsevvsvskkvlihdfVSALPDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNK 613
Cdd:cd03296   126 ---------------------LDWLADRY-------PAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAK 170
cbiO PRK13642
energy-coupling factor transporter ATPase;
381-656 9.04e-16

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 79.37  E-value: 9.04e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  381 KKIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIInDSHNLKDVNLKWWRS 460
Cdd:PRK13642    3 KILEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKI-DGELLTAENVWNLRR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  461 KIGVVSQDPllfsnsiknnikyslyslkDLEALSEESNED-GFSSQSDSNSRnscrakcagdlNDMIQTTDSTELiqvrk 539
Cdd:PRK13642   82 KIGMVFQNP-------------------DNQFVGATVEDDvAFGMENQGIPR-----------EEMIKRVDEALL----- 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  540 nyetiedsevvsvskKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQ 619
Cdd:PRK13642  127 ---------------AVNMLDFKTREP-----------ARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIM 180
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 156095386  620 KTINNLKGNENRITIIIAHRLSTIRYANTIFVLSNRE 656
Cdd:PRK13642  181 RVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGE 217
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
1275-1450 9.26e-16

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: 80.54  E-value: 9.26e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1275 GKILLDGVDICD----YNLKDLRNLFSIVSQEPMLF-NMSIYENIKFGKENATREDvkRACKFAAIDEF--IESLpnqyd 1347
Cdd:TIGR02142   52 GEIVLNGRTLFDsrkgIFLPPEKRRIGYVFQEARLFpHLSVRGNLRYGMKRARPSE--RRISFERVIELlgIGHL----- 124
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1348 tnVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR-SDKI 1426
Cdd:TIGR02142  125 --LGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRlADRV 202
                          170       180
                   ....*....|....*....|....
gi 156095386  1427 VVFNNpdrtGSfVQAQGTHEELLS 1450
Cdd:TIGR02142  203 VVLED----GR-VAAAGPIAEVWA 221
nickel_nikE TIGR02769
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ...
383-669 1.05e-15

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: 78.69  E-value: 1.05e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   383 IQFKNVRFHYDT------RKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIIN--DSHNLKDVN 454
Cdd:TIGR02769    3 LEVRDVTHTYRTgglfgaKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRgqDLYQLDRKQ 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   455 LKWWRSKIGVVSQDpllfsnsiknnikyslyslkdlealseesnedgfsSQSDSNSRNSCRAKCAGDLNDMiqtTDSTEL 534
Cdd:TIGR02769   83 RRAFRRDVQLVFQD-----------------------------------SPSAVNPRMTVRQIIGEPLRHL---TSLDES 124
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   535 IQVRKNYETIEDSEVVSvskkvlihDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS 614
Cdd:TIGR02769  125 EQKARIAELLDMVGLRS--------EDADKLP-----------RQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVL 185
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 156095386   615 EYLVQKTINNLKGNENRITIIIAHRLSTI-RYANTIFVLsnrENGSTVDVDVLGED 669
Cdd:TIGR02769  186 QAVILELLRKLQQAFGTAYLFITHDLRLVqSFCQRVAVM---DKGQIVEECDVAQL 238
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
1352-1416 1.18e-15

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: 76.04  E-value: 1.18e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156095386 1352 PYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDikdkADKTIITIAHR 1416
Cdd:cd03223    87 PWDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKE----LGITVISVGHR 147
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
1196-1428 1.39e-15

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 81.61  E-value: 1.39e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1196 AIVGETGSGKSTVMSLLMRFYDlkndhhivfkneqtgesskeqmqqgdeeqnvgmknanefssskegADgqsstlfknSG 1275
Cdd:COG3845    35 ALLGENGAGKSTLMKILYGLYQ---------------------------------------------PD---------SG 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1276 KILLDG--VDIcdYNLKDLRNLfSI--VSQEPMLF-NMSIYENIKFGKENATREDVKRAckfAAIDEfIESLPNQYDTNV 1350
Cdd:COG3845    61 EILIDGkpVRI--RSPRDAIAL-GIgmVHQHFMLVpNLTVAENIVLGLEPTKGGRLDRK---AARAR-IRELSERYGLDV 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1351 GPYGK--SLSGGQKQRIAIARALLREPKILLLDEATSSL-DSNSEKLIEkTIVDIKDkADKTIITIAHRIASIKR-SDKI 1426
Cdd:COG3845   134 DPDAKveDLSVGEQQRVEILKALYRGARILILDEPTAVLtPQEADELFE-ILRRLAA-EGKSIIFITHKLREVMAiADRV 211

                  ..
gi 156095386 1427 VV 1428
Cdd:COG3845   212 TV 213
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
1175-1401 1.44e-15

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: 77.13  E-value: 1.44e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1175 SRPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMrfydlkndhhivfkneqtgesskeqmqqgdeeqnvgmknan 1254
Cdd:COG4133    11 RRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILA----------------------------------------- 49
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1255 efssskegadGQSSTLfknSGKILLDGVDIcDYNLKDLRNLFSIVSQEPMLF-NMSIYENIKF----GKENATREDVKRA 1329
Cdd:COG4133    50 ----------GLLPPS---AGEVLWNGEPI-RDAREDYRRRLAYLGHADGLKpELTVRENLRFwaalYGLRADREAIDEA 115
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 156095386 1330 CKFAAIDEFIESLPNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVD 1401
Cdd:COG4133   116 LEAVGLAGLADLPVRQ-----------LSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAA 176
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
403-654 1.56e-15

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: 79.77  E-value: 1.56e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   403 DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDS---HNLKDVNLKWWRSKIGVVSQDPLLFSN-SIKN 478
Cdd:TIGR02142   15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtlfDSRKGIFLPPEKRRIGYVFQEARLFPHlSVRG 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   479 NIKYSLyslkdlealseesnedgfsSQSDSNSRNSCRAKCagdlndmiqttdsTELIQVrknyetiedsevvsvskkvli 558
Cdd:TIGR02142   95 NLRYGM-------------------KRARPSERRISFERV-------------IELLGI--------------------- 121
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   559 hdfvsalpdkyETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgNENRITII-IA 637
Cdd:TIGR02142  122 -----------GHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERLH-AEFGIPILyVS 189
                          250
                   ....*....|....*...
gi 156095386   638 HRLSTI-RYANTIFVLSN 654
Cdd:TIGR02142  190 HSLQEVlRLADRVVVLED 207
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
406-611 1.63e-15

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 79.62  E-value: 1.63e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  406 FTLTEGKTYAFVGESGCGKSTI---LKLIERlydPTEGDVIInDSHNLKDVN---LKWWRSKIGVVSQDPllfsnsiknn 479
Cdd:PRK11308   36 FTLERGKTLAVVGESGCGKSTLarlLTMIET---PTGGELYY-QGQDLLKADpeaQKLLRQKIQIVFQNP---------- 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  480 ikY-SLYSLKDLEALSEESNEdgfssqsdsnsrnscrakcagdlndmIQTTDSTeliQVRKnyetiedSEVVSVSKKV-L 557
Cdd:PRK11308  102 --YgSLNPRKKVGQILEEPLL--------------------------INTSLSA---AERR-------EKALAMMAKVgL 143
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 156095386  558 IHDFVSALPDKYetlvgsnasklSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:PRK11308  144 RPEHYDRYPHMF-----------SGGQRQRIAIARALMLDPDVVVADEPVSALD 186
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
1164-1449 1.87e-15

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: 77.82  E-value: 1.87e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYLSRPnvpIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRfydlknDHHivfkneQTgesskeqmqqgd 1243
Cdd:COG1119     4 LELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITG------DLP------PT------------ 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 eeqnvgmknanefssskegaDGQSSTLFknsGKILlDGVDIcdynlKDLRNLFSIVS---QEPMLFNMSIYENI---KFG 1317
Cdd:COG1119    57 --------------------YGNDVRLF---GERR-GGEDV-----WELRKRIGLVSpalQLRFPRDETVLDVVlsgFFD 107
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1318 K----ENATREDVKRAckFAAIDEF-IESLPNQydtnvgPYGkSLSGGQKQRIAIARALLREPKILLLDEATSSLD-SNS 1391
Cdd:COG1119   108 SiglyREPTDEQRERA--RELLELLgLAHLADR------PFG-TLSQGEQRRVLIARALVKDPELLILDEPTAGLDlGAR 178
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 156095386 1392 EKLIEkTIVDIKDKADKTIITIAHRIASIKRS-DKIVVFnnpdRTGSfVQAQGTHEELL 1449
Cdd:COG1119   179 ELLLA-LLDKLAAEGAPTLVLVTHHVEEIPPGiTHVLLL----KDGR-VVAAGPKEEVL 231
ABC_6TM_Pgp_ABCB1 cd18558
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ...
830-1116 2.28e-15

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: 78.86  E-value: 2.28e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  830 LSIMVAGGLYPLFALLYAKYVGTLFD-------------------FANLEANSNKYSLYILVIAIAMFISETLKNYYNNV 890
Cdd:cd18558     6 LCAIIHGGLLPAFMVIFGDMTDSFTNggmtnitgnssglnssagpFEKLEEEMTLYAYYYLIIGAIVLITAYIQGSFWGL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  891 IGEKVEKTMKLRLFENIMYQEISFFDQdsHAPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSTVMSFYFCPIVAA 970
Cdd:cd18558    86 AAGRQTKKIRYKFFHAIMRQEIGWFDV--NDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRGWKLTL 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  971 VLTGTYFIFMRVFAIRARI-AANKDVEKKRVNQPGTafvynsddeifkdpsfLIQEAFYNMNTVIIYGLEDYFCTLIEKA 1049
Cdd:cd18558   164 VILAISPVLGLSAVVWAKIlSGFTDKEKKAYAKAGA----------------VAEEVLEAFRTVIAFGGQQKEETRYAQN 227
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156095386 1050 IDYSNKGQKRKTLINSMLWGFSQSAQFFINSFAYWFGSFLIRRGTIQVDDFMKSLFTFLFTGSYAGK 1116
Cdd:cd18558   228 LEIAKRNGIKKAITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGEVLTVFFSVLIGAFSAGQ 294
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
1299-1450 2.30e-15

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: 79.37  E-value: 2.30e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1299 VSQEPMLF-NMSIYENIKFGKENATREDvkRACKFAAIDEF--IESLPNQYDTNvgpygksLSGGQKQRIAIARALLREP 1375
Cdd:COG4148    82 VFQEARLFpHLSVRGNLLYGRKRAPRAE--RRISFDEVVELlgIGHLLDRRPAT-------LSGGERQRVAIGRALLSSP 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1376 KILLLDEATSSLD--SNSEKL--IEKtivdIKDKADKTIITIAHRIASIKR-SDKIVVFNNpdrtGSfVQAQGTHEELLS 1450
Cdd:COG4148   153 RLLLMDEPLAALDlaRKAEILpyLER----LRDELDIPILYVSHSLDEVARlADHVVLLEQ----GR-VVASGPLAEVLS 223
cbiO PRK13641
energy-coupling factor transporter ATPase;
1164-1428 2.58e-15

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 78.33  E-value: 2.58e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYlsRPNVPIYK----DLTFSCESKKTTAIVGETGSGKSTvmslLMRFYDlkndhhivfkneqtgesskeqm 1239
Cdd:PRK13641    3 IKFENVDYIY--SPGTPMEKkgldNISFELEEGSFVALVGHTGSGKST----LMQHFN---------------------- 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1240 qqgdeeqnvgmknanefssskegadgqsSTLFKNSGKILLDGVDIC----DYNLKDLRNLFSIVSQ--EPMLFNMSIYEN 1313
Cdd:PRK13641   55 ----------------------------ALLKPSSGTITIAGYHITpetgNKNLKKLRKKVSLVFQfpEAQLFENTVLKD 106
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1314 IKFGKEN--ATREDVK-RACKFAAIDEFIESLPNQydtnvGPYgkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSN 1390
Cdd:PRK13641  107 VEFGPKNfgFSEDEAKeKALKWLKKVGLSEDLISK-----SPF--ELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPE 179
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 156095386 1391 SEKLIEKTIVDIKdKADKTIITIAHRIASI-KRSDKIVV 1428
Cdd:PRK13641  180 GRKEMMQLFKDYQ-KAGHTVILVTHNMDDVaEYADDVLV 217
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
1273-1459 3.11e-15

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: 76.81  E-value: 3.11e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1273 NSGKILLDGVDICDYNLKDLRNL-FSIVSQEPMLF-NMSIYENIKFGKENATREDVKRACKFAA-IDEF-IESLPNQYdt 1348
Cdd:cd03218    53 DSGKILLDGQDITKLPMHKRARLgIGYLPQEASIFrKLTVEENILAVLEIRGLSKKEREEKLEElLEEFhITHLRKSK-- 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1349 nvgpyGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIIT---------IAHRiAS 1419
Cdd:cd03218   131 -----ASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITdhnvretlsITDR-AY 204
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 156095386 1420 IKRSDKIVvfnnpdrtgsfvqAQGTHEELLSVQDgVYKKY 1459
Cdd:cd03218   205 IIYEGKVL-------------AEGTPEEIAANEL-VRKVY 230
ABC_6TM_MsbA_like cd18552
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ...
825-1109 3.54e-15

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: 77.85  E-value: 3.54e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  825 IAIIALSIMVAGGLYPLFALLyakyVGTLFDfaNLEANSNKYSLYILVIAI-AMF----ISETLKNYYNNVIGEKVEKTM 899
Cdd:cd18552     1 LALAILGMILVAATTAALAWL----LKPLLD--DIFVEKDLEALLLVPLAIiGLFllrgLASYLQTYLMAYVGQRVVRDL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  900 KLRLFENIMYQEISFFDQdsHAPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSTVMSFYFCP---IVAAVLTGTY 976
Cdd:cd18552    75 RNDLFDKLLRLPLSFFDR--NSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWkltLIALVVLPLA 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  977 FIFMRVFAIRARIAANKdvekkrvNQPGTAFVYNsddeifkdpsfLIQEAFYNMNTVIIYGLEDY----FCTLIEKAIDY 1052
Cdd:cd18552   153 ALPIRRIGKRLRKISRR-------SQESMGDLTS-----------VLQETLSGIRVVKAFGAEDYeikrFRKANERLRRL 214
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 156095386 1053 SNKGQKRKTLINSMlwgfSQsaqfFINSFA----YWFGSFLIRRGTIQVDDFMkSLFTFLF 1109
Cdd:cd18552   215 SMKIARARALSSPL----ME----LLGAIAialvLWYGGYQVISGELTPGEFI-SFITALL 266
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
1184-1428 3.63e-15

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


Pssm-ID: 443658 [Multi-domain]  Cd Length: 329  Bit Score: 78.62  E-value: 3.63e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1184 DLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYdlkndhhivfknEQTgesskeqmqqgdeeqnvgmknanefssskega 1263
Cdd:COG4608    36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLE------------EPT-------------------------------- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1264 dgqsstlfknSGKILLDGVDICDYNLKDLRNL---FSIVSQEPM--LfN--MSIYENIKFGKENATREDVkrackfAAID 1336
Cdd:COG4608    72 ----------SGEILFDGQDITGLSGRELRPLrrrMQMVFQDPYasL-NprMTVGDIIAEPLRIHGLASK------AERR 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1337 EFIESL-------PNQYDTnvgpYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLD-SnseklIEKTIV----DIKD 1404
Cdd:COG4608   135 ERVAELlelvglrPEHADR----YPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDvS-----IQAQVLnlleDLQD 205
                         250       260
                  ....*....|....*....|....*
gi 156095386 1405 KADKTIITIAHRIASIKR-SDKIVV 1428
Cdd:COG4608   206 ELGLTYLFISHDLSVVRHiSDRVAV 230
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
383-611 4.35e-15

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 78.92  E-value: 4.35e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHYDtrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDSHnLKDVNLKwwRSKI 462
Cdd:PRK11000    4 VTLRNVTKAYG---DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKR-MNDVPPA--ERGV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  463 GVVSQDPLLFSN-SIKNNIKYSLyslkdlealseesnedgfssqsdsnsrnscraKCAGdlndmiqtTDSTElIQVRKNy 541
Cdd:PRK11000   78 GMVFQSYALYPHlSVAENMSFGL--------------------------------KLAG--------AKKEE-INQRVN- 115
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  542 etiEDSEVVSvskkvLIHdfvsalpdkyetLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:PRK11000  116 ---QVAEVLQ-----LAH------------LLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD 165
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
1268-1417 4.51e-15

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 77.20  E-value: 4.51e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1268 STLFKN--------SGKILLDGVDIcDYNLKDLRNL---FSIVSQEP--MLFNMSIYENIKFG------KENATREDVKR 1328
Cdd:PRK13636   46 STLFQNlngilkpsSGRILFDGKPI-DYSRKGLMKLresVGMVFQDPdnQLFSASVYQDVSFGavnlklPEDEVRKRVDN 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1329 ACKFAAIdEFIESLPNQYdtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADK 1408
Cdd:PRK13636  125 ALKRTGI-EHLKDKPTHC----------LSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGL 193

                  ....*....
gi 156095386 1409 TIITIAHRI 1417
Cdd:PRK13636  194 TIIIATHDI 202
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
1153-1443 5.55e-15

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: 80.72  E-value: 5.55e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1153 KIKNSNDIKGKIEIMD-VNFRYLSRPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMrfydlkndhhivfkneqt 1231
Cdd:TIGR01271  412 KIKQNNKARKQPNGDDgLFFSNFSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIM------------------ 473
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1232 GESskeqmqqgdeeqnvgmknanefssskEGADGQsstlFKNSGKIlldgvdicdynlkdlrnlfSIVSQEPMLFNMSIY 1311
Cdd:TIGR01271  474 GEL--------------------------EPSEGK----IKHSGRI-------------------SFSPQTSWIMPGTIK 504
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1312 ENIKFG--KENATREDVKRACKfaaIDEFIESLPNQYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDS 1389
Cdd:TIGR01271  505 DNIIFGlsYDEYRYTSVIKACQ---LEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDV 581
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 156095386  1390 NSEKLIEKTIVdIKDKADKTIITIAHRIASIKRSDKIVVFNNPDR--TGSFVQAQG 1443
Cdd:TIGR01271  582 VTEKEIFESCL-CKLMSNKTRILVTSKLEHLKKADKILLLHEGVCyfYGTFSELQA 636
cbiO PRK13649
energy-coupling factor transporter ATPase;
383-661 6.90e-15

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 76.71  E-value: 6.90e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHYDTRKDVE--IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIIND---SHNLKDVNLKW 457
Cdd:PRK13649    3 INLQNVSYTYQAGTPFEgrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDtliTSTSKNKDIKQ 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  458 WRSKIGVVSQDP--LLFSNSIknnikyslysLKDLealseesnedGFSSQSDSNSRnscrakcagdlndmiqttdsteli 535
Cdd:PRK13649   83 IRKKVGLVFQFPesQLFEETV----------LKDV----------AFGPQNFGVSQ------------------------ 118
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  536 qvrknyetiEDSEVVSVSKKVLIHdfVSalpdkyETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSE 615
Cdd:PRK13649  119 ---------EEAEALAREKLALVG--IS------ESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGR 181
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 156095386  616 YLVQKTINNLkgNENRITIIIAHRL--STIRYANTIFVLsnrENGSTV 661
Cdd:PRK13649  182 KELMTLFKKL--HQSGMTIVLVTHLmdDVANYADFVYVL---EKGKLV 224
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
385-654 7.24e-15

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: 74.51  E-value: 7.24e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  385 FKNVRF---HYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLI--ERLYDPTEGDVIINDshnlKDVNLKWWR 459
Cdd:cd03213     6 FRNLTVtvkSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLING----RPLDKRSFR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  460 SKIGVVSQDPLLFSN-SIKNNIKYSlyslkdlealseesnedgfssqsdsnsrnscrAKCAGdlndmiqttdsteliqvr 538
Cdd:cd03213    82 KIIGYVPQDDILHPTlTVRETLMFA--------------------------------AKLRG------------------ 111
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  539 knyetiedsevvsvskkvlihdfvsalpdkyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLV 618
Cdd:cd03213   112 -----------------------------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQV 150
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 156095386  619 QKTINNLkGNENRITIIIAHRLSTIRYA--NTIFVLSN 654
Cdd:cd03213   151 MSLLRRL-ADTGRTIICSIHQPSSEIFElfDKLLLLSQ 187
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
1268-1398 7.27e-15

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


Pssm-ID: 440718 [Multi-domain]  Cd Length: 264  Bit Score: 76.28  E-value: 7.27e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1268 STLFK--------NSGKILLDGVDICdyNLKDLR--NLFSIVSQEPML---FNMSIYENI----KFGKenatREDVKRAC 1330
Cdd:COG1101    46 STLLNaiagslppDSGSILIDGKDVT--KLPEYKraKYIGRVFQDPMMgtaPSMTIEENLalayRRGK----RRGLRRGL 119
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156095386 1331 KFAAIDEFIES-------LPNQYDTNVGpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLD-SNSEKLIEKT 1398
Cdd:COG1101   120 TKKRRELFRELlatlglgLENRLDTKVG----LLSGGQRQALSLLMATLTKPKLLLLDEHTAALDpKTAALVLELT 191
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
383-652 8.33e-15

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 76.66  E-value: 8.33e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHY-DTRKDVEIY--KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDSHNLKDVNLKWWR 459
Cdd:PRK13633    5 IKCKNVSYKYeSNEESTEKLalDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWDIR 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  460 SKIGVVSQDPllfSNSIknnikyslyslkdLEALSEEsnEDGFssqsdsnsrnscrakcaGDLNDMIQTtdstELIQVRk 539
Cdd:PRK13633   85 NKAGMVFQNP---DNQI-------------VATIVEE--DVAF-----------------GPENLGIPP----EEIRER- 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  540 nyetIEDSevvsvSKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQ 619
Cdd:PRK13633  125 ----VDES-----LKKVGMYEYRRHAP-----------HLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVV 184
                         250       260       270
                  ....*....|....*....|....*....|...
gi 156095386  620 KTINNLKGNENRITIIIAHRLSTIRYANTIFVL 652
Cdd:PRK13633  185 NTIKELNKKYGITIILITHYMEEAVEADRIIVM 217
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
340-1420 1.00e-14

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: 79.95  E-value: 1.00e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   340 IILPNITEYMKslEATNNLYEIINrkplvENNQDGKKLKDIKKIQFKNVRFHYdtrkdVEIYKDLNFTLTEGKTYAFVGE 419
Cdd:TIGR01271  393 VEMVNVTASWD--EGIGELFEKIK-----QNNKARKQPNGDDGLFFSNFSLYV-----TPVLKNISFKLEKGQLLAVAGS 460
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   420 SGCGKSTILKLIERLYDPTEGDViindSHNlkdvnlkwwrSKIGVVSQDPLLFSNSIKNNIKYSLyslkdlealseesne 499
Cdd:TIGR01271  461 TGSGKSSLLMMIMGELEPSEGKI----KHS----------GRISFSPQTSWIMPGTIKDNIIFGL--------------- 511
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   500 dgfssqsdsnsrnscrakcagdlndmiqttdsteliqvrknyeTIEDSEVVSVSKKVLIHDFVSALPDKYETLVGSNASK 579
Cdd:TIGR01271  512 -------------------------------------------SYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGIT 548
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   580 LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEY-LVQKTINNLKGNENRItiIIAHRLSTIRYANTIFVLSNREN- 657
Cdd:TIGR01271  549 LSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKeIFESCLCKLMSNKTRI--LVTSKLEHLKKADKILLLHEGVCy 626
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   658 --GSTVDVDvlGEDPTKDSNEKNEKHDKQEKGGKNSS---------ANQKIGNAGSYI------IEQGTHDALMKNKNGI 720
Cdd:TIGR01271  627 fyGTFSELQ--AKRPDFSSLLLGLEAFDNFSAERRNSiltetlrrvSIDGDSTVFSGPetikqsFKQPPPEFAEKRKQSI 704
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   721 YYTMINNQKVSSKSSSNNDNDKDSDMKSSIYKDSERGYD--PDEANGNAKNESASAKKSEKMSDAK--------ASNTNA 790
Cdd:TIGR01271  705 ILNPIASARKFSFVQMGPQKAQATTIEDAVREPSERKFSlvPEDEQGEESLPRGNQYHHGLQHQAQrrqsvlqlMTHSNR 784
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   791 G-GRLAFLRNLFKRKPKAP-----------------------------------------NNLRVV------YREIFSYK 822
Cdd:TIGR01271  785 GeNRREQLQTSFRKKSSITqqnelaseldiysrrlskdsvyeiseeineedlkecfaderENVFETttwntyLRYITTNR 864
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   823 KDIAIIALSIM-----VAGGLYPLFaLLYAKYVGTLFDFANLEANSNKYSLYilviaiAMFISETLKNYYNNVIGEKVEK 897
Cdd:TIGR01271  865 NLVFVLIFCLViflaeVAASLLGLW-LITDNPSAPNYVDQQHANASSPDVQK------PVIITPTSAYYIFYIYVGTADS 937
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   898 TMKLRLFENI-MYQEISFFDQDSHAPGLLS------AHINRdvhlLKTGLVNN--------------IVIFThFIVLFL- 955
Cdd:TIGR01271  938 VLALGFFRGLpLVHTLLTVSKRLHEQMLHSvlqapmAVLNT----MKAGRILNrftkdmaiiddmlpLTLFD-FIQLTLi 1012
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   956 ------VSTVMSFYFcpIVAAVLTGTYFIFMRVFAIRAriaankDVEKKRVNQPGTAFVYnsddeifkdpSFLIQeAFYN 1029
Cdd:TIGR01271 1013 vlgaifVVSVLQPYI--FIAAIPVAVIFIMLRAYFLRT------SQQLKQLESEARSPIF----------SHLIT-SLKG 1073
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1030 MNTVIIYGLEDYFCTLIEKAIDysnkgqkrktlINSMLWgfsqsaqFFINSFAYWFgsfLIRRGTIQVDDFMKSLF-TFL 1108
Cdd:TIGR01271 1074 LWTIRAFGRQSYFETLFHKALN-----------LHTANW-------FLYLSTLRWF---QMRIDIIFVFFFIAVTFiAIG 1132
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1109 FTGSYAGKL-------MSLKG----------DSENAKLSFERYYPLITRKSLIDVRDNGGIKIKNSNDI----------- 1160
Cdd:TIGR01271 1133 TNQDGEGEVgiiltlaMNILStlqwavnssiDVDGLMRSVSRVFKFIDLPQEEPRPSGGGGKYQLSTVLvienphaqkcw 1212
                          970       980       990      1000      1010      1020      1030      1040
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1161 --KGKIEIMDVNFRYLSRPNVpIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRfydlkndhhivfkneqtgesskeq 1238
Cdd:TIGR01271 1213 psGGQMDVQGLTAKYTEAGRA-VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLR------------------------ 1267
                         1050      1060      1070      1080      1090      1100      1110      1120
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1239 mqqgdeeqnvgmknanefssskegadgqsstLFKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKfGK 1318
Cdd:TIGR01271 1268 -------------------------------LLSTEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLD-PY 1315
                         1130      1140      1150      1160      1170      1180      1190      1200
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1319 ENATREDVKRACKFAAIDEFIESLPNQYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKT 1398
Cdd:TIGR01271 1316 EQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKT 1395
                         1210      1220
                   ....*....|....*....|..
gi 156095386  1399 IVdiKDKADKTIITIAHRIASI 1420
Cdd:TIGR01271 1396 LK--QSFSNCTVILSEHRVEAL 1415
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
1174-1428 1.10e-14

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: 74.12  E-value: 1.10e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1174 LSRPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMrfydlkndhhivfkneqtgesskeqmqqgdeeqnvgmkna 1253
Cdd:cd03213    17 PSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALA---------------------------------------- 56
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1254 nefssskegadGQSSTLfKNSGKILLDGVDIcdyNLKDLRNLFSIVSQEPMLF-NMSIYENIKFGkenatredvkrackf 1332
Cdd:cd03213    57 -----------GRRTGL-GVSGEVLINGRPL---DKRSFRKIIGYVPQDDILHpTLTVRETLMFA--------------- 106
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1333 AAIdefieslpnqydtnvgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTIIT 1412
Cdd:cd03213   107 AKL-------------------RGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTG-RTIIC 166
                         250
                  ....*....|....*...
gi 156095386 1413 IAHRIAS--IKRSDKIVV 1428
Cdd:cd03213   167 SIHQPSSeiFELFDKLLL 184
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
383-644 1.10e-14

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


Pssm-ID: 443326 [Multi-domain]  Cd Length: 242  Bit Score: 75.43  E-value: 1.10e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHYDTrkdVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDSH-----NLKDVNLKW 457
Cdd:COG4161     3 IQLKNINCFYGS---HQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQfdfsqKPSEKAIRL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  458 WRSKIGVVSQdpllfsnsiknniKYSLYS-LKDLEALSEesnedgfssqsdsnsrnscrAKCagdlndmiqttdsteliQ 536
Cdd:COG4161    80 LRQKVGMVFQ-------------QYNLWPhLTVMENLIE--------------------APC-----------------K 109
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  537 VRKNYETIEDSEVVSVSKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEY 616
Cdd:COG4161   110 VLGLSKEQAREKAMKLLARLRLTDKADRFP-----------LHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITA 178
                         250       260
                  ....*....|....*....|....*....
gi 156095386  617 LVQKTINNLKGNEnrIT-IIIAHRLSTIR 644
Cdd:COG4161   179 QVVEIIRELSQTG--ITqVIVTHEVEFAR 205
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
402-626 1.34e-14

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: 74.78  E-value: 1.34e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  402 KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDSHNLKDV---------NLKwwRSKIGVVSQ----- 467
Cdd:COG4778    28 DGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWVDLaqaspreilALR--RRTIGYVSQflrvi 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  468 ----------DPLLfsnsiknnikyslyslkdlealseesnEDGFSsqsdsnsRNSCRAKcAGDLndmiqttdsteLIQV 537
Cdd:COG4778   106 prvsaldvvaEPLL---------------------------ERGVD-------REEARAR-AREL-----------LARL 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  538 RknyetiedsevvsvskkvlihdfvsaLPdkyETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYL 617
Cdd:COG4778   140 N--------------------------LP---ERLWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAV 190

                  ....*....
gi 156095386  618 VQKTINNLK 626
Cdd:COG4778   191 VVELIEEAK 199
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
396-643 1.39e-14

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: 74.18  E-value: 1.39e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  396 KDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDShnlKDVNLKWWRSKIGVVSQDPLLFSNs 475
Cdd:cd03268    11 GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGK---SYQKNIEALRRIGALIEAPGFYPN- 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  476 iknnikyslyslkdleaLSEEsnedgfssqsdSNSRNSCRAKcagdlndmiqttdsteliqvrknyeTIEDSEVVSVSKK 555
Cdd:cd03268    87 -----------------LTAR-----------ENLRLLARLL-------------------------GIRKKRIDEVLDV 113
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  556 VLIHDfvsaLPDKyetlvgsNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNEnrITII 635
Cdd:cd03268   114 VGLKD----SAKK-------KVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQG--ITVL 180

                  ....*....
gi 156095386  636 IA-HRLSTI 643
Cdd:cd03268   181 ISsHLLSEI 189
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
580-664 1.59e-14

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 78.31  E-value: 1.59e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  580 LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINN-LKGnenrITII-IAHRLSTIRYANTIFVLSNREN 657
Cdd:COG4178   486 LSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREeLPG----TTVIsVGHRSTLAAFHDRVLELTGDGS 561

                  ....*..
gi 156095386  658 GSTVDVD 664
Cdd:COG4178   562 WQLLPAE 568
urea_trans_UrtE TIGR03410
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ...
1268-1411 1.78e-14

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: 74.48  E-value: 1.78e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1268 STLFK--------NSGKILLDGVDICDYNLKDL-RNLFSIVSQEPMLF-NMSIYENIKFGKENATREDVKrackfaaIDE 1337
Cdd:TIGR03410   40 TTLLKtlmgllpvKSGSIRLDGEDITKLPPHERaRAGIAYVPQGREIFpRLTVEENLLTGLAALPRRSRK-------IPD 112
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156095386  1338 FIESLPNQYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTII 1411
Cdd:TIGR03410  113 EIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAIL 186
CeuD COG4604
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ...
1164-1449 1.82e-14

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


Pssm-ID: 443654 [Multi-domain]  Cd Length: 252  Bit Score: 74.73  E-value: 1.82e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYlsrPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRfydlkndhhivfkneqtgesskeqmqqgd 1243
Cdd:COG4604     2 IEIKNVSKRY---GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISR----------------------------- 49
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 eeqnvgmknanefssskegadgqssTLFKNSGKILLDGVDICDYNLKDL-RNLfSIVSQEPMlFNM--SIYENIKFG--- 1317
Cdd:COG4604    50 -------------------------LLPPDSGEVLVDGLDVATTPSRELaKRL-AILRQENH-INSrlTVRELVAFGrfp 102
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1318 --KENATREDVkrackfAAIDEFI-----ESLPNQY-DTnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDS 1389
Cdd:COG4604   103 ysKGRLTAEDR------EIIDEAIayldlEDLADRYlDE--------LSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDM 168
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 156095386 1390 NSEKLIEKTIVDIKDKADKTIITIAHRI--ASiKRSDKIVVFNNpdrtGSfVQAQGTHEELL 1449
Cdd:COG4604   169 KHSVQMMKLLRRLADELGKTVVIVLHDInfAS-CYADHIVAMKD----GR-VVAQGTPEEII 224
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
1184-1417 1.96e-14

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 76.04  E-value: 1.96e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1184 DLTFSCESKKTTAIVGETGSGKSTvmsLLMRFYDLKndhhivfkneqtgESSKEQMQQGDeeqnvgMKNANEFssskega 1263
Cdd:PRK13631   44 NISYTFEKNKIYFIIGNSGSGKST---LVTHFNGLI-------------KSKYGTIQVGD------IYIGDKK------- 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1264 DGQSSTLFKNSGKIlldgvdicdYNLKDLRNLFSIVSQEP--MLFNMSIYENIKFGKEN--ATREDVKRACKFaaideFI 1339
Cdd:PRK13631   95 NNHELITNPYSKKI---------KNFKELRRRVSMVFQFPeyQLFKDTIEKDIMFGPVAlgVKKSEAKKLAKF-----YL 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 156095386 1340 ESLPNQYD-TNVGPYGksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKdKADKTIITIAHRI 1417
Cdd:PRK13631  161 NKMGLDDSyLERSPFG--LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAK-ANNKTVFVITHTM 236
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
383-656 2.03e-14

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 75.11  E-value: 2.03e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHYDtrKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIIN------DSHNLKDVnlk 456
Cdd:PRK13639    2 LETRDLKYSYP--DGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKgepikyDKKSLLEV--- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  457 wwRSKIGVVSQDP--LLFSNSIKNNIKYSLYSLKdleaLSEESNEDgfssqsdsnsrnscRAKCAgdlndmiqttdstel 534
Cdd:PRK13639   77 --RKTVGIVFQNPddQLFAPTVEEDVAFGPLNLG----LSKEEVEK--------------RVKEA--------------- 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  535 iqvrknyetiedsevvsvSKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS 614
Cdd:PRK13639  122 ------------------LKAVGMEGFENKPP-----------HHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMG 172
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 156095386  615 EYLVQKTINNLkgNENRITIIIA-HRLSTI-RYANTIFVLSNRE 656
Cdd:PRK13639  173 ASQIMKLLYDL--NKEGITIIIStHDVDLVpVYADKVYVMSDGK 214
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
383-649 2.24e-14

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: 73.67  E-value: 2.24e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHYDTRKdveIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDsHNLKDVNLKWwRSKI 462
Cdd:COG4133     3 LEAENLSCRRGERL---LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNG-EPIRDAREDY-RRRL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  463 GVVSQDPLLFSNsiknnikyslysLKDLEALSeesnedgFSSQSDSNSRNscrakcAGDLNDMIQTTDSTELIQVRknye 542
Cdd:COG4133    78 AYLGHADGLKPE------------LTVRENLR-------FWAALYGLRAD------REAIDEALEAVGLAGLADLP---- 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  543 tiedsevvsvskkvlihdfvsalpdkyetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI 622
Cdd:COG4133   129 ----------------------------------VRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELI 174
                         250       260
                  ....*....|....*....|....*..
gi 156095386  623 NNLKGNeNRITIIIAHRLSTIRYANTI 649
Cdd:COG4133   175 AAHLAR-GGAVLLTTHQPLELAAARVL 200
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
1273-1448 2.56e-14

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 76.28  E-value: 2.56e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1273 NSGKILLDGVDICDYNLKDLRNLFsiVSQEPMLF-NMSIYENIKFG------KENATREDVKRacKFAAIDEFI--ESLP 1343
Cdd:PRK10851   55 TSGHIRFHGTDVSRLHARDRKVGF--VFQHYALFrHMTVFDNIAFGltvlprRERPNAAAIKA--KVTQLLEMVqlAHLA 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1344 NQYDTNvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH-RIASIKR 1422
Cdd:PRK10851  131 DRYPAQ-------LSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHdQEEAMEV 203
                         170       180
                  ....*....|....*....|....*.
gi 156095386 1423 SDKIVVFNNpdrtGSFVQAqGTHEEL 1448
Cdd:PRK10851  204 ADRVVVMSQ----GNIEQA-GTPDQV 224
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
1164-1431 2.56e-14

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 74.77  E-value: 2.56e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYlsRPNVPIYKDLTFSCESKKTTAIVGETGSGKSTvmsLLMRFydlkNDHHIVfkneqtgesskeqmQQGd 1243
Cdd:PRK13647    5 IEVEDLHFRY--KDGTKALKGLSLSIPEGSKTALLGPNGAGKST---LLLHL----NGIYLP--------------QRG- 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 eeqnvgmknanefssskegadgqsstlfknsgKILLDGVDICDYNLKDLRNLFSIVSQEP--MLFNMSIYENIKFGKENA 1321
Cdd:PRK13647   61 --------------------------------RVKVMGREVNAENEKWVRSKVGLVFQDPddQVFSSTVWDDVAFGPVNM 108
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1322 --TREDVKR----ACKFAAIDEFIESLPNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLI 1395
Cdd:PRK13647  109 glDKDEVERrveeALKAVRMWDFRDKPPYH-----------LSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETL 177
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 156095386 1396 eKTIVDIKDKADKTIITIAHRI-ASIKRSDKIVVFNN 1431
Cdd:PRK13647  178 -MEILDRLHNQGKTVIVATHDVdLAAEWADQVIVLKE 213
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
371-611 2.86e-14

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 75.91  E-value: 2.86e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  371 NQDGKKLKDIKKiqfknvRFHYDTRKDveiykDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIInDSHNL 450
Cdd:PRK11432    3 QKNFVVLKNITK------RFGSNTVID-----NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFI-DGEDV 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  451 KDVNLKwwRSKIGVVSQDPLLFSN-SIKNNIKyslYSLKDLEALSEESNEdgfssqsdsnsrnscRAKCAGDLNDMiqtt 529
Cdd:PRK11432   71 THRSIQ--QRDICMVFQSYALFPHmSLGENVG---YGLKMLGVPKEERKQ---------------RVKEALELVDL---- 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  530 dsteliqvrknyETIEDSEVvsvskkvlihdfvsalpdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSS 609
Cdd:PRK11432  127 ------------AGFEDRYV----------------------------DQISGGQQQRVALARALILKPKVLLFDEPLSN 166

                  ..
gi 156095386  610 LD 611
Cdd:PRK11432  167 LD 168
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
383-652 3.14e-14

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 75.06  E-value: 3.14e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHYDTRKDVE---IYkDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIIND---SHNLKDVNLK 456
Cdd:PRK13634    3 ITFQKVEHRYQYKTPFErraLY-DVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGErviTAGKKNKKLK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  457 WWRSKIGVVSQDP--LLFSNSIknnikyslysLKDLealseesnedgfssqsdsnsrnscrakCAGDLNDMIQTTDSTel 534
Cdd:PRK13634   82 PLRKKVGIVFQFPehQLFEETV----------EKDI---------------------------CFGPMNFGVSEEDAK-- 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  535 iqvRKNYETIedsEVVSVSKKVLIHD-FvsalpdkyetlvgsnasKLSGGQKQRISIARAIIRNPKILILDEATSSLDNK 613
Cdd:PRK13634  123 ---QKAREMI---ELVGLPEELLARSpF-----------------ELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPK 179
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 156095386  614 SEYLVQKTINNLKGNENRITIIIAHRLSTI-RYANTIFVL 652
Cdd:PRK13634  180 GRKEMMEMFYKLHKEKGLTTVLVTHSMEDAaRYADQIVVM 219
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
383-611 3.67e-14

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 73.64  E-value: 3.67e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHYDTRkdveiYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIIND-SHNLKDVNlkwwRSK 461
Cdd:COG3840     2 LRLDDLTYRYGDF-----PLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGqDLTALPPA----ERP 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  462 IGVVSQDPLLFSN-SIKNNIkyslyslkdleALseesnedGFSSqsdsnsrnSCRakcagdLNDmiqttdsteliqvrkn 540
Cdd:COG3840    73 VSMLFQENNLFPHlTVAQNI-----------GL-------GLRP--------GLK------LTA---------------- 104
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 156095386  541 yetIEDSEVVSVSKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:COG3840   105 ---EQRAQVEQALERVGLAGLLDRLP-----------GQLSGGQRQRVALARCLVRKRPILLLDEPFSALD 161
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
1275-1450 3.92e-14

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


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 76.23  E-value: 3.92e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1275 GKILLDGVDICDYNLKDLRNL----FSIVSQE-PMLFNMSIYENIKFGKENA------TREDVKRACKFAAIDEFIESLP 1343
Cdd:PRK10070   83 GQVLIDGVDIAKISDAELREVrrkkIAMVFQSfALMPHMTVLDNTAFGMELAginaeeRREKALDALRQVGLENYAHSYP 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1344 NQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR- 1422
Cdd:PRK10070  163 DE-----------LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRi 231
                         170       180
                  ....*....|....*....|....*...
gi 156095386 1423 SDKIVVFNNpdrtGSFVQAqGTHEELLS 1450
Cdd:PRK10070  232 GDRIAIMQN----GEVVQV-GTPDEILN 254
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
1262-1448 4.31e-14

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 76.03  E-value: 4.31e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1262 GADG-QSSTLFK--------NSGKILLDGVDICDynLKDLRNLFSIVSQEPMLF-NMSIYENIKFG------KENATRED 1325
Cdd:PRK11607   52 GASGcGKSTLLRmlagfeqpTAGQIMLDGVDLSH--VPPYQRPINMMFQSYALFpHMTVEQNIAFGlkqdklPKAEIASR 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1326 VKRACKFAAIDEFIESLPNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDK 1405
Cdd:PRK11607  130 VNEMLGLVHMQEFAKRKPHQ-----------LSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILER 198
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 156095386 1406 ADKTIITIAH-RIASIKRSDKIVVFNNpdrtGSFVQAqGTHEEL 1448
Cdd:PRK11607  199 VGVTCVMVTHdQEEAMTMAGRIAIMNR----GKFVQI-GEPEEI 237
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...
1268-1447 4.83e-14

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: 73.92  E-value: 4.83e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1268 STLFK--------NSGKILLDGVDICDYNLKDLRNL-----FsivsQEPMLF-NMSIYENIKFG---------------- 1317
Cdd:COG0411    44 TTLFNlitgfyrpTSGRILFDGRDITGLPPHRIARLgiartF----QNPRLFpELTVLENVLVAaharlgrgllaallrl 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1318 -----KENATREDVKRACKFAAIDEFIESLPnqydtnvgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSN-S 1391
Cdd:COG0411   120 prarrEEREARERAEELLERVGLADRADEPA-----------GNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEeT 188
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 156095386 1392 EKLIEkTIVDIKDKADKTIITIAHRIASIKR-SDKIVVFNNpdrtGSfVQAQGTHEE 1447
Cdd:COG0411   189 EELAE-LIRRLRDERGITILLIEHDMDLVMGlADRIVVLDF----GR-VIAEGTPAE 239
SapF COG4167
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
1164-1458 5.07e-14

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


Pssm-ID: 443328 [Multi-domain]  Cd Length: 265  Bit Score: 73.72  E-value: 5.07e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRY------LSRPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfkneqtgesske 1237
Cdd:COG4167     5 LEVRNLSKTFkyrtglFRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKML------------------------- 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1238 qmqqgdeeqnVGMknanefssskegadgQSSTlfknSGKILLDGVDICDYNLKDLRNLFSIVSQEPmlfNMSIYENIKFG 1317
Cdd:COG4167    60 ----------AGI---------------IEPT----SGEILINGHKLEYGDYKYRCKHIRMIFQDP---NTSLNPRLNIG 107
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1318 -------KENATREDVKRACKFAAIDEFIESLPNQYDTnvgpYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSN 1390
Cdd:COG4167   108 qileeplRLNTDLTAEEREERIFATLRLVGLLPEHANF----YPHMLSSGQKQRVALARALILQPKIIIADEALAALDMS 183
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 156095386 1391 SEKLIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVVFNNpdrtGSFVQAQGTHEELLSVQDGVYKK 1458
Cdd:COG4167   184 VRSQIINLMLELQEKLGISYIYVSQHLGIVKHiSDKVLVMHQ----GEVVEYGKTAEVFANPQHEVTKR 248
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
1164-1448 5.40e-14

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: 72.92  E-value: 5.40e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYLSRPNvPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfkneqTGEsskeqmqqgd 1243
Cdd:cd03263     1 LQIRNLTKTYKKGTK-PAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKML------------------TGE---------- 51
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 eeqnvgmknanefssskegadgqsstLFKNSGKILLDGVDIcDYNLKDLRNLFSIVSQEPMLF-NMSIYENIKF-----G 1317
Cdd:cd03263    52 --------------------------LRPTSGTAYINGYSI-RTDRKAARQSLGYCPQFDALFdELTVREHLRFyarlkG 104
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1318 KENATREDVkrackfaaIDEFIE--SLPNQYDTNVgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLI 1395
Cdd:cd03263   105 LPKSEIKEE--------VELLLRvlGLTDKANKRA----RTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAI 172
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 156095386 1396 EKTIVDIkdKADKTIITIAHRIASIKR-SDKIVVFNNpdrtGSfVQAQGTHEEL 1448
Cdd:cd03263   173 WDLILEV--RKGRSIILTTHSMDEAEAlCDRIAIMSD----GK-LRCIGSPQEL 219
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
1147-1450 5.48e-14

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: 74.12  E-value: 5.48e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1147 RDNGGIKIKNSNDikgkieimDVNFRYLSRPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMrfydlkndhhivf 1226
Cdd:cd03291    26 QENNDRKHSSDDN--------NLFFSNLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLIL------------- 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1227 kneqtgesskeqmqqGDEEQnvgmknanefssskegadgqSSTLFKNSGKIlldgvdicdynlkdlrnlfSIVSQEPMLF 1306
Cdd:cd03291    85 ---------------GELEP--------------------SEGKIKHSGRI-------------------SFSSQFSWIM 110
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1307 NMSIYENIKFG--KENATREDVKRACKfaaIDEFIESLPNQYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEAT 1384
Cdd:cd03291   111 PGTIKENIIFGvsYDEYRYKSVVKACQ---LEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPF 187
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156095386 1385 SSLDSNSEKLIEKTIVdIKDKADKTIITIAHRIASIKRSDKIVVFNNPDR--TGSFVQAQGTHEELLS 1450
Cdd:cd03291   188 GYLDVFTEKEIFESCV-CKLMANKTRILVTSKMEHLKKADKILILHEGSSyfYGTFSELQSLRPDFSS 254
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
1268-1431 5.50e-14

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: 72.61  E-value: 5.50e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1268 STLFK-NSGKILLDGVDICDYNLKdLRNLFSIVSQEPMLF-NMSIYENIKF----GKENATREDvkrackfAAIDEFIEs 1341
Cdd:cd03264    46 ATLTPpSSGTIRIDGQDVLKQPQK-LRRRIGYLPQEFGVYpNFTVREFLDYiawlKGIPSKEVK-------ARVDEVLE- 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1342 lpnqyDTNVGPYGK----SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIkdKADKTIITIAHRI 1417
Cdd:cd03264   117 -----LVNLGDRAKkkigSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSEL--GEDRIVILSTHIV 189
                         170
                  ....*....|....*
gi 156095386 1418 ASIKRS-DKIVVFNN 1431
Cdd:cd03264   190 EDVESLcNQVAVLNK 204
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
1181-1431 6.59e-14

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: 72.69  E-value: 6.59e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1181 IYKDLTFSCESKKTTAIVGETGSGKSTVMSLLM-RFYDLKNDHHIVFKNEQtgESSKEQMQqgdeeqnvgmknanefsss 1259
Cdd:cd03234    22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISgRVEGGGTTSGQILFNGQ--PRKPDQFQ------------------- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1260 kegadgqsstlfknsgkilldgvDICDYNLKDLRNLFSIVSQEPMLFnmsiYENIKFGKENATREDVKRACkfaaidefI 1339
Cdd:cd03234    81 -----------------------KCVAYVRQDDILLPGLTVRETLTY----TAILRLPRKSSDAIRKKRVE--------D 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1340 ESLPNQYDTNVG-PYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKdKADKTIITIAHRia 1418
Cdd:cd03234   126 VLLRDLALTRIGgNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLA-RRNRIVILTIHQ-- 202
                         250
                  ....*....|...
gi 156095386 1419 siKRSDKIVVFNN 1431
Cdd:cd03234   203 --PRSDLFRLFDR 213
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
383-663 8.00e-14

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 72.82  E-value: 8.00e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHYDtrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIIND-SHNLKDVNLKWWRSK 461
Cdd:PRK09493    2 IEFKNVSKHFG---PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGlKVNDPKVDERLIRQE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  462 IGVVSQDPLLFSNsiknnikyslyslkdLEALSeesnedgfssqsdsnsrnscrakcagdlNDMIQTtdstelIQVRKny 541
Cdd:PRK09493   79 AGMVFQQFYLFPH---------------LTALE----------------------------NVMFGP------LRVRG-- 107
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  542 etiedsevvsvSKKVLIHDFVSALPDKyetlVGSNA------SKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSE 615
Cdd:PRK09493  108 -----------ASKEEAEKQARELLAK----VGLAErahhypSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELR 172
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 156095386  616 YLVQKTINNLkGNENRITIIIAHRLSTIRYANT--IFVLSNR--ENGSTVDV 663
Cdd:PRK09493  173 HEVLKVMQDL-AEEGMTMVIVTHEIGFAEKVASrlIFIDKGRiaEDGDPQVL 223
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
1183-1432 8.73e-14

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: 75.88  E-value: 8.73e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1183 KDLTFSCESKKTTAIVGETGSGKSTVMSLLMRfydlkndhhivfkneqtgesskeqmqqgdeeqnvgmknanefssskeg 1262
Cdd:COG4172   303 DGVSLTLRRGETLGLVGESGSGKSTLGLALLR------------------------------------------------ 334
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1263 adgqsstLFKNSGKILLDGVDICDYNLKDLRNL---FSIVSQEPM-LFN--MSIYENI-------KFGKENATREDvkRA 1329
Cdd:COG4172   335 -------LIPSEGEIRFDGQDLDGLSRRALRPLrrrMQVVFQDPFgSLSprMTVGQIIaeglrvhGPGLSAAERRA--RV 405
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1330 CkfAAIDEfieslpnqydtnVG--P-----YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDsnseKLIEKTIVDI 1402
Cdd:COG4172   406 A--EALEE------------VGldPaarhrYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALD----VSVQAQILDL 467
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 156095386 1403 -KDKADKT-----IIT--------IAHRIASIKRSdKIV-------VFNNP 1432
Cdd:COG4172   468 lRDLQREHglaylFIShdlavvraLAHRVMVMKDG-KVVeqgpteqVFDAP 517
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
402-673 8.98e-14

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


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 75.07  E-value: 8.98e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  402 KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIIN--DSHNLKDVNLKW-WRSKIGVVSQDPLLFSN-SIK 477
Cdd:PRK10070   45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDgvDIAKISDAELREvRRKKIAMVFQSFALMPHmTVL 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  478 NNIKYSLyslkDLEALSEESNEDgfssqsdsnsrnscrakcagdlndmiqttdsteliqvrknyetiedsEVVSVSKKVL 557
Cdd:PRK10070  125 DNTAFGM----ELAGINAEERRE-----------------------------------------------KALDALRQVG 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  558 IHDFVSALPDKyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIA 637
Cdd:PRK10070  154 LENYAHSYPDE-----------LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFIS 222
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 156095386  638 HRL-STIRYANTIFVLSNRENGSTVDVDVLGEDPTKD 673
Cdd:PRK10070  223 HDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNNPAND 259
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
1270-1388 1.21e-13

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 71.92  E-value: 1.21e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1270 LFKNSGKILLDGVDiCDYNLKDLRNLfSIVSQEPMLFN-MSIYENIKFG-----KENAT-REDVKRACKFAAIDEFIESL 1342
Cdd:PRK10771   49 LTPASGSLTLNGQD-HTTTPPSRRPV-SMLFQENNLFShLTVAQNIGLGlnpglKLNAAqREKLHAIARQMGIEDLLARL 126
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 156095386 1343 PNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLD 1388
Cdd:PRK10771  127 PGQ-----------LSGGQRQRVALARCLVREQPILLLDEPFSALD 161
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
1171-1428 1.78e-13

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: 71.24  E-value: 1.78e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1171 FRYLSRPNVPIyKDLTFSCESKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfkneqtgesskeqmqqgdeeqnvgm 1250
Cdd:cd03266    11 FRDVKKTVQAV-DGVSFTVKPGEVTGLLGPNGAGKTTTLRML-------------------------------------- 51
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1251 knanefssskegadgqsSTLFK-NSGKILLDGVDICDYNLKDLRNLfSIVSQEPMLFN-MSIYENIKFgkeNATREDVKR 1328
Cdd:cd03266    52 -----------------AGLLEpDAGFATVDGFDVVKEPAEARRRL-GFVSDSTGLYDrLTARENLEY---FAGLYGLKG 110
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1329 ACKFAAIDEFIESLpnqydtNVGPY----GKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKD 1404
Cdd:cd03266   111 DELTARLEELADRL------GMEELldrrVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRA 184
                         250       260
                  ....*....|....*....|....*
gi 156095386 1405 kADKTIITIAHRIASIKR-SDKIVV 1428
Cdd:cd03266   185 -LGKCILFSTHIMQEVERlCDRVVV 208
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
1273-1418 2.05e-13

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 71.66  E-value: 2.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1273 NSGKILLDGVDICDYNLKD--LRNLFSIVSQEPMLF-NMSIYENIKFGKENatredVKRACKFAAIDEFIESLpnqydTN 1349
Cdd:PRK09493   54 TSGDLIVDGLKVNDPKVDErlIRQEAGMVFQQFYLFpHLTALENVMFGPLR-----VRGASKEEAEKQARELL-----AK 123
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156095386 1350 VG------PYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSnseKLIEKTIVDIKDKADK--TIITIAHRIA 1418
Cdd:PRK09493  124 VGlaerahHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDP---ELRHEVLKVMQDLAEEgmTMVIVTHEIG 197
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
383-654 2.36e-13

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: 70.77  E-value: 2.36e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHYdtrKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDSHNLKDVnlkwwRSKI 462
Cdd:cd03269     1 LEVENVTKRF---GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA-----RNRI 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  463 GVVSQDPLLFSN-SIKNNIKY--SLYSLKDLEALSEesnedgfssqsdsnsrnscrakcagdlndmiqttdSTELIqvrK 539
Cdd:cd03269    73 GYLPEERGLYPKmKVIDQLVYlaQLKGLKKEEARRR-----------------------------------IDEWL---E 114
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  540 NYEtIEDSEvvsvSKKVlihdfvsalpdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQ 619
Cdd:cd03269   115 RLE-LSEYA----NKRV---------------------EELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLK 168
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 156095386  620 KTINNLKGNENRItIIIAHRLSTI-RYANTIFVLSN 654
Cdd:cd03269   169 DVIRELARAGKTV-ILSTHQMELVeELCDRVLLLNK 203
cbiO PRK13641
energy-coupling factor transporter ATPase;
383-652 2.38e-13

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 72.17  E-value: 2.38e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHYDTRKDVEI--YKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDSH---NLKDVNLKW 457
Cdd:PRK13641    3 IKFENVDYIYSPGTPMEKkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHitpETGNKNLKK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  458 WRSKIGVVSQDP--LLFSNSIKNNIKYSLYSLkdlealseesnedGFSSQsdsnsrnscRAKcagdlndmiqttdsteli 535
Cdd:PRK13641   83 LRKKVSLVFQFPeaQLFENTVLKDVEFGPKNF-------------GFSED---------EAK------------------ 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  536 qvrknyetiedSEVVSVSKKVlihdfvsALPdkyETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSE 615
Cdd:PRK13641  123 -----------EKALKWLKKV-------GLS---EDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGR 181
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 156095386  616 YLVQKTINNLKgNENRITIIIAHRLSTI-RYANTIFVL 652
Cdd:PRK13641  182 KEMMQLFKDYQ-KAGHTVILVTHNMDDVaEYADDVLVL 218
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
1164-1419 3.55e-13

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 70.81  E-value: 3.55e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYLSRPnvpIYKDLTFSCESKKTTAIVGETGSGKSTvmslLMRFYDLkndhhivFKNEQTGESSKEQmqqgd 1243
Cdd:PRK11124    3 IQLNGINCFYGAHQ---ALFDITLDCPQGETLVLLGPSGAGKSS----LLRVLNL-------LEMPRSGTLNIAG----- 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 eeqnvgmknaNEFSSSKEGADGQSSTLFKNSGKILLDgvdicdYNLkdlrnlfsivsqEPmlfNMSIYENI--------K 1315
Cdd:PRK11124   64 ----------NHFDFSKTPSDKAIRELRRNVGMVFQQ------YNL------------WP---HLTVQQNLieapcrvlG 112
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1316 FGKENAtredVKRACKFAA---IDEFIESLPNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNse 1392
Cdd:PRK11124  113 LSKDQA----LARAEKLLErlrLKPYADRFPLH-----------LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPE-- 175
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 156095386 1393 klIEKTIVDIKDKADKTIIT---------IAHRIAS 1419
Cdd:PRK11124  176 --ITAQIVSIIRELAETGITqvivtheveVARKTAS 209
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
580-657 3.56e-13

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: 69.10  E-value: 3.56e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 156095386  580 LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnenrITII-IAHRLSTIRYANTIFVLSNREN 657
Cdd:cd03223    92 LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELG-----ITVIsVGHRPSLWKFHDRVLDLDGEGG 165
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
1268-1462 3.94e-13

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 71.26  E-value: 3.94e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1268 STLF--------KNSGKILLDGVDIcDYNLKDL---RNLFSIVSQEP--MLFNMSIYENIKFG------KENATREDVKR 1328
Cdd:PRK13639   42 STLFlhfngilkPTSGEVLIKGEPI-KYDKKSLlevRKTVGIVFQNPddQLFAPTVEEDVAFGplnlglSKEEVEKRVKE 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1329 ACKFAAIDEFIESLPNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdK 1408
Cdd:PRK13639  121 ALKAVGMEGFENKPPHH-----------LSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEG-I 188
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 156095386 1409 TIITIAHRIASI-KRSDKIVVFNNpdrtGSFVqAQGTHEELLSVQDGVYKKYVKL 1462
Cdd:PRK13639  189 TIIISTHDVDLVpVYADKVYVMSD----GKII-KEGTPKEVFSDIETIRKANLRL 238
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
1271-1450 4.42e-13

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 71.28  E-value: 4.42e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1271 FKNSGKILLDGVDICDY-NLKDLRNLFSIVSQEPMLFNMSIYENIKFGKenatredvkRACKFAAIDEFiESLPNQYDTN 1349
Cdd:PRK14271   77 YRYSGDVLLGGRSIFNYrDVLEFRRRVGMLFQRPNPFPMSIMDNVLAGV---------RAHKLVPRKEF-RGVAQARLTE 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1350 VGPYGK----------SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdkTIITIAHRIAS 1419
Cdd:PRK14271  147 VGLWDAvkdrlsdspfRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQ 224
                         170       180       190
                  ....*....|....*....|....*....|..
gi 156095386 1420 IKR-SDKIVVFNNpdrtGSFVQaQGTHEELLS 1450
Cdd:PRK14271  225 AARiSDRAALFFD----GRLVE-EGPTEQLFS 251
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
402-611 6.79e-13

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 70.49  E-value: 6.79e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  402 KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDS--HNLKDVNLKWWRSKIGVVSQDPLlfsnsiknn 479
Cdd:PRK10419   29 NNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEplAKLNRAQRKAFRRDIQMVFQDSI--------- 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  480 ikyslyslkdlealseesnedgfssqSDSNSRNSCRAKCAGDLNDMIQTTDSTELIQVRKNYETIEdsevvsvskkvLIH 559
Cdd:PRK10419  100 --------------------------SAVNPRKTVREIIREPLRHLLSLDKAERLARASEMLRAVD-----------LDD 142
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 156095386  560 DFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:PRK10419  143 SVLDKRP-----------PQLSGGQLQRVCLARALAVEPKLLILDEAVSNLD 183
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
1176-1452 7.38e-13

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 73.35  E-value: 7.38e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1176 RPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYdlkndhhivfknEQTG-ESSKEQMqqgdeeqnvgmknan 1254
Cdd:PRK10261   26 QQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLL------------EQAGgLVQCDKM--------------- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1255 efssskegadgqsstLFKNSGKILLDGVDICDYNLKDLRNL-FSIVSQEPM-----LFNM--SIYENIK----FGKENAT 1322
Cdd:PRK10261   79 ---------------LLRRRSRQVIELSEQSAAQMRHVRGAdMAMIFQEPMtslnpVFTVgeQIAESIRlhqgASREEAM 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1323 REdVKRACKFAAIDEfieslpnqYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDI 1402
Cdd:PRK10261  144 VE-AKRMLDQVRIPE--------AQTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVL 214
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 156095386 1403 KDKADKTIITIAHriasikrsDKIVVFNNPDRTgsFVQAQGTHEELLSVQ 1452
Cdd:PRK10261  215 QKEMSMGVIFITH--------DMGVVAEIADRV--LVMYQGEAVETGSVE 254
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
1177-1450 8.62e-13

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 72.64  E-value: 8.62e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1177 PNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYdlkndhhivfkNEQTGEsskeqMQQGDEEQNvgmknanef 1256
Cdd:PRK11288   15 PGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNY-----------QPDAGS-----ILIDGQEMR--------- 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1257 ssskegadgqsstlFKNSGKILLDGVdicdynlkdlrnlfSIVSQEPMLF-NMSIYENI-------KFG--KENATREDV 1326
Cdd:PRK11288   70 --------------FASTTAALAAGV--------------AIIYQELHLVpEMTVAENLylgqlphKGGivNRRLLNYEA 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1327 KRacKFAAIDEFIEslPnqyDTNVgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDS-NSEKLIeKTIVDIKDK 1405
Cdd:PRK11288  122 RE--QLEHLGVDID--P---DTPL----KYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSArEIEQLF-RVIRELRAE 189
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 156095386 1406 AdKTIITIAHRIASIKR-SDKIVVFnnpdRTGSFVQ-----AQGTHEELLS 1450
Cdd:PRK11288  190 G-RVILYVSHRMEEIFAlCDAITVF----KDGRYVAtfddmAQVDRDQLVQ 235
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
393-611 1.23e-12

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: 68.93  E-value: 1.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  393 DTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIIND---SHNLKDVnlkwwRSKIGVVSQDP 469
Cdd:cd03266    13 DVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfdvVKEPAEA-----RRRLGFVSDST 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  470 LLFSN-SIKNNIKY--SLYSLKDLEALseesnedgfssqsdsnsrnscrakcaGDLNDMIQTTDSTELIQVRknyetied 546
Cdd:cd03266    88 GLYDRlTARENLEYfaGLYGLKGDELT--------------------------ARLEELADRLGMEELLDRR-------- 133
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156095386  547 sevvsvskkvlihdfvsalpdkyetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:cd03266   134 ------------------------------VGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLD 168
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
397-681 1.39e-12

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 69.31  E-value: 1.39e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  397 DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERL---YDP---TEGDVII--NDSHNLKDVNLkwwRSKIGVVSQD 468
Cdd:PRK14246   22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiYDSkikVDGKVLYfgKDIFQIDAIKL---RKEVGMVFQQ 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  469 PLLFSN-SIKNNIKYSLYSlkdlealseesnedgfssqsdsnsrnscrakcagdlndmiqttdstELIQVRKNYETIEDS 547
Cdd:PRK14246   99 PNPFPHlSIYDNIAYPLKS----------------------------------------------HGIKEKREIKKIVEE 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  548 EVVSVSKKVLIHDFVSalpdkyetlvgSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKg 627
Cdd:PRK14246  133 CLRKVGLWKEVYDRLN-----------SPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELK- 200
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 156095386  628 NENRITIIIAHRLSTIRYANTIFVLSnreNGSTVDVDVLGEDPTKDSNEKNEKH 681
Cdd:PRK14246  201 NEIAIVIVSHNPQQVARVADYVAFLY---NGELVEWGSSNEIFTSPKNELTEKY 251
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
400-643 1.43e-12

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: 69.88  E-value: 1.43e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDpTEGDVIInDSHNLKDVNLKWWRSKIGVVSQDPLLFSNSIKNN 479
Cdd:cd03289    19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQI-DGVSWNSVPLQKWRKAFGVIPQKVFIFSGTFRKN 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  480 IkyslyslkdlealseesnedgfssqsdsnsrnscrakcagdlndmiqttdsteliqvrKNYETIEDSEVVSVSKKVLIH 559
Cdd:cd03289    97 L----------------------------------------------------------DPYGKWSDEEIWKVAEEVGLK 118
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  560 DFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTinnLKGNENRITIIIA-H 638
Cdd:cd03289   119 SVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKT---LKQAFADCTVILSeH 195

                  ....*
gi 156095386  639 RLSTI 643
Cdd:cd03289   196 RIEAM 200
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
383-613 1.45e-12

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 71.02  E-value: 1.45e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHYDTRKDVEiykDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIInDSHNLKDVnlKWWRSKI 462
Cdd:PRK11607   20 LEIRNLTKSFDGQHAVD---DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIML-DGVDLSHV--PPYQRPI 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  463 GVVSQDPLLFSN-SIKNNIKYSLyslkdlealseesNEDGFSsqsdsnsrnscRAKCAGDLNDMIQttdsteliqvrkny 541
Cdd:PRK11607   94 NMMFQSYALFPHmTVEQNIAFGL-------------KQDKLP-----------KAEIASRVNEMLG-------------- 135
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156095386  542 etiedsevvsvskkvLIH--DFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNK 613
Cdd:PRK11607  136 ---------------LVHmqEFAKRKP-----------HQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKK 183
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
383-636 1.90e-12

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 69.10  E-value: 1.90e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHYDtrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYD-----PTEGDV-IINDSHNLKDVNLK 456
Cdd:PRK14267    5 IETVNLRVYYG---SNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVrLFGRNIYSPDVDPI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  457 WWRSKIGVVSQDPLLFSN-SIKNNIKYSLyslkdlealseesnedgfssqsdsnsrnscrakcagDLNDMIQTTDstELi 535
Cdd:PRK14267   82 EVRREVGMVFQYPNPFPHlTIYDNVAIGV------------------------------------KLNGLVKSKK--EL- 122
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  536 qvrknyetieDSEVVSVSKKvlihdfvSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSE 615
Cdd:PRK14267  123 ----------DERVEWALKK-------AALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGT 185
                         250       260
                  ....*....|....*....|.
gi 156095386  616 YLVQKTINNLKgneNRITIII 636
Cdd:PRK14267  186 AKIEELLFELK---KEYTIVL 203
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
397-654 2.13e-12

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: 68.13  E-value: 2.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  397 DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDSHNLKDVNLKWW---RSKIGVVSQDPLLFS 473
Cdd:cd03290    13 GLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRsrnRYSVAYAAQKPWLLN 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  474 NSIKNNIKYslyslkdlealseesnEDGFSSQSDSNSRNSCRAKCAGDLndmiqttdsteliqvrknyetiedsevvsvs 553
Cdd:cd03290    93 ATVEENITF----------------GSPFNKQRYKAVTDACSLQPDIDL------------------------------- 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  554 kkvlihdfvsaLPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD-NKSEYLVQKTINNLKGNENRI 632
Cdd:cd03290   126 -----------LPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDiHLSDHLMQEGILKFLQDDKRT 194
                         250       260
                  ....*....|....*....|..
gi 156095386  633 TIIIAHRLSTIRYANTIFVLSN 654
Cdd:cd03290   195 LVLVTHKLQYLPHADWIIAMKD 216
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
1308-1430 2.42e-12

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 70.44  E-value: 2.42e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1308 MSIYENIKFG------KENATREDVKRACKFAAIDEFIESLPnqydtnvgpygKSLSGGQKQRIAIARALLREPKILLLD 1381
Cdd:PRK11000   90 LSVAENMSFGlklagaKKEEINQRVNQVAEVLQLAHLLDRKP-----------KALSGGQRQRVAIGRTLVAEPSVFLLD 158
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 156095386 1382 EATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH-RIASIKRSDKIVVFN 1430
Cdd:PRK11000  159 EPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHdQVEAMTLADKIVVLD 208
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
1358-1432 2.85e-12

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: 67.84  E-value: 2.85e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156095386 1358 SGGQKQRIAIARALLREPKILLLDEATSSLDS-NSEKLIEKtIVDIKDkADKTIITIAHRIASIKR-SDKIVVFNNP 1432
Cdd:COG4778   154 SGGEQQRVNIARGFIADPPLLLLDEPTASLDAaNRAVVVEL-IEEAKA-RGTAIIGIFHDEEVREAvADRVVDVTPF 228
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
1176-1415 3.08e-12

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


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 71.23  E-value: 3.08e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1176 RPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMrFYDLKNdhhivfkneqtgesskeqmqqgdeeqnvgmknane 1255
Cdd:TIGR00955   35 RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKG----------------------------------- 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1256 fssskegadgqsstlFKNSGKILLDGVDIcdyNLKDLRNLFSIVSQEPMLF-NMSIYENIKFGKENATREDVKRACKFAA 1334
Cdd:TIGR00955   79 ---------------VKGSGSVLLNGMPI---DAKEMRAISAYVQQDDLFIpTLTVREHLMFQAHLRMPRRVTKKEKRER 140
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1335 IDEFIE--SLPNQYDTNVGPYG--KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTI 1410
Cdd:TIGR00955  141 VDEVLQalGLRKCANTRIGVPGrvKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKG-KTI 219

                   ....*
gi 156095386  1411 ITIAH 1415
Cdd:TIGR00955  220 ICTIH 224
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
383-638 3.20e-12

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: 70.99  E-value: 3.20e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   383 IQFKNVRFHYDtrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERL--YDPTEGDVIINDSHNLKdvnlkwwRS 460
Cdd:TIGR03269    1 IEVKNLTKKFD---GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHVALCEK-------CG 70
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   461 KIGVVSQdpllfsnsIKNNIKYSLYSLKDLEAlseesnedGFSSQSDSNSRNsCRAKCAgdlnDMIQTT-----DSTELI 535
Cdd:TIGR03269   71 YVERPSK--------VGEPCPVCGGTLEPEEV--------DFWNLSDKLRRR-IRKRIA----IMLQRTfalygDDTVLD 129
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   536 QVRKNYETIEDSEVVSVSKKVLIHDFVsalpdKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSE 615
Cdd:TIGR03269  130 NVLEALEEIGYEGKEAVGRAVDLIEMV-----QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTA 204
                          250       260
                   ....*....|....*....|...
gi 156095386   616 YLVQKTINNLKGNENRITIIIAH 638
Cdd:TIGR03269  205 KLVHNALEEAVKASGISMVLTSH 227
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
1274-1428 5.25e-12

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 69.96  E-value: 5.25e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1274 SGKILLDGVDICDYNLKDL-RNLFSIVSQEPMLF-NMSIYENIKFGKE--NATREDvkrackFAAIDEFIESLPNQYDTN 1349
Cdd:PRK13549   61 EGEIIFEGEELQASNIRDTeRAGIAIIHQELALVkELSVLENIFLGNEitPGGIMD------YDAMYLRAQKLLAQLKLD 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1350 VGPYGK--SLSGGQKQRIAIARALLREPKILLLDEATSSLdSNSEKLIEKTIV-DIKDKaDKTIITIAHRIASIKR-SDK 1425
Cdd:PRK13549  135 INPATPvgNLGLGQQQLVEIAKALNKQARLLILDEPTASL-TESETAVLLDIIrDLKAH-GIACIYISHKLNEVKAiSDT 212

                  ...
gi 156095386 1426 IVV 1428
Cdd:PRK13549  213 ICV 215
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
1308-1431 8.01e-12

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: 66.72  E-value: 8.01e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1308 MSIYENIKFGKeNATREDVKRACKFAAIDEFIESLPNQYDTNVGPygKSLSGGQKQRIAIARALLREPKILLLDEATSSL 1387
Cdd:TIGR01184   69 LTVRENIALAV-DRVLPDLSKSERRAIVEEHIALVGLTEAADKRP--GQLSGGMKQRVAIARALSIRPKVLLLDEPFGAL 145
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 156095386  1388 DSNSEKLIEKTIVDIKDKADKTIITIAHRI-ASIKRSDKIVVFNN 1431
Cdd:TIGR01184  146 DALTRGNLQEELMQIWEEHRVTVLMVTHDVdEALLLSDRVVMLTN 190
cbiO PRK13645
energy-coupling factor transporter ATPase;
1184-1430 8.95e-12

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 67.73  E-value: 8.95e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1184 DLTFSceSKKTTAIVGETGSGKSTVMSLLMRFYDLKNDHHIVfkneqtgesskeqmqqGDEEQNVGMKNANEfssskega 1263
Cdd:PRK13645   31 SLTFK--KNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIV----------------GDYAIPANLKKIKE-------- 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1264 dgqsstlfknsgkilldgvdicdynLKDLRNLFSIVSQEP--MLFNMSIYENIKFGKEN--ATREDVkrackFAAIDEFI 1339
Cdd:PRK13645   85 -------------------------VKRLRKEIGLVFQFPeyQLFQETIEKDIAFGPVNlgENKQEA-----YKKVPELL 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1340 E--SLPNQYdTNVGPYgkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRI 1417
Cdd:PRK13645  135 KlvQLPEDY-VKRSPF--ELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNM 211
                         250
                  ....*....|....
gi 156095386 1418 ASIKR-SDKIVVFN 1430
Cdd:PRK13645  212 DQVLRiADEVIVMH 225
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
1187-1388 1.02e-11

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 68.07  E-value: 1.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1187 FSCESKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfkneqtgesskeqmqqgdeeqnvgmknanefssskegadgq 1266
Cdd:PRK11308   36 FTLERGKTLAVVGESGCGKSTLARLL------------------------------------------------------ 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1267 ssTLFKN--SGKILLDGVDICDYN---LKDLRNLFSIVSQ-----------------EPMLFNMSIyenikfgkenaTRE 1324
Cdd:PRK11308   62 --TMIETptGGELYYQGQDLLKADpeaQKLLRQKIQIVFQnpygslnprkkvgqileEPLLINTSL-----------SAA 128
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156095386 1325 DvkRACKFAAIDEFIESLPNQYDTnvgpYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLD 1388
Cdd:PRK11308  129 E--RREKALAMMAKVGLRPEHYDR----YPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALD 186
PLN03130 PLN03130
ABC transporter C family member; Provisional
1292-1450 1.10e-11

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 70.15  E-value: 1.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1292 LRNLFSIVSQEPMLFNMSIYENIKFGKE-NATRedVKRACKFAAIDEFIESLPNQYDTNVGPYGKSLSGGQKQRIAIARA 1370
Cdd:PLN03130  677 IRGTVAYVPQVSWIFNATVRDNILFGSPfDPER--YERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARA 754
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1371 LLREPKILLLDEATSSLDSN-SEKLIEKTIVDikDKADKTIITIAHRIASIKRSDKIVVFNNpdrtgSFVQAQGTHEELL 1449
Cdd:PLN03130  755 VYSNSDVYIFDDPLSALDAHvGRQVFDKCIKD--ELRGKTRVLVTNQLHFLSQVDRIILVHE-----GMIKEEGTYEELS 827

                  .
gi 156095386 1450 S 1450
Cdd:PLN03130  828 N 828
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
1179-1450 1.13e-11

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: 69.33  E-value: 1.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1179 VPIYKDLTFSCESKKTTAIVGETGSGKS----TVMSLLmrfydlkndhhivfkneqtgesskeqmqqgdeeqnvgmknan 1254
Cdd:COG4172    23 VEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLL------------------------------------------ 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1255 efssskegADGQSSTlfknSGKILLDGVDICDYNLKDLRNL----FSIVSQEPM-----LFNMS--IYENIKFgKENATR 1323
Cdd:COG4172    61 --------PDPAAHP----SGSILFDGQDLLGLSERELRRIrgnrIAMIFQEPMtslnpLHTIGkqIAEVLRL-HRGLSG 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1324 EDVKRAckfaAID----------EF-IESLPNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSE 1392
Cdd:COG4172   128 AAARAR----ALEllervgipdpERrLDAYPHQ-----------LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQ 192
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 156095386 1393 KLIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVVFnnpdRTGSFVQaQGTHEELLS 1450
Cdd:COG4172   193 AQILDLLKDLQRELGMALLLITHDLGVVRRfADRVAVM----RQGEIVE-QGPTAELFA 246
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
382-613 1.89e-11

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


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 67.56  E-value: 1.89e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  382 KIQFKNVRFHYDTrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDshnlKDVN-LKWWRS 460
Cdd:PRK11650    3 GLKLQAVRKSYDG--KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGG----RVVNeLEPADR 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  461 KIGVVSQDPLLFSN-SIKNNIKYSLyslkdlealseesnedgfssqsdsnsrnscraKCAGdlndmiqtTDSTElIQVRk 539
Cdd:PRK11650   77 DIAMVFQNYALYPHmSVRENMAYGL--------------------------------KIRG--------MPKAE-IEER- 114
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156095386  540 nyetiedseVVSVSKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNK 613
Cdd:PRK11650  115 ---------VAEAARILELEPLLDRKP-----------RELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAK 168
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
376-669 2.28e-11

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


Pssm-ID: 440718 [Multi-domain]  Cd Length: 264  Bit Score: 65.88  E-value: 2.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  376 KLKDIKKIqfknvrFHYDTRKDVEIYKDLNFTLTEGKtyaFV---GESGCGKSTILKLIERLYDPTEGDVIINDshnlKD 452
Cdd:COG1101     3 ELKNLSKT------FNPGTVNEKRALDGLNLTIEEGD---FVtviGSNGAGKSTLLNAIAGSLPPDSGSILIDG----KD 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  453 V-NLK-WWRSK-IGVVSQDPLL---FSNSIKNNIkySLYSLKdlealseeSNEDGFSSQSDSNSRNSCRAKCAG-DLNdm 525
Cdd:COG1101    70 VtKLPeYKRAKyIGRVFQDPMMgtaPSMTIEENL--ALAYRR--------GKRRGLRRGLTKKRRELFRELLATlGLG-- 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  526 iqttdsteliqvrknyetiedsevvsvskkvlihdfvsaLPDKYETLVGSnaskLSGGQKQRISIARAIIRNPKILILDE 605
Cdd:COG1101   138 ---------------------------------------LENRLDTKVGL----LSGGQRQALSLLMATLTKPKLLLLDE 174
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156095386  606 ATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLS-TIRYANTIFVLsnrENGSTVdVDVLGED 669
Cdd:COG1101   175 HTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEqALDYGNRLIMM---HEGRII-LDVSGEE 235
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
1262-1431 2.31e-11

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: 64.93  E-value: 2.31e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1262 GADGQ-SSTLFK--------NSGKILLDGVDICDyNLKDLRNLFSIVSqEPMLF-NMSIYENIKFgkeNATREDVKRAck 1331
Cdd:cd03268    33 GPNGAgKTTTMKiilglikpDSGEITFDGKSYQK-NIEALRRIGALIE-APGFYpNLTARENLRL---LARLLGIRKK-- 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1332 faAIDEFIE--SLPNQYDTNVGPYgkSLsgGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKT 1409
Cdd:cd03268   106 --RIDEVLDvvGLKDSAKKKVKGF--SL--GMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQG-IT 178
                         170       180
                  ....*....|....*....|...
gi 156095386 1410 IITIAHRIASI-KRSDKIVVFNN 1431
Cdd:cd03268   179 VLISSHLLSEIqKVADRIGIINK 201
ABC_6TM_TAP cd18572
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ...
65-309 2.35e-11

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: 66.41  E-value: 2.35e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   65 SFVCATISGGT---LPFFVS--VFGVIMKNMnlGENVNDIIFSLVLIGIFQFILSFISSFCMDVVTTKILKTLKIEFLKS 139
Cdd:cd18572     1 AFVFLVVAALSelaIPHYTGavIDAVVADGS--REAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  140 VFYQDGQFHD-NNPG---SKLTSDLDfyleQVNAGIGTKFITIFTYASAFLGLYIWSLFKNARLTLCITCVFPLIYIcgv 215
Cdd:cd18572    79 LLRQDIAFFDaTKTGeltSRLTSDCQ----KVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIAL--- 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  216 ICNKKVKINKKTSLLYNN---NTMSIIEEALVGIRTVVSYCGENTILKKFNLSEKLYSKYTLKANLMESLHIGMINGFIL 292
Cdd:cd18572   152 ITKVYGRYYRKLSKEIQDalaEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQN 231
                         250
                  ....*....|....*..
gi 156095386  293 ASYAFGFWYGTRIIISD 309
Cdd:cd18572   232 GTQVLVLFYGGHLVLSG 248
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
383-662 2.49e-11

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 65.42  E-value: 2.49e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHYDTRkdvEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIIND-----SHNLKDVNLKW 457
Cdd:PRK11124    3 IQLNGINCFYGAH---QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfSKTPSDKAIRE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  458 WRSKIGVVSQdpllfsnsiknniKYSLYS-LKDLEALSEesnedgfssqsdsnsrnscrAKCagdlndmiqttdsteliQ 536
Cdd:PRK11124   80 LRRNVGMVFQ-------------QYNLWPhLTVQQNLIE--------------------APC-----------------R 109
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  537 VRKNYETIEDSEVVSVSKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEY 616
Cdd:PRK11124  110 VLGLSKDQALARAEKLLERLRLKPYADRFP-----------LHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITA 178
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 156095386  617 LVQKTINNLKgnENRIT-IIIAHRLSTIRYANTIFVLsnRENGSTVD 662
Cdd:PRK11124  179 QIVSIIRELA--ETGITqVIVTHEVEVARKTASRVVY--MENGHIVE 221
ABC_6TM_AtABCB27_like cd18780
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ...
64-355 3.13e-11

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: 66.12  E-value: 3.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   64 VSFVCATISGGTLPFFV-SVFGVIMKNMNLG-----ENVNDIIFSLVLIGIFQFILSFISSFCMDVVTTKILKTLKIEFL 137
Cdd:cd18780     3 IALLVSSGTNLALPYFFgQVIDAVTNHSGSGgeealRALNQAVLILLGVVLIGSIATFLRSWLFTLAGERVVARLRKRLF 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  138 KSVFYQDGQFHD-NNPG---SKLTSDldfylEQV--NAGIGTKFITIFTYASAFLGLYIwsLFK-NARLTLCITCVFPLI 210
Cdd:cd18780    83 SAIIAQEIAFFDvTRTGellNRLSSD-----TQVlqNAVTVNLSMLLRYLVQIIGGLVF--MFTtSWKLTLVMLSVVPPL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  211 YICGVICNKKVKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGENTILKKFnlSEKLYSKYTLKANLmeSLHIGMINGF 290
Cdd:cd18780   156 SIGAVIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRY--SEKINESYLLGKKL--ARASGGFNGF 231
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 156095386  291 ILA----SYAFGFWYGTRIIISDlsnqqpnnDFHGGSVISILLGVLISMFMLTIILPNITEYMKSLEAT 355
Cdd:cd18780   232 MGAaaqlAIVLVLWYGGRLVIDG--------ELTTGLLTSFLLYTLTVAMSFAFLSSLYGDFMQAVGAS 292
cbiO PRK13643
energy-coupling factor transporter ATPase;
383-652 3.34e-11

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 65.91  E-value: 3.34e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHYDTRKDV--EIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIIND---SHNLKDVNLKW 457
Cdd:PRK13643    2 IKFEKVNYTYQPNSPFasRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDivvSSTSKQKEIKP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  458 WRSKIGVVSQDP--LLFSNSIknnikyslysLKDLealseesnedGFSSQSDSNSRNSCRAKCAgdlndmiqttdsteli 535
Cdd:PRK13643   82 VRKKVGVVFQFPesQLFEETV----------LKDV----------AFGPQNFGIPKEKAEKIAA---------------- 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  536 qvrknyetiEDSEVVSVSKkvlihDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSE 615
Cdd:PRK13643  126 ---------EKLEMVGLAD-----EFWEKSP-----------FELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKAR 180
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 156095386  616 YLVQKTINNLKgNENRITIIIAHRLSTIR-YANTIFVL 652
Cdd:PRK13643  181 IEMMQLFESIH-QSGQTVVLVTHLMDDVAdYADYVYLL 217
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
383-654 3.42e-11

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 65.53  E-value: 3.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHYdtRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDSHnLKDVNLKWWRSKI 462
Cdd:PRK13647    5 IEVEDLHFRY--KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGRE-VNAENEKWVRSKV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  463 GVVSQDP--LLFSNSIKNNIKYslyslkdlealseesnedgfssqsdsnsrnscrakcaGDLNdmiQTTDSTELiqvrkn 540
Cdd:PRK13647   82 GLVFQDPddQVFSSTVWDDVAF-------------------------------------GPVN---MGLDKDEV------ 115
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  541 yetieDSEVVSVSKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQK 620
Cdd:PRK13647  116 -----ERRVEEALKAVRMWDFRDKPP-----------YHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLME 179
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 156095386  621 TINNLkgNENRITIIIA-HRLS-TIRYANTIFVLSN 654
Cdd:PRK13647  180 ILDRL--HNQGKTVIVAtHDVDlAAEWADQVIVLKE 213
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
382-611 4.08e-11

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 64.93  E-value: 4.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  382 KIQFKNVRFHYDtrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYD-----PTEGDVIInDSHNLKDVNLK 456
Cdd:PRK14247    3 KIEIRDLKVSFG---QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYL-DGQDIFKMDVI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  457 WWRSKIGVVSQDPLLFSN-SIKNNIKYSLyslkdlealseesnedgfssqsdsnsrnscrakcagDLNDMIQTtdSTELI 535
Cdd:PRK14247   79 ELRRRVQMVFQIPNPIPNlSIFENVALGL------------------------------------KLNRLVKS--KKELQ 120
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156095386  536 Q-VRKNYETIEdsevvsvskkvlihdfvsaLPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:PRK14247  121 ErVRWALEKAQ-------------------LWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLD 178
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
383-625 4.45e-11

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 66.01  E-value: 4.45e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHYdtrKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDSHNLKDVNLKwwRSKI 462
Cdd:PRK13536   42 IDLAGVSKSY---GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLA--RARI 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  463 GVVSQdpllFSNSiknnikyslyslkDLEALSEESnedgfssqsdsnsrnscrakcagdlndmiqttdstelIQVRKNYE 542
Cdd:PRK13536  117 GVVPQ----FDNL-------------DLEFTVREN-------------------------------------LLVFGRYF 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  543 TIEDSEVVSVSKKVLihDFvSALPDKYETLVgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI 622
Cdd:PRK13536  143 GMSTREIEAVIPSLL--EF-ARLESKADARV----SDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERL 215

                  ...
gi 156095386  623 NNL 625
Cdd:PRK13536  216 RSL 218
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
1163-1448 4.50e-11

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 65.88  E-value: 4.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1163 KIEIMDVNFRYLSRpnVPIY----KDLTFSCESKKTTAIVGETGSGKSTV---MSLLMrfydLKNDHHI--VFKNEQTGE 1233
Cdd:PRK13651    2 QIKVKNIVKIFNKK--LPTElkalDNVSVEINQGEFIAIIGQTGSGKTTFiehLNALL----LPDTGTIewIFKDEKNKK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1234 SSKEQMQQGDEeqnvgmknanefssskegaDGQSSTLFKNSGKIlldgvdicdynlKDLRNLFSIVSQ--EPMLFNMSIY 1311
Cdd:PRK13651   76 KTKEKEKVLEK-------------------LVIQKTRFKKIKKI------------KEIRRRVGVVFQfaEYQLFEQTIE 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1312 ENIKFG-------KENATredvKRACKFAAIdefiESLPNQYdTNVGPYGksLSGGQKQRIAIARALLREPKILLLDEAT 1384
Cdd:PRK13651  125 KDIIFGpvsmgvsKEEAK----KRAAKYIEL----VGLDESY-LQRSPFE--LSGGQKRRVALAGILAMEPDFLVFDEPT 193
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156095386 1385 SSLDSNSEKLIEKtIVDIKDKADKTIITIAHRIASI-KRSDKIVVFNNpdrtGSFVQAQGTHEEL 1448
Cdd:PRK13651  194 AGLDPQGVKEILE-IFDNLNKQGKTIILVTHDLDNVlEWTKRTIFFKD----GKIIKDGDTYDIL 253
ABC_6TM_Tm288_like cd18547
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ...
62-291 4.91e-11

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: 65.50  E-value: 4.91e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   62 LGVSFVCATISGGT---LPFFVS-VFGVIMKNMNLGENVN-----DIIFSLVLIGIFQFILSFISSFCMDVVTTKILKTL 132
Cdd:cd18547     1 LILVIILAIISTLLsvlGPYLLGkAIDLIIEGLGGGGGVDfsgllRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  133 ------KIEFLkSVFYqdgqFHDNNPG---SKLTSDLDfyleQVNAGIGTKFITIFTYASAFLGLYIWSLFKNARLTLCI 203
Cdd:cd18547    81 rkdlfeKLQRL-PLSY----FDTHSHGdimSRVTNDVD----NISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIV 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  204 TCVFPLIYICGVIcnkkvkINKKTSLLYNNNTMSI------IEEALVGIRTVVSYCGENTILKKFN-LSEKLYsKYTLKA 276
Cdd:cd18547   152 LVTVPLSLLVTKF------IAKRSQKYFRKQQKALgelngyIEEMISGQKVVKAFNREEEAIEEFDeINEELY-KASFKA 224
                         250
                  ....*....|....*
gi 156095386  277 NLMESLhIGMINGFI 291
Cdd:cd18547   225 QFYSGL-LMPIMNFI 238
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
1179-1396 5.24e-11

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: 64.38  E-value: 5.24e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1179 VPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfkneqtgesskeqmqqgdeeqnvgmknAnefss 1258
Cdd:COG4181    25 LTILKGISLEVEAGESVAIVGASGSGKSTLLGLL----------------------------------------A----- 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1259 skeGADGQSStlfknsGKILLDGVDICDYN---LKDLRN-LFSIVSQEPMLF-NMSIYENIK-----FGKENAtREDVKR 1328
Cdd:COG4181    60 ---GLDRPTS------GTVRLAGQDLFALDedaRARLRArHVGFVFQSFQLLpTLTALENVMlplelAGRRDA-RARARA 129
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 156095386 1329 ACKFAAIDEFIESLPNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDS-NSEKLIE 1396
Cdd:COG4181   130 LLERVGLGHRLDHYPAQ-----------LSGGEQQRVALARAFATEPAILFADEPTGNLDAaTGEQIID 187
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
1350-1446 5.95e-11

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: 62.97  E-value: 5.95e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1350 VGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVV 1428
Cdd:cd03222    65 YKPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYlSDRIHV 144
                          90
                  ....*....|....*....
gi 156095386 1429 F-NNPDRTGSFVQAQGTHE 1446
Cdd:cd03222   145 FeGEPGVYGIASQPKGTRE 163
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
402-652 6.06e-11

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 66.59  E-value: 6.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  402 KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDshnlKDVNLkwwRS-------KIGVVSQDPLLFSN 474
Cdd:COG3845    22 DDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDG----KPVRI---RSprdaialGIGMVHQHFMLVPN 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  475 -SIKNNIkyslyslkdleALSEESNEDGFSSqsdsnsRNSCRAKcagdlndmiqttdsteliqvrknyetiedsevvsvs 553
Cdd:COG3845    95 lTVAENI-----------VLGLEPTKGGRLD------RKAARAR------------------------------------ 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  554 kkvlihdfVSALPDKY------ETLVGSnaskLSGGQKQRISIARAIIRNPKILILDEATSSL-DNKSEYLVqKTINNLK 626
Cdd:COG3845   122 --------IRELSERYgldvdpDAKVED----LSVGEQQRVEILKALYRGARILILDEPTAVLtPQEADELF-EILRRLA 188
                         250       260
                  ....*....|....*....|....*...
gi 156095386  627 gnENRITII-IAHRLSTIR-YANTIFVL 652
Cdd:COG3845   189 --AEGKSIIfITHKLREVMaIADRVTVL 214
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
1268-1450 6.48e-11

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: 63.85  E-value: 6.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1268 STLFK--------NSGKILLDGVDIcdynlkdlRNL---------FSIVSQEPMLF-NMSIYENIKFG-----KENATRE 1324
Cdd:COG0410    43 TTLLKaisgllppRSGSIRFDGEDI--------TGLpphriarlgIGYVPEGRRIFpSLTVEENLLLGayarrDRAEVRA 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1325 DVKRACK-FAAIDEFIESLpnqydtnvgpyGKSLSGGQKQRIAIARALLREPKILLLDEATSSLdsnSEKLIEK---TIV 1400
Cdd:COG0410   115 DLERVYElFPRLKERRRQR-----------AGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGL---APLIVEEifeIIR 180
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 156095386 1401 DIKDkADKTIITI---AHRIASIkrSDKIVVFnnpdRTGSFVqAQGTHEELLS 1450
Cdd:COG0410   181 RLNR-EGVTILLVeqnARFALEI--ADRAYVL----ERGRIV-LEGTAAELLA 225
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
398-652 6.49e-11

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 66.61  E-value: 6.49e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  398 VEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDSHNLKDVNLKWWRSKIGVVSQDPLLFSN-SI 476
Cdd:PRK15439   24 VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGIYLVPQEPLLFPNlSV 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  477 KNNIKYSLyslkdlealseesnedgfssqsdsnsrnscrAKCAGDLNDMiqttdsTELIQvrknyetiedseVVSVSKKv 556
Cdd:PRK15439  104 KENILFGL-------------------------------PKRQASMQKM------KQLLA------------ALGCQLD- 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  557 lihdfvsalPDkyetlvgSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD-NKSEYLVQKtINNLKGNENRItII 635
Cdd:PRK15439  134 ---------LD-------SSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTpAETERLFSR-IRELLAQGVGI-VF 195
                         250
                  ....*....|....*...
gi 156095386  636 IAHRLSTIR-YANTIFVL 652
Cdd:PRK15439  196 ISHKLPEIRqLADRISVM 213
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
383-653 7.23e-11

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 64.87  E-value: 7.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHYDtrKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIIN----DSHNLKDVNLkww 458
Cdd:PRK13636    6 LKVEELNYNYS--DGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDgkpiDYSRKGLMKL--- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  459 RSKIGVVSQDP--LLFSNSIKNNIKYSLYSLKdleaLSEEsnedgfssqsdsnsrnscrakcagdlndmiqttdsteliQ 536
Cdd:PRK13636   81 RESVGMVFQDPdnQLFSASVYQDVSFGAVNLK----LPED---------------------------------------E 117
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  537 VRKNYETIedsevvsvskkvLIHDFVSALPDKyetlvgsNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEY 616
Cdd:PRK13636  118 VRKRVDNA------------LKRTGIEHLKDK-------PTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVS 178
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 156095386  617 LVQKTINNLKgNENRITIIIA-HRLSTIR-YANTIFVLS 653
Cdd:PRK13636  179 EIMKLLVEMQ-KELGLTIIIAtHDIDIVPlYCDNVFVMK 216
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
383-656 7.95e-11

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: 61.70  E-value: 7.95e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHYDTRKdveIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDshnlkdvnlkwwRSKI 462
Cdd:cd03221     1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS------------TVKI 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  463 GVVSQdpllfsnsiknnikyslyslkdlealseesnedgfssqsdsnsrnscrakcagdlndmiqttdsteliqvrknye 542
Cdd:cd03221    66 GYFEQ--------------------------------------------------------------------------- 70
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  543 tiedsevvsvskkvlihdfvsalpdkyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI 622
Cdd:cd03221    71 -------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEAL 113
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 156095386  623 NNLKGnenrITIIIAH-R--LSTIryANTIFVLSNRE 656
Cdd:cd03221   114 KEYPG----TVILVSHdRyfLDQV--ATKIIELEDGK 144
SufC COG0396
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ...
1178-1431 8.28e-11

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


Pssm-ID: 440165 [Multi-domain]  Cd Length: 245  Bit Score: 63.93  E-value: 8.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1178 NVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMrfydlkndhhivfkneqtgesskeqmqqGDEEQNVgmknanefs 1257
Cdd:COG0396    12 GKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLM----------------------------GHPKYEV--------- 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1258 sskegadgqsstlfkNSGKILLDGVDICDYNLKD--LRNLFsiVS-QEP--------MLFNMSIYeNIKFGKENATREDV 1326
Cdd:COG0396    55 ---------------TSGSILLDGEDILELSPDEraRAGIF--LAfQYPveipgvsvSNFLRTAL-NARRGEELSAREFL 116
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1327 KRACKFAAI----DEFIESlpnqyDTNVGpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDI 1402
Cdd:COG0396   117 KLLKEKMKElgldEDFLDR-----YVNEG-----FSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKL 186
                         250       260       270
                  ....*....|....*....|....*....|.
gi 156095386 1403 KDKaDKTIITIAH--RIASIKRSDKIVVFNN 1431
Cdd:COG0396   187 RSP-DRGILIITHyqRILDYIKPDFVHVLVD 216
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
1308-1388 9.54e-11

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


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 65.25  E-value: 9.54e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1308 MSIYENIKFGKENA------TREDVKRACKFAAIDEFIESLPNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLD 1381
Cdd:PRK11650   91 MSVRENMAYGLKIRgmpkaeIEERVAEAARILELEPLLDRKPRE-----------LSGGQRQRVAMGRAIVREPAVFLFD 159

                  ....*..
gi 156095386 1382 EATSSLD 1388
Cdd:PRK11650  160 EPLSNLD 166
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
1171-1460 9.65e-11

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 64.04  E-value: 9.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1171 FRY----LSRPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfkneqtgesskeqmqqgdeeq 1246
Cdd:PRK15112   14 FRYrtgwFRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKML---------------------------------- 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1247 nvgmknanefssskegadgqSSTLFKNSGKILLDGVDIC--DYNLKDLRnlFSIVSQEPmlfNMSIYENIKFG------- 1317
Cdd:PRK15112   60 --------------------AGMIEPTSGELLIDDHPLHfgDYSYRSQR--IRMIFQDP---STSLNPRQRISqildfpl 114
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1318 KENATREDVKRACKFAAIDEFIESLPNqydtNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEK 1397
Cdd:PRK15112  115 RLNTDLEPEQREKQIIETLRQVGLLPD----HASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLIN 190
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156095386 1398 TIVDIKDKADKTIITIAHRIASIKR-SDKIVVFNNpdrtGSFVQAQGTHEELLSVQDGVYKKYV 1460
Cdd:PRK15112  191 LMLELQEKQGISYIYVTQHLGMMKHiSDQVLVMHQ----GEVVERGSTADVLASPLHELTKRLI 250
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
1273-1382 9.87e-11

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


Pssm-ID: 440752 [Multi-domain]  Cd Length: 240  Bit Score: 63.51  E-value: 9.87e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1273 NSGKILLDGVDICDYNLkDLRNLFSI--VSQEPMLF-NMSIYENIK-----FGKENATREDvkracKFAA-IDEF-IESL 1342
Cdd:COG1137    56 DSGRIFLDGEDITHLPM-HKRARLGIgyLPQEASIFrKLTVEDNILavlelRKLSKKEREE-----RLEElLEEFgITHL 129
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 156095386 1343 PNQYdtnvgpyGKSLSGGQKQRIAIARALLREPKILLLDE 1382
Cdd:COG1137   130 RKSK-------AYSLSGGERRRVEIARALATNPKFILLDE 162
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
1356-1427 1.17e-10

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 63.88  E-value: 1.17e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 156095386 1356 SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRI-ASIKRSDKIV 1427
Cdd:PRK09984  152 TLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVdYALRYCERIV 224
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
1268-1448 1.35e-10

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: 62.77  E-value: 1.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1268 STLFK-NSGKILLDGVDI-CDynLKDLRNLFSIVSQEPMLFN-MSIYENIKFgkeNATREDVKRACKFAAIDEFIE--SL 1342
Cdd:cd03265    47 TTLLKpTSGRATVAGHDVvRE--PREVRRRIGIVFQDLSVDDeLTGWENLYI---HARLYGVPGAERRERIDELLDfvGL 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1343 PNQYDTNVGPYgkslSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASI-K 1421
Cdd:cd03265   122 LEAADRLVKTY----SGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAeQ 197
                         170       180
                  ....*....|....*....|....*..
gi 156095386 1422 RSDKIVVFNNpdrtGSFVqAQGTHEEL 1448
Cdd:cd03265   198 LCDRVAIIDH----GRII-AEGTPEEL 219
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
396-611 1.37e-10

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 66.03  E-value: 1.37e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  396 KDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDSH--NLKDVNLKWWRSKIGVVSQDPLLfS 473
Cdd:PRK10261  335 REVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRidTLSPGKLQALRRDIQFIFQDPYA-S 413
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  474 NSIKNNIKYSLyslkdLEALSEESNEDGFSSQSdsnsrnscrakcagdlndmiqttdsteliqvrknyetiedsEVVSVS 553
Cdd:PRK10261  414 LDPRQTVGDSI-----MEPLRVHGLLPGKAAAA-----------------------------------------RVAWLL 447
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 156095386  554 KKV-LIHDFVSALPDKYetlvgsnasklSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:PRK10261  448 ERVgLLPEHAWRYPHEF-----------SGGQRQRICIARALALNPKVIIADEAVSALD 495
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
1163-1450 1.40e-10

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 63.45  E-value: 1.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1163 KIEIMDVNFRYLSRPnvpIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLmRFYDLKNDHHIVFKNeqtgesskeqmqqg 1242
Cdd:PRK10619    5 KLNVIDLHKRYGEHE---VLKGVSLQANAGDVISIIGSSGSGKSTFLRCI-NFLEKPSEGSIVVNG-------------- 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1243 deeQNVGMKNANefssskegaDGQSSTLFKNsgkilldgvdicdyNLKDLRNLFSIVSQEPMLFN-MSIYENIK------ 1315
Cdd:PRK10619   67 ---QTINLVRDK---------DGQLKVADKN--------------QLRLLRTRLTMVFQHFNLWShMTVLENVMeapiqv 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1316 --FGKENAtREDVKRACKFAAIDEFIEslpnqydtnvGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSnseK 1393
Cdd:PRK10619  121 lgLSKQEA-RERAVKYLAKVGIDERAQ----------GKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDP---E 186
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 156095386 1394 LIEKTIVDIKDKAD--KTIITIAHRIASIKRSDKIVVFNNPDRtgsfVQAQGTHEELLS 1450
Cdd:PRK10619  187 LVGEVLRIMQQLAEegKTMVVVTHEMGFARHVSSHVIFLHQGK----IEEEGAPEQLFG 241
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
386-610 1.46e-10

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: 62.84  E-value: 1.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  386 KNVRFHYDtrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDshnlKDV-NLKWW---RSK 461
Cdd:cd03224     4 ENLNAGYG---KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDG----RDItGLPPHeraRAG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  462 IGVVSQDPLLFSN-SIKNNIKYSLYSLKDlealseesnedgfssqsdsnsrnscrakcagdlndmiqttdsteliqvRKN 540
Cdd:cd03224    77 IGYVPEGRRIFPElTVEENLLLGAYARRR------------------------------------------------AKR 108
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  541 YETIEDsevvsvskkvlIHDFVSALPDKYETLVGSnaskLSGGQKQRISIARAIIRNPKILILDEATSSL 610
Cdd:cd03224   109 KARLER-----------VYELFPRLKERRKQLAGT----LSGGEQQMLAIARALMSRPKLLLLDEPSEGL 163
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
402-652 1.46e-10

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: 62.84  E-value: 1.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  402 KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIIN--DSHNLKDVNlkwwRSKIGVVS--QDPLLFSN-SI 476
Cdd:cd03219    17 DDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDgeDITGLPPHE----IARLGIGRtfQIPRLFPElTV 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  477 KNNIKYSLYSlkdlealseeSNEDGFSSQSDSNSRNSCRAKCAgdlndmiqttdstELIqvrknyetiedsevvsvskkv 556
Cdd:cd03219    93 LENVMVAAQA----------RTGSGLLLARARREEREARERAE-------------ELL--------------------- 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  557 lihDFVsALPDKYETLVGSnaskLSGGQKQRISIARAIIRNPKILILDEATSSLdNKSEylVQKTINNLKG-NENRITI- 634
Cdd:cd03219   129 ---ERV-GLADLADRPAGE----LSYGQQRRLEIARALATDPKLLLLDEPAAGL-NPEE--TEELAELIRElRERGITVl 197
                         250
                  ....*....|....*....
gi 156095386  635 IIAHRLSTI-RYANTIFVL 652
Cdd:cd03219   198 LVEHDMDVVmSLADRVTVL 216
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
1299-1388 1.47e-10

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 64.51  E-value: 1.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1299 VSQEPMLF-NMSIYENIKFGKENATREdvkracKFAAIDEF--IESLPNQYdtnvgPYgkSLSGGQKQRIAIARALLREP 1375
Cdd:PRK11144   81 VFQDARLFpHYKVRGNLRYGMAKSMVA------QFDKIVALlgIEPLLDRY-----PG--SLSGGEKQRVAIGRALLTAP 147
                          90
                  ....*....|...
gi 156095386 1376 KILLLDEATSSLD 1388
Cdd:PRK11144  148 ELLLMDEPLASLD 160
PTZ00243 PTZ00243
ABC transporter; Provisional
1163-1428 1.60e-10

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 66.34  E-value: 1.60e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1163 KIEIMDVNFRYLSRPNVpIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfkneQTGESSKEQMqqg 1242
Cdd:PTZ00243  658 KTPKMKTDDFFELEPKV-LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEI-----------SEGRVWAERS--- 722
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1243 deeqnvgmknanefssskegadgqsstlfknsgkilldgvdicdynlkdlrnlFSIVSQEPMLFNMSIYENIKF-GKENA 1321
Cdd:PTZ00243  723 -----------------------------------------------------IAYVPQQAWIMNATVRGNILFfDEEDA 749
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1322 TR-EDVKRACKFAAiDefIESLPNQYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSN-SEKLIEKTI 1399
Cdd:PTZ00243  750 ARlADAVRVSQLEA-D--LAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHvGERVVEECF 826
                         250       260
                  ....*....|....*....|....*....
gi 156095386 1400 vdIKDKADKTIITIAHRIASIKRSDKIVV 1428
Cdd:PTZ00243  827 --LGALAGKTRVLATHQVHVVPRADYVVA 853
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
1356-1429 1.71e-10

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 61.87  E-value: 1.71e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156095386 1356 SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkADKTIITIAHRIASIKRSDKIVVF 1429
Cdd:NF040873  119 ELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHA-RGATVVVVTHDLELVRRADPCVLL 191
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
1274-1428 1.84e-10

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 63.96  E-value: 1.84e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1274 SGKILLDGVDI---CDYNLKDLRNLFSIVSQEP-------MLFNMSIYENIKFGKENATREDVKRACKfaAIDEFIESLP 1343
Cdd:PRK15079   75 DGEVAWLGKDLlgmKDDEWRAVRSDIQMIFQDPlaslnprMTIGEIIAEPLRTYHPKLSRQEVKDRVK--AMMLKVGLLP 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1344 NQydtnVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNseklIEKTIVDIKDKADK----TIITIAHRIAS 1419
Cdd:PRK15079  153 NL----INRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVS----IQAQVVNLLQQLQRemglSLIFIAHDLAV 224
                         170
                  ....*....|
gi 156095386 1420 IKR-SDKIVV 1428
Cdd:PRK15079  225 VKHiSDRVLV 234
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
383-636 2.22e-10

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: 62.00  E-value: 2.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHYDtrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDSHNLKDVnlKWWRSKI 462
Cdd:cd03265     1 IEVENLVKKYG---DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREP--REVRRRI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  463 GVVSQDPLL------FSNSIknnIKYSLYSLKDLEAlseesnedgfssqsdsnsrnscRAKCAgdlndmiQTTDSTELIQ 536
Cdd:cd03265    76 GIVFQDLSVddeltgWENLY---IHARLYGVPGAER----------------------RERID-------ELLDFVGLLE 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  537 VRknyetiedsevvsvskkvlihdfvsalpDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEY 616
Cdd:cd03265   124 AA----------------------------DRL-------VKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRA 168
                         250       260
                  ....*....|....*....|
gi 156095386  617 LVQKTINNLKgNENRITIII 636
Cdd:cd03265   169 HVWEYIEKLK-EEFGMTILL 187
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
1269-1450 2.45e-10

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 64.48  E-value: 2.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1269 TLFKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPML-FNMSIYENIKFGK----------ENATREDVKRACKFAAIDE 1337
Cdd:PRK09536   52 TLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFEFDVRQVVEMGRtphrsrfdtwTETDRAAVERAMERTGVAQ 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1338 FIeslpnqyDTNVgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKlieKTIVDIKDKAD--KTIITIAH 1415
Cdd:PRK09536  132 FA-------DRPV----TSLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQV---RTLELVRRLVDdgKTAVAAIH 197
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 156095386 1416 RIASIKR-SDKIVVFnnpdrTGSFVQAQGTHEELLS 1450
Cdd:PRK09536  198 DLDLAARyCDELVLL-----ADGRVRAAGPPADVLT 228
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
383-661 2.51e-10

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: 61.74  E-value: 2.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHYDtrkdvEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIIND-SHNLKDVNlkwwRSK 461
Cdd:cd03298     1 VRLDKIRFSYG-----EQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGvDVTAAPPA----DRP 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  462 IGVVSQDPLLFSN-SIKNNIKYSLY-SLKdleaLSEESNEdgfssqsdsnsrnscrakcagdlndmiqttdsteliqvrk 539
Cdd:cd03298    72 VSMLFQENNLFAHlTVEQNVGLGLSpGLK----LTAEDRQ---------------------------------------- 107
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  540 nyetiedsEVVSVSKKVLIHDFVSALPDKyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQ 619
Cdd:cd03298   108 --------AIEVALARVGLAGLEKRLPGE-----------LSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEML 168
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 156095386  620 KTINNLKGNENRITIIIAHRLSTIR--YANTIFVlsnrENGSTV 661
Cdd:cd03298   169 DLVLDLHAETKMTVLMVTHQPEDAKrlAQRVVFL----DNGRIA 208
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
345-638 2.93e-10

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: 64.44  E-value: 2.93e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   345 ITEYMKSLEATNNLYEIINRKPLVennqdgkKLKDIKKiqfknvRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGK 424
Cdd:TIGR03269  257 VAVFMEGVSEVEKECEVEVGEPII-------KVRNVSK------RYISVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGK 323
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   425 STILKLIERLYDPTEGDVIINDSHNLKDVNLKWW----RSK--IGVVSQDpllfsnsiknnikYSLYSLKD-LEALsees 497
Cdd:TIGR03269  324 TTLSKIIAGVLEPTSGEVNVRVGDEWVDMTKPGPdgrgRAKryIGILHQE-------------YDLYPHRTvLDNL---- 386
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   498 nedgfssqsdsnsrnscrakcagdlndmiqttdsTELIqvrknyeTIEDSEVVSVSKKVLIHDFVSALPDKYETLVGSNA 577
Cdd:TIGR03269  387 ----------------------------------TEAI-------GLELPDELARMKAVITLKMVGFDEEKAEEILDKYP 425
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 156095386   578 SKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAH 638
Cdd:TIGR03269  426 DELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSH 486
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
1139-1428 2.98e-10

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 63.59  E-value: 2.98e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1139 TRKSLIDVRDnggikiknsndikgkieiMDVNFrylSRP--NVPIYKDLTFSCESKKTTAIVGETGSGKS----TVMSLL 1212
Cdd:PRK09473    8 QADALLDVKD------------------LRVTF---STPdgDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLL 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1213 MrfydlkndhhivfKNEQTGESSKeqmQQGDEEQNVGMKNANEFSSSKegadgqsstlfknsgkilldgvdicdynlkdl 1292
Cdd:PRK09473   67 A-------------ANGRIGGSAT---FNGREILNLPEKELNKLRAEQ-------------------------------- 98
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1293 rnlFSIVSQEPML-FN--MSIYENI--------KFGKENATREDVKR--ACKFAAIDEFIESLPNQYdtnvgpygkslSG 1359
Cdd:PRK09473   99 ---ISMIFQDPMTsLNpyMRVGEQLmevlmlhkGMSKAEAFEESVRMldAVKMPEARKRMKMYPHEF-----------SG 164
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 156095386 1360 GQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHR---IASIkrSDKIVV 1428
Cdd:PRK09473  165 GMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDlgvVAGI--CDKVLV 234
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
390-653 3.07e-10

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 63.33  E-value: 3.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  390 FHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIIND--------------SHNLKDV-N 454
Cdd:PRK13631   31 FDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDiyigdkknnhelitNPYSKKIkN 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  455 LKWWRSKIGVVSQDP--LLFSNSIKNNIKYSLYSLKdlealseesnedgfssqsdsNSRNSCRAKCAGDLNDMiqttdst 532
Cdd:PRK13631  111 FKELRRRVSMVFQFPeyQLFKDTIEKDIMFGPVALG--------------------VKKSEAKKLAKFYLNKM------- 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  533 eliqvrknyetiedsevvsvskkvlihdfvsALPDKYetlVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDN 612
Cdd:PRK13631  164 -------------------------------GLDDSY---LERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDP 209
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 156095386  613 KSEYLVQKTINNLKGNeNRITIIIAHRLSTI-RYANTIFVLS 653
Cdd:PRK13631  210 KGEHEMMQLILDAKAN-NKTVFVITHTMEHVlEVADEVIVMD 250
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
404-612 3.11e-10

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 61.81  E-value: 3.11e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  404 LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVII--NDSHNLKDVNLKWWRSKIGVVSQDP-LLFSNSIKNNI 480
Cdd:PRK10908   21 VTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFsgHDITRLKNREVPFLRRQIGMIFQDHhLLMDRTVYDNV 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  481 KYSLyslkdleALSEESNEDgfssqsdsnsrnsCRAKCAGDLndmiqttDSTELIQVRKNYETiedsevvsvskkvlihd 560
Cdd:PRK10908  101 AIPL-------IIAGASGDD-------------IRRRVSAAL-------DKVGLLDKAKNFPI----------------- 136
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 156095386  561 fvsalpdkyetlvgsnasKLSGGQKQRISIARAIIRNPKILILDEATSSLDN 612
Cdd:PRK10908  137 ------------------QLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDD 170
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
398-644 3.39e-10

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 64.42  E-value: 3.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  398 VEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDshnlkdvnlkwwrskigvVSQDPLLFSNSIK 477
Cdd:PRK09700   18 VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINN------------------INYNKLDHKLAAQ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  478 NNIKYSLYSLKDLEALSEESNEdgfssqsdSNSRNSCRAKCAGDLNDMIQTTDSTELIQVRknyetiedsevvsVSKKVL 557
Cdd:PRK09700   80 LGIGIIYQELSVIDELTVLENL--------YIGRHLTKKVCGVNIIDWREMRVRAAMMLLR-------------VGLKVD 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  558 IHDFVSalpdkyetlvgsnasKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS-EYLVQkTINNLKgNENRITIII 636
Cdd:PRK09700  139 LDEKVA---------------NLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEvDYLFL-IMNQLR-KEGTAIVYI 201

                  ....*...
gi 156095386  637 AHRLSTIR 644
Cdd:PRK09700  202 SHKLAEIR 209
ABC_6TM_bac_exporter_ABCB8_10_like cd18575
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ...
94-308 3.61e-10

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: 62.89  E-value: 3.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   94 ENVNDIIFSLVLIGIFQFILSFISSFCMDVVTTKILKTLKIEFLKSVFYQDGQFHDNN-PG---SKLTSDLDFyLEQVna 169
Cdd:cd18575    33 ALLNRAFLLLLAVALVLALASALRFYLVSWLGERVVADLRKAVFAHLLRLSPSFFETTrTGevlSRLTTDTTL-IQTV-- 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  170 gIGTKFITIFTYASAFLGLYIWSLFKNARLTLCITCVFPLIYICGVICNKKVKINKKTSLLYNNNTMSIIEEALVGIRTV 249
Cdd:cd18575   110 -VGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFGRRVRRLSRASQDRLADLSAFAEETLSAIKTV 188
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  250 VSYCGENTILKKFN-LSEKLYsKYTLKANLMESLHIGMINGFILASYAFGFWYGTRIIIS 308
Cdd:cd18575   189 QAFTREDAERQRFAtAVEAAF-AAALRRIRARALLTALVIFLVFGAIVFVLWLGAHDVLA 247
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
366-640 3.83e-10

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 63.20  E-value: 3.83e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  366 PLVENNQDGKKLKDIKkiqfkNVRFHYDTRK-DVEIYKDLNFTLTEGKTYAFVGESGCGKS-TILKLIERLYDP--TEGD 441
Cdd:PRK09473    1 TVPLAQQQADALLDVK-----DLRVTFSTPDgDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANgrIGGS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  442 VIINDSH--NLKDVNLKWWRS-KIGVVSQDPLLfsnsiknnikyslyslkdlealseesnedgfssqsdsnsrnscrakc 518
Cdd:PRK09473   76 ATFNGREilNLPEKELNKLRAeQISMIFQDPMT----------------------------------------------- 108
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  519 agDLNDMIQTTDstELIQVRKNYETIEDSEVVSVSKKVLihDFVSaLPDKYETLvGSNASKLSGGQKQRISIARAIIRNP 598
Cdd:PRK09473  109 --SLNPYMRVGE--QLMEVLMLHKGMSKAEAFEESVRML--DAVK-MPEARKRM-KMYPHEFSGGMRQRVMIAMALLCRP 180
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 156095386  599 KILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRL 640
Cdd:PRK09473  181 KLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDL 222
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
1183-1431 4.05e-10

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: 61.14  E-value: 4.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1183 KDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYdLKNDHHIVFKNEQTGESSKEQMQQGDEEQNvgmknanefssskeg 1262
Cdd:cd03269    17 DDISFSVEKGEIFGLLGPNGAGKTTTIRMILGII-LPDSGEVLFDGKPLDIAARNRIGYLPEERG--------------- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1263 adgqsstLFKNSgKILldgvDICDYnLKDLRNLfsivsqepmlfnmsiyenikfGKENATREdvkrackfaaIDEFIESL 1342
Cdd:cd03269    81 -------LYPKM-KVI----DQLVY-LAQLKGL---------------------KKEEARRR----------IDEWLERL 116
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1343 pnqydtNVGPYGKS----LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTIITIAHRIA 1418
Cdd:cd03269   117 ------ELSEYANKrveeLSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAG-KTVILSTHQME 189
                         250
                  ....*....|....
gi 156095386 1419 SIKR-SDKIVVFNN 1431
Cdd:cd03269   190 LVEElCDRVLLLNK 203
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
1178-1450 4.25e-10

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 61.95  E-value: 4.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1178 NVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFydlkndhhivfkneqtgesskeqmqqgdeeqnvgmknanefs 1257
Cdd:PRK11231   14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARL------------------------------------------ 51
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1258 sskegadgqsstLFKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPML-FNMSIYENIKFGKE-------NATRED---V 1326
Cdd:PRK11231   52 ------------LTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTpEGITVRELVAYGRSpwlslwgRLSAEDnarV 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1327 KRACKFAAIDEFIESLPNqydtnvgpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKA 1406
Cdd:PRK11231  120 NQAMEQTRINHLADRRLT-----------DLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQG 188
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 156095386 1407 dKTIITIAHRIASIKR-SDKIVVFNNpdrtGSFVqAQGTHEELLS 1450
Cdd:PRK11231  189 -KTVVTVLHDLNQASRyCDHLVVLAN----GHVM-AQGTPEEVMT 227
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
383-611 4.59e-10

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: 61.30  E-value: 4.59e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHYDTR-KDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDsHNLKDVN----LKW 457
Cdd:COG4181     9 IELRGLTKTVGTGaGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAG-QDLFALDedarARL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  458 WRSKIGVVSQDPLLfsnsiknnikysLYSLKDLE--ALSEESnedgfssQSDSNSRNscRAKcagdlndmiqttdsTELi 535
Cdd:COG4181    88 RARHVGFVFQSFQL------------LPTLTALEnvMLPLEL-------AGRRDARA--RAR--------------ALL- 131
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156095386  536 qvrknyetiedsEVVSVSKKVlihdfvSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:COG4181   132 ------------ERVGLGHRL------DHYP-----------AQLSGGEQQRVALARAFATEPAILFADEPTGNLD 178
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
403-668 4.91e-10

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 62.97  E-value: 4.91e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  403 DLNFTL-TEGKTYAFvGESGCGKSTILKLIERLYDPTEGDVIINDsHNL----KDVNLKWWRSKIGVVSQDPLLFSN-SI 476
Cdd:PRK11144   16 TVNLTLpAQGITAIF-GRSGAGKTSLINAISGLTRPQKGRIVLNG-RVLfdaeKGICLPPEKRRIGYVFQDARLFPHyKV 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  477 KNNIKYSlyslkdlealseesnedgfssqsdsnsrnsCRAKCAGDLNDMIQTTDsteliqvrknyetIEdsevvsvskkv 556
Cdd:PRK11144   94 RGNLRYG------------------------------MAKSMVAQFDKIVALLG-------------IE----------- 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  557 lihdfvsALPDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLD--NKSE---YL--VQKTINnlkgne 629
Cdd:PRK11144  120 -------PLLDRY-------PGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlpRKREllpYLerLAREIN------ 179
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 156095386  630 nrITII-IAHRLSTI-RYANTIFVLsnrENGSTVDVDVLGE 668
Cdd:PRK11144  180 --IPILyVSHSLDEIlRLADRVVVL---EQGKVKAFGPLEE 215
cbiO PRK13649
energy-coupling factor transporter ATPase;
1184-1393 5.19e-10

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 62.07  E-value: 5.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1184 DLTFSCESKKTTAIVGETGSGKSTVMSLLmrfydlkNDHHIvfkneqtgesskeqmqqgdeeqnvgmknanefssskega 1263
Cdd:PRK13649   25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLL-------NGLHV--------------------------------------- 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1264 dgqsstlfKNSGKILLDGVDIC----DYNLKDLRNLFSIVSQ--EPMLFNMSIYENIKFGKEN---ATREDVKRACKFAA 1334
Cdd:PRK13649   59 --------PTQGSVRVDDTLITstskNKDIKQIRKKVGLVFQfpESQLFEETVLKDVAFGPQNfgvSQEEAEALAREKLA 130
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 156095386 1335 IDEFIESLpnqYDTNvgPYgkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEK 1393
Cdd:PRK13649  131 LVGISESL---FEKN--PF--ELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRK 182
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
402-638 5.59e-10

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: 61.33  E-value: 5.59e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   402 KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINdshnlkdvnlkwwrskiGVVSQDP-----LLFSNsi 476
Cdd:TIGR01184    2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILE-----------------GKQITEPgpdrmVVFQN-- 62
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   477 knnikYSLYSLKdlealseesnedgfssqsdsnsrnSCRAKCAGDLNDMIQTTDSTEliqvrknYETIEDSEVVSVSkkv 556
Cdd:TIGR01184   63 -----YSLLPWL------------------------TVRENIALAVDRVLPDLSKSE-------RRAIVEEHIALVG--- 103
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   557 lihdfVSALPDKYETlvgsnasKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLkGNENRIT-II 635
Cdd:TIGR01184  104 -----LTEAADKRPG-------QLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELMQI-WEEHRVTvLM 170

                   ...
gi 156095386   636 IAH 638
Cdd:TIGR01184  171 VTH 173
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
1272-1449 6.32e-10

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 63.48  E-value: 6.32e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1272 KNSGKILLDGVDICDYNLKD-LRNLFSIVSQEP----MLFNMSIYENI------KFGKENATredVKRACKFAAIDEFIE 1340
Cdd:PRK10762  304 RTSGYVTLDGHEVVTRSPQDgLANGIVYISEDRkrdgLVLGMSVKENMsltalrYFSRAGGS---LKHADEQQAVSDFIR 380
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1341 SL----PNQyDTNVGpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKdKADKTIITIAHR 1416
Cdd:PRK10762  381 LFniktPSM-EQAIG----LLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFK-AEGLSIILVSSE 454
                         170       180       190
                  ....*....|....*....|....*....|....
gi 156095386 1417 IASI-KRSDKIVVFNNPDRTGSFVQAQGTHEELL 1449
Cdd:PRK10762  455 MPEVlGMSDRILVMHEGRISGEFTREQATQEKLM 488
cbiO PRK13645
energy-coupling factor transporter ATPase;
381-652 6.79e-10

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 61.95  E-value: 6.79e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  381 KKIQFKNVRFHYDTRKDVEiYKDLN---FTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIIND---SHNLKDVN 454
Cdd:PRK13645    5 KDIILDNVSYTYAKKTPFE-FKALNntsLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaiPANLKKIK 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  455 -LKWWRSKIGVVSQDP--LLFSNSIKNNIKYSLYSLKdlealseESNEDGFssqsdsnsrnscraKCAGDLNDMIQttds 531
Cdd:PRK13645   84 eVKRLRKEIGLVFQFPeyQLFQETIEKDIAFGPVNLG-------ENKQEAY--------------KKVPELLKLVQ---- 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  532 teliqvrknyetiedsevvsvskkvlihdfvsaLPDKYetlVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:PRK13645  139 ---------------------------------LPEDY---VKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLD 182
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 156095386  612 NKSEYLVQKTINNLKGNENRITIIIAHRLSTI-RYANTIFVL 652
Cdd:PRK13645  183 PKGEEDFINLFERLNKEYKKRIIMVTHNMDQVlRIADEVIVM 224
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
387-671 6.98e-10

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 63.72  E-value: 6.98e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  387 NVRFHYDtRKDVEIYKDLNFTLTEGKTYAFVGESGCGKS-TILKLIeRLYDPTEGDviindshnlkdvnlkwwrskigvV 465
Cdd:PRK10261   19 NIAFMQE-QQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALM-RLLEQAGGL-----------------------V 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  466 SQDPLLFSNSIKNNIkyslyslkdleALSEesnedgfssQSDSNSRNSCRAKCAgdlndMIQTTDSTELIQVRKNYETIE 545
Cdd:PRK10261   74 QCDKMLLRRRSRQVI-----------ELSE---------QSAAQMRHVRGADMA-----MIFQEPMTSLNPVFTVGEQIA 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  546 DS----------EVVSVSKKVLihDFVSaLPDKyETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSE 615
Cdd:PRK10261  129 ESirlhqgasreEAMVEAKRML--DQVR-IPEA-QTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQ 204
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 156095386  616 YLVQKTINNLKGNENRITIIIAHRLSTI-RYANTIFVLSNRENGSTVDVDVLGEDPT 671
Cdd:PRK10261  205 AQILQLIKVLQKEMSMGVIFITHDMGVVaEIADRVLVMYQGEAVETGSVEQIFHAPQ 261
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
1353-1395 8.44e-10

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 63.19  E-value: 8.44e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 156095386 1353 YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLI 1395
Cdd:PRK15134  422 YPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQI 464
ABC_6TM_YwjA_like cd18549
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ...
59-347 9.08e-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: 61.70  E-value: 9.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   59 RKLLGVSFVCATISGGT---LPFFVSVF---GVIMKNMNLGenvndIIFSLVLIGIFqfILSFISSFCMD----VVTTKI 128
Cdd:cd18549     1 KKLFFLDLFCAVLIAALdlvFPLIVRYIiddLLPSKNLRLI-----LIIGAILLALY--ILRTLLNYFVTywghVMGARI 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  129 LKTLKIEFLKSVFYQDGQFHDNNP-G---SKLTSDLdFYL-EQVNAGIGTKFITIFTyasaFLGLYIWSLFKNARLTLCI 203
Cdd:cd18549    74 ETDMRRDLFEHLQKLSFSFFDNNKtGqlmSRITNDL-FDIsELAHHGPEDLFISIIT----IIGSFIILLTINVPLTLIV 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  204 TCVFPLIYICGVICNKKVK-----INKKTSLLYnnntmSIIEEALVGIRTVVSYCGENTILKKFNLSEKLYSKYTLKANL 278
Cdd:cd18549   149 FALLPLMIIFTIYFNKKMKkafrrVREKIGEIN-----AQLEDSLSGIRVVKAFANEEYEIEKFDEGNDRFLESKKKAYK 223
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156095386  279 MESLHIGMINGFI----LASYAFGFW--YGTRIIISDLsnqqpnndfhggsvISILLgvLISMFMLTI-ILPNITE 347
Cdd:cd18549   224 AMAYFFSGMNFFTnllnLVVLVAGGYfiIKGEITLGDL--------------VAFLL--YVNVFIKPIrRLVNFTE 283
cbiO PRK13646
energy-coupling factor transporter ATPase;
1240-1450 9.35e-10

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 61.33  E-value: 9.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1240 QQGDEEQNVGMKNAN-EFSSSKEGA-DGQS----STLFKN--------SGKILLDGVDIC----DYNLKDLRNLFSIVSQ 1301
Cdd:PRK13646   13 QKGTPYEHQAIHDVNtEFEQGKYYAiVGQTgsgkSTLIQNinallkptTGTVTVDDITIThktkDKYIRPVRKRIGMVFQ 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1302 --EPMLFNMSIYENIKFGKENaTREDVKRAcKFAAIDEFIESLPNQYDTNVGPYgkSLSGGQKQRIAIARALLREPKILL 1379
Cdd:PRK13646   93 fpESQLFEDTVEREIIFGPKN-FKMNLDEV-KNYAHRLLMDLGFSRDVMSQSPF--QMSGGQMRKIAIVSILAMNPDIIV 168
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 156095386 1380 LDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVVFNNpdrtGSFVQaQGTHEELLS 1450
Cdd:PRK13646  169 LDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARyADEVIVMKE----GSIVS-QTSPKELFK 235
ABC_6TM_ABCB10_like cd18573
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ...
826-1115 9.59e-10

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: 61.38  E-value: 9.59e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  826 AIIALSIMVAGGL-YPLFallyakyVGTLFDFANLEANSNK---YSLY--------ILVI-AIAMFisetLKNYYNNVIG 892
Cdd:cd18573     1 ALALLLVSSAVTMsVPFA-------IGKLIDVASKESGDIEifgLSLKtfalallgVFVVgAAANF----GRVYLLRIAG 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  893 EKVEKTMKLRLFENIMYQEISFFDQdsHAPGLLsahINR---DVHLLKTGLVNNIVIFTHFIVLFLVSTVMSFYFCPIVA 969
Cdd:cd18573    70 ERIVARLRKRLFKSILRQDAAFFDK--NKTGEL---VSRlssDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLT 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  970 AVLTGT---YFIFMRVFAIRARIAANKdvekkrvnqpgtafVYNSDDEIFKdpsfLIQEAFYNMNTVIIYGLEDYFCTLI 1046
Cdd:cd18573   145 LVMLLVvppIAVGAVFYGRYVRKLSKQ--------------VQDALADATK----VAEERLSNIRTVRAFAAERKEVERY 206
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 156095386 1047 EKAIDYSNKGQKRKTLINSMLWGfsqSAQFFINSFAY---WFGSFLIRRGTIQVDDfmksLFTFLFTGSYAG 1115
Cdd:cd18573   207 AKKVDEVFDLAKKEALASGLFFG---STGFSGNLSLLsvlYYGGSLVASGELTVGD----LTSFLMYAVYVG 271
ABC_6TM_bac_exporter_ABCB8_10_like cd18576
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ...
833-1120 9.85e-10

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: 61.35  E-value: 9.85e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  833 MVAGGLYPLFALLYAKYVGTLFDFANLEANS---NKYSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMKLRLFENIMY 909
Cdd:cd18576     2 LILLLLSSAIGLVFPLLAGQLIDAALGGGDTaslNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  910 QEISFFDQDSHapGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSTVMSFYFCPIVAAVLTGT---YFIFMRVF--A 984
Cdd:cd18576    82 LPLSFFHERRV--GELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATvpvVVLVAVLFgrR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  985 IRaRIAankdveKKRVNQPGTAFVYnsddeifkdpsflIQEAFYNMNTVIIYGLEDY----FCTLIEKAIDYSNKGQKrk 1060
Cdd:cd18576   160 IR-KLS------KKVQDELAEANTI-------------VEETLQGIRVVKAFTREDYeierYRKALERVVKLALKRAR-- 217
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 156095386 1061 tlINSMLWGFSQSAQFFINSFAYWFGSFLIRRGTIQVDDfmksLFTFLF-TGSYAGKLMSL 1120
Cdd:cd18576   218 --IRALFSSFIIFLLFGAIVAVLWYGGRLVLAGELTAGD----LVAFLLyTLFIAGSIGSL 272
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
1265-1412 1.10e-09

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 60.68  E-value: 1.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1265 GQSSTLF-------KNSGKILLDGVDICDYNLKD-LRNLFSIVSQEPMLFN-MSIYENIKFGKEnaTREDVKRACKFAAI 1335
Cdd:PRK10895   41 GKTTTFYmvvgivpRDAGNIIIDDEDISLLPLHArARRGIGYLPQEASIFRrLSVYDNLMAVLQ--IRDDLSAEQREDRA 118
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156095386 1336 DEFIESLPNQYDTNvgPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIIT 1412
Cdd:PRK10895  119 NELMEEFHIEHLRD--SMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLIT 193
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
392-636 1.14e-09

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: 60.25  E-value: 1.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  392 YDTRKDVeiyKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDsHNLKDVNL-KWWRSKIGVVSQDPL 470
Cdd:cd03218    10 YGKRKVV---NGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDG-QDITKLPMhKRARLGIGYLPQEAS 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  471 LFSN-SIKNNIKYSLYSLKDLEALSEESNEDgfssqsdsnsrnscrakcagdlndmiqttdsteliqvrknyetiedsev 549
Cdd:cd03218    86 IFRKlTVEENILAVLEIRGLSKKEREEKLEE------------------------------------------------- 116
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  550 vsvskkvLIHDFvsalpdKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnE 629
Cdd:cd03218   117 -------LLEEF------HITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILK--D 181

                  ....*..
gi 156095386  630 NRITIII 636
Cdd:cd03218   182 RGIGVLI 188
TauB COG4525
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
1357-1417 1.21e-09

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


Pssm-ID: 443596 [Multi-domain]  Cd Length: 262  Bit Score: 60.65  E-value: 1.21e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 156095386 1357 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRI 1417
Cdd:COG4525   135 LSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSV 195
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
390-636 1.22e-09

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: 60.42  E-value: 1.22e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  390 FHYDTRkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDshnlkdvnLKWWRSKIGVVSQDP 469
Cdd:cd03267    27 FKRKYR-EVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG--------LVPWKRRKKFLRRIG 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  470 LLFSNsiKNNIKYslyslkDLEALseesneDGFSsqsdsnsrnscrakcagdLNDMIQTTDSTELiqvRKNYETIedSEV 549
Cdd:cd03267    98 VVFGQ--KTQLWW------DLPVI------DSFY------------------LLAAIYDLPPARF---KKRLDEL--SEL 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  550 VSVskkvlihdfvsalpdkyETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLkgNE 629
Cdd:cd03267   141 LDL-----------------EELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEY--NR 201

                  ....*..
gi 156095386  630 NRITIII 636
Cdd:cd03267   202 ERGTTVL 208
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
1274-1428 1.22e-09

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: 62.53  E-value: 1.22e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1274 SGKILLDGVDICDYNLKDL-RNLFSIVSQEPMLF-NMSIYENIKFGKE---NATRED----VKRACKFAA---IDEFIES 1341
Cdd:TIGR02633   57 DGEIYWSGSPLKASNIRDTeRAGIVIIHQELTLVpELSVAENIFLGNEitlPGGRMAynamYLRAKNLLRelqLDADNVT 136
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1342 LPnqydtnVGPYGkslsGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTIITIAHRIASIK 1421
Cdd:TIGR02633  137 RP------VGDYG----GGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHG-VACVYISHKLNEVK 205

                   ....*...
gi 156095386  1422 R-SDKIVV 1428
Cdd:TIGR02633  206 AvCDTICV 213
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
374-611 1.24e-09

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 62.39  E-value: 1.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  374 GKKLkdikkIQFKNVRFHYDtrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIIndSHNLkdv 453
Cdd:COG0488   312 GKKV-----LELEGLSKSYG---DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL--GETV--- 378
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  454 nlkwwrsKIGVVSQdpllfsnsiknnikyslyslkDLEALSEESNedgfssqsdsnsrnscrakcagdlndMIQttdstE 533
Cdd:COG0488   379 -------KIGYFDQ---------------------HQEELDPDKT--------------------------VLD-----E 399
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  534 LIQVRKNYETIEdsevvsvskkvlIHDFVSAL---PDKYETLVGsnasKLSGGQKQRISIARAIIRNPKILILDEATSSL 610
Cdd:COG0488   400 LRDGAPGGTEQE------------VRGYLGRFlfsGDDAFKPVG----VLSGGEKARLALAKLLLSPPNVLLLDEPTNHL 463

                  .
gi 156095386  611 D 611
Cdd:COG0488   464 D 464
nickel_nikE TIGR02769
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ...
1164-1455 1.45e-09

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: 60.59  E-value: 1.45e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1164 IEIMDVNFRYLS------RPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFydlkndhhivfkneqtgesskE 1237
Cdd:TIGR02769    3 LEVRDVTHTYRTgglfgaKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGL---------------------E 61
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1238 QMQQGdeeqNVGMKnanefssskegadGQSSTLFKNSGKilldgvdicdynlKDLRNLFSIVSQE-PMLFN--MSIYENI 1314
Cdd:TIGR02769   62 KPAQG----TVSFR-------------GQDLYQLDRKQR-------------RAFRRDVQLVFQDsPSAVNprMTVRQII 111
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1315 KFGKENATRED-VKRACKFAAIDEFIESLPNQYDTnvgpYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEK 1393
Cdd:TIGR02769  112 GEPLRHLTSLDeSEQKARIAELLDMVGLRSEDADK----LPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQA 187
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 156095386  1394 LIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVVFNNpdrtGSFVQAQGTHEELLSVQDGV 1455
Cdd:TIGR02769  188 VILELLRKLQQAFGTAYLFITHDLRLVQSfCQRVAVMDK----GQIVEECDVAQLLSFKHPAG 246
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
396-644 1.47e-09

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 60.15  E-value: 1.47e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  396 KDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEG-----DVIINDSHNLKDVN--LKWWRSKIGVVSQD 468
Cdd:PRK11264   14 HGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGtirvgDITIDTARSLSQQKglIRQLRQHVGFVFQN 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  469 PLLFSNsiknnikyslyslkdlealseesnedgfssqsdsnsRNScrakcagdLNDMIQTTdstelIQVRKnyetIEDSE 548
Cdd:PRK11264   94 FNLFPH------------------------------------RTV--------LENIIEGP-----VIVKG----EPKEE 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  549 VVSVSKKVLIHDFVSALPDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKseyLVQKTINNLKG- 627
Cdd:PRK11264  121 ATARARELLAKVGLAGKETSY-------PRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPE---LVGEVLNTIRQl 190
                         250
                  ....*....|....*...
gi 156095386  628 -NENRITIIIAHRLSTIR 644
Cdd:PRK11264  191 aQEKRTMVIVTHEMSFAR 208
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
394-611 1.50e-09

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


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 59.42  E-value: 1.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  394 TRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDP---TEGDVIINDshnlKDVN-LKWWRSKIGVVSQDP 469
Cdd:COG4136    10 TLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNG----RRLTaLPAEQRRIGILFQDD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  470 LLFSN-SIKNNIKYSLyslkdlealseesnedgfssqSDSNSRNSCRAKCAgdlndmiQTTDSTELiqvrknyetiedse 548
Cdd:COG4136    86 LLFPHlSVGENLAFAL---------------------PPTIGRAQRRARVE-------QALEEAGL-------------- 123
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 156095386  549 vvsvskkvliHDFVSALPDKyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:COG4136   124 ----------AGFADRDPAT-----------LSGGQRARVALLRALLAEPRALLLDEPFSKLD 165
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
399-651 1.69e-09

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 60.37  E-value: 1.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  399 EIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDsHNLKDVNLKWWRSKIGVVSQDPLLFSNSIKN 478
Cdd:PRK10619   19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNG-QTINLVRDKDGQLKVADKNQLRLLRTRLTMV 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  479 NIKYSLYS-LKDLEALSEESnedgfssqsdsnsrnscrakcagdlndmiqttdstelIQVRKNYETIEDSEVVSVSKKVL 557
Cdd:PRK10619   98 FQHFNLWShMTVLENVMEAP-------------------------------------IQVLGLSKQEARERAVKYLAKVG 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  558 IHDfvsALPDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLkGNENRITIIIA 637
Cdd:PRK10619  141 IDE---RAQGKY-------PVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQL-AEEGKTMVVVT 209
                         250
                  ....*....|....*.
gi 156095386  638 HRLSTIRYANT--IFV 651
Cdd:PRK10619  210 HEMGFARHVSShvIFL 225
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
1174-1388 1.71e-09

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 62.00  E-value: 1.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1174 LSRPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMrfydlkndhhivfkneqtgesskeqmqqGDEEqnvgmkna 1253
Cdd:COG0488     6 KSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILA----------------------------GELE-------- 49
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1254 nefssskegADgqsstlfknSGKILLDgvdicdynlKDLRnlFSIVSQEPMLF-NMSIYENIKFG--------------- 1317
Cdd:COG0488    50 ---------PD---------SGEVSIP---------KGLR--IGYLPQEPPLDdDLTVLDTVLDGdaelraleaeleele 100
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1318 -KENATREDVKRA----CKFAAIDEF-----IESL-------PNQYDTNVGpygkSLSGGQKQRIAIARALLREPKILLL 1380
Cdd:COG0488   101 aKLAEPDEDLERLaelqEEFEALGGWeaearAEEIlsglgfpEEDLDRPVS----ELSGGWRRRVALARALLSEPDLLLL 176

                  ....*...
gi 156095386 1381 DEATSSLD 1388
Cdd:COG0488   177 DEPTNHLD 184
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
578-652 1.87e-09

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 60.03  E-value: 1.87e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156095386  578 SKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLS-TIRYANTIFVL 652
Cdd:PRK09984  151 STLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDyALRYCERIVAL 226
ABC_6TM_bac_exporter_ABCB8_10_like cd18576
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ...
65-309 1.99e-09

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: 60.58  E-value: 1.99e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   65 SFVCATISGGT---LPFFV-SVFGVIMKNMNLGeNVNDIIFSLVLIGIFQFILSFISSFCMDVVTTKILKTLKIEFLKSV 140
Cdd:cd18576     1 GLILLLLSSAIglvFPLLAgQLIDAALGGGDTA-SLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  141 FYQDGQFHDNN-PG---SKLTSDldfyLEQVNAGIGTKFITIFTYASAFLGLYIWSLFKNARLTLCITCVFPLIYICGVI 216
Cdd:cd18576    80 QRLPLSFFHERrVGeltSRLSND----VTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  217 CNKKV-KINKKT--SLlynNNTMSIIEEALVGIRTVVSYCGENTILKKFNLSEKLYSKYTLKANLMESLHIGMINGFILA 293
Cdd:cd18576   156 FGRRIrKLSKKVqdEL---AEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFG 232
                         250
                  ....*....|....*.
gi 156095386  294 SYAFGFWYGTRIIISD 309
Cdd:cd18576   233 AIVAVLWYGGRLVLAG 248
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
1353-1418 2.18e-09

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 59.76  E-value: 2.18e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156095386 1353 YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSnseKLIEKTIVDIKDKAD--KTIITIAHRIA 1418
Cdd:PRK11264  141 YPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDP---ELVGEVLNTIRQLAQekRTMVIVTHEMS 205
ABC_6TM_ABCB10_like cd18573
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ...
61-308 2.47e-09

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: 60.22  E-value: 2.47e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   61 LLGVSfvcatiSGGTL--PFFV-----SVFGVIMKNMNLGENVNdiIFSLVLIGIFQF--ILSFISSFCMDVVTTKILKT 131
Cdd:cd18573     4 LLLVS------SAVTMsvPFAIgklidVASKESGDIEIFGLSLK--TFALALLGVFVVgaAANFGRVYLLRIAGERIVAR 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  132 LKIEFLKSVFYQDGQFHDNNP----GSKLTSDLDFYLEQV--NAGIGTKFItIFTYASAFLGLYIwslfkNARLTLCITC 205
Cdd:cd18573    76 LRKRLFKSILRQDAAFFDKNKtgelVSRLSSDTSVVGKSLtqNLSDGLRSL-VSGVGGIGMMLYI-----SPKLTLVMLL 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  206 VFPLIYICGVICNKKVKinKKTSLLYNN--NTMSIIEEALVGIRTVVSYCGENTILKKFNLSEKLYSKYTLKANLMESLH 283
Cdd:cd18573   150 VVPPIAVGAVFYGRYVR--KLSKQVQDAlaDATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLF 227
                         250       260
                  ....*....|....*....|....*
gi 156095386  284 IGMINGFILASYAFGFWYGTRIIIS 308
Cdd:cd18573   228 FGSTGFSGNLSLLSVLYYGGSLVAS 252
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
1164-1388 2.75e-09

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 59.40  E-value: 2.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYLSRPnvpIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfkneqTGEsskeqmqqgd 1243
Cdd:PRK13548    3 LEARNLSVRLGGRT---LLDDVSLTLRPGEVVAILGPNGAGKSTLLRAL------------------SGE---------- 51
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 eeqnvgmknanefssskegadgqsstLFKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPML-FNMSIYENIKFGKENAT 1322
Cdd:PRK13548   52 --------------------------LSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFTVEEVVAMGRAPHG 105
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156095386 1323 REDVKRAckfAAIDEFIESlpnqydTNVGPYGK----SLSGGQKQRIAIARALLR------EPKILLLDEATSSLD 1388
Cdd:PRK13548  106 LSRAEDD---ALVAAALAQ------VDLAHLAGrdypQLSGGEQQRVQLARVLAQlwepdgPPRWLLLDEPTSALD 172
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
403-654 3.07e-09

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 61.26  E-value: 3.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  403 DLNFTLTEGKTYAFVGESGCGKS-TILKLIERLYDP----TEGDVIINDSHNLK--DVNLKWWR-SKIGVVSQDPLLFSN 474
Cdd:PRK15134   27 DVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHasEQTLRGVRgNKIAMIFQEPMVSLN 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  475 SIkNNIKYSLYslkdlEALSEESNEdgfssqsdsnSRNSCRAkcagdlnDMIQTTDSTELIQVRKNyetiedsevvsvsk 554
Cdd:PRK15134  107 PL-HTLEKQLY-----EVLSLHRGM----------RREAARG-------EILNCLDRVGIRQAAKR-------------- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  555 kvlIHDFvsalpdkyetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITI 634
Cdd:PRK15134  150 ---LTDY---------------PHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLL 211
                         250       260
                  ....*....|....*....|.
gi 156095386  635 IIAHRLSTIR-YANTIFVLSN 654
Cdd:PRK15134  212 FITHNLSIVRkLADRVAVMQN 232
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
388-445 3.07e-09

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


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 59.32  E-value: 3.07e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 156095386  388 VRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIIN 445
Cdd:COG1134    29 LRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVN 86
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
1337-1429 3.13e-09

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 61.36  E-value: 3.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1337 EFIE--SLPNQYDTNVgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIA 1414
Cdd:PRK13409  436 EIIKplQLERLLDKNV----KDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVD 511
                          90
                  ....*....|....*.
gi 156095386 1415 HRIASIKR-SDKIVVF 1429
Cdd:PRK13409  512 HDIYMIDYiSDRLMVF 527
ABC_6TM_AtABCB27_like cd18780
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ...
864-1123 3.15e-09

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: 59.96  E-value: 3.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  864 NKYSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMKLRLFENIMYQEISFFDQdsHAPGLLSAHINRDVHLLKTGLVNN 943
Cdd:cd18780    42 NQAVLILLGVVLIGSIATFLRSWLFTLAGERVVARLRKRLFSAIIAQEIAFFDV--TRTGELLNRLSSDTQVLQNAVTVN 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  944 IVIFTHFIVLFLVSTVMSFYFCPivaaVLTGTYFIFMRVFAIRARIAANKDVEKKRVNQPGTAfvynsddeifkDPSFLI 1023
Cdd:cd18780   120 LSMLLRYLVQIIGGLVFMFTTSW----KLTLVMLSVVPPLSIGAVIYGKYVRKLSKKFQDALA-----------AASTVA 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1024 QEAFYNMNTVIIYGLEDYFCTLIEKAIDYSNKGQKRKTLINSMLWGFSQSAQFFINSFAYWFGSFLIRRGTIQVDD---F 1100
Cdd:cd18780   185 EESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQLAIVLVLWYGGRLVIDGELTTGLltsF 264
                         250       260
                  ....*....|....*....|...
gi 156095386 1101 MksLFTFLFTGSYAGkLMSLKGD 1123
Cdd:cd18780   265 L--LYTLTVAMSFAF-LSSLYGD 284
ABC_6TM_PCAT1_LagD_like cd18570
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ...
825-1134 3.56e-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: 59.77  E-value: 3.56e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  825 IAIIALSIMVAgglypLFALLYAKYVGTLFDF---ANLEANSNKYSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMKL 901
Cdd:cd18570     5 ILILLLSLLIT-----LLGIAGSFFFQILIDDiipSGDINLLNIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLIL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  902 RLFENIMYQEISFFdqDSHAPGLLSAHIN-----RDV--HLLKTGLVNNIVIFTHFIVLFLVSTVMsFYFCPIVAAVLTG 974
Cdd:cd18570    80 GYFKHLLKLPLSFF--ETRKTGEIISRFNdankiREAisSTTISLFLDLLMVIISGIILFFYNWKL-FLITLLIIPLYIL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  975 TYFIFMRVF--AIRARIAANKDVEkkrvnqpgtafvynsddeifkdpSFLIqEAFYNMNTVIIYGLEDYFCTLIEKAIDY 1052
Cdd:cd18570   157 IILLFNKPFkkKNREVMESNAELN-----------------------SYLI-ESLKGIETIKSLNAEEQFLKKIEKKFSK 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1053 SNKGQKRKTLINSMLWGFSQSAQFFINSFAYWFGSFLIRRGTIQVDDFM--KSLFTFlFTGSyAGKLMSLKGDSENAKLS 1130
Cdd:cd18570   213 LLKKSFKLGKLSNLQSSIKGLISLIGSLLILWIGSYLVIKGQLSLGQLIafNALLGY-FLGP-IENLINLQPKIQEAKVA 290

                  ....
gi 156095386 1131 FERY 1134
Cdd:cd18570   291 ADRL 294
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
1355-1431 3.77e-09

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


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 59.74  E-value: 3.77e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 156095386 1355 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDS-NSEkLIEKTIVDIKDKaDKTIITIAHRIASIKR-SDKIVVFNN 1431
Cdd:COG4152   128 EELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPvNVE-LLKDVIRELAAK-GTTVIFSSHQMELVEElCDRIVIINK 204
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
1274-1431 4.27e-09

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: 57.44  E-value: 4.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1274 SGKILLDGVDICDYNLKDLRNL-FSIVSQEPM---LF-NMSIYENIkfgkenatredvkrackfaaidefieSLPNQydt 1348
Cdd:cd03215    54 SGEITLDGKPVTRRSPRDAIRAgIAYVPEDRKregLVlDLSVAENI--------------------------ALSSL--- 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1349 nvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkADKTIITIAHRIASIKR-SDKIV 1427
Cdd:cd03215   105 --------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELAD-AGKAVLLISSELDELLGlCDRIL 175

                  ....
gi 156095386 1428 VFNN 1431
Cdd:cd03215   176 VMYE 179
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
1341-1429 4.49e-09

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: 60.95  E-value: 4.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1341 SLPNQYDTNVgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASI 1420
Cdd:COG1245   444 GLEKLLDKNV----KDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLI 519
                          90
                  ....*....|
gi 156095386 1421 KR-SDKIVVF 1429
Cdd:COG1245   520 DYiSDRLMVF 529
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
369-654 4.68e-09

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: 59.10  E-value: 4.68e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  369 ENNQDGKKLKDIKKIQFKNVRFHYDTrkdveIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGdvIINDSh 448
Cdd:cd03291    26 QENNDRKHSSDDNNLFFSNLCLVGAP-----VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEG--KIKHS- 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  449 nlkdvnlkwwrSKIGVVSQDPLLFSNSIKNNIKYSLyslkdlealseesnedgfssqsdsnSRNSCRAKcagdlndmiqt 528
Cdd:cd03291    98 -----------GRISFSSQFSWIMPGTIKENIIFGV-------------------------SYDEYRYK----------- 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  529 tdsteliqvrknyetiedsevvSVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATS 608
Cdd:cd03291   131 ----------------------SVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFG 188
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 156095386  609 SLDNKSEYLV-QKTINNLKGNENRitIIIAHRLSTIRYANTIFVLSN 654
Cdd:cd03291   189 YLDVFTEKEIfESCVCKLMANKTR--ILVTSKMEHLKKADKILILHE 233
PvdE COG4615
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...
378-472 4.88e-09

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: 60.58  E-value: 4.88e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  378 KDIKKIQFKNVRFHYDTRKDVEIYK--DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDsHNLKDVNL 455
Cdd:COG4615   323 ADFQTLELRGVTYRYPGEDGDEGFTlgPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDG-QPVTADNR 401
                          90
                  ....*....|....*..
gi 156095386  456 KWWRSKIGVVSQDPLLF 472
Cdd:COG4615   402 EAYRQLFSAVFSDFHLF 418
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
1339-1429 5.03e-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: 58.57  E-value: 5.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1339 IESLpnqYDTNVgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIA 1418
Cdd:cd03237   105 IEQI---LDREV----PELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNEKTAFVVEHDII 177
                          90
                  ....*....|..
gi 156095386 1419 SIKR-SDKIVVF 1429
Cdd:cd03237   178 MIDYlADRLIVF 189
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
1183-1451 5.16e-09

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: 60.59  E-value: 5.16e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1183 KDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDLKNDHHIVFKNEQTGESskeqmqqgdeeqnVGMKNANEFSSSKEG 1262
Cdd:TIGR03269   17 KNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEPTSGRIIYHVALCEK-------------CGYVERPSKVGEPCP 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1263 ADGQSSTLFKnsgkilLDGVDICDYNLKDLRNLFSIVSQEPMLF--NMSIYENIKFGKENA---TREDVKRACkfaaidE 1337
Cdd:TIGR03269   84 VCGGTLEPEE------VDFWNLSDKLRRRIRKRIAIMLQRTFALygDDTVLDNVLEALEEIgyeGKEAVGRAV------D 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1338 FIESLpnQYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRI 1417
Cdd:TIGR03269  152 LIEMV--QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWP 229
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 156095386  1418 ASI-KRSDKIVVFNNpdrtGSFVQaQGTHEELLSV 1451
Cdd:TIGR03269  230 EVIeDLSDKAIWLEN----GEIKE-EGTPDEVVAV 259
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
1330-1433 5.17e-09

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: 56.61  E-value: 5.17e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   1330 CKFAAIDEFIESLPNQY-DTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVD-----IK 1403
Cdd:smart00382   33 VIYIDGEDILEEVLDQLlLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELrllllLK 112
                            90       100       110
                    ....*....|....*....|....*....|....*.
gi 156095386   1404 DKADKTIITIAHRIASIK------RSDKIVVFNNPD 1433
Cdd:smart00382  113 SEKNLTVILTTNDEKDLGpallrrRFDRRIVLLLIL 148
ABC_6TM_TmrA_like cd18544
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ...
99-309 5.88e-09

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: 58.94  E-value: 5.88e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   99 IIFSLVLIG--IFQFILSFISSFCMDVVTTKILKTLKIEFLKSVFYQDGQFHDNNPG----SKLTSDLDFYLEQVNAGIG 172
Cdd:cd18544    41 LLLALLYLGllLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDRTPVgrlvTRVTNDTEALNELFTSGLV 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  173 TKFITIFTyasaFLGLYIWSLFKNARLTLCITCVFPLIYICGVICNKKVK-----INKKTSLLynnNTMsiIEEALVGIR 247
Cdd:cd18544   121 TLIGDLLL----LIGILIAMFLLNWRLALISLLVLPLLLLATYLFRKKSRkayreVREKLSRL---NAF--LQESISGMS 191
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 156095386  248 TVVSYCGENTILKKFN-LSEKLYsKYTLKANLMESLHIGMINGFILASYAFGFWYGTRIIISD 309
Cdd:cd18544   192 VIQLFNREKREFEEFDeINQEYR-KANLKSIKLFALFRPLVELLSSLALALVLWYGGGQVLSG 253
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
1357-1431 6.76e-09

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: 55.92  E-value: 6.76e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156095386 1357 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKdkadKTIITIAHRIASIKR-SDKIVVFNN 1431
Cdd:cd03221    71 LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEYP----GTVILVSHDRYFLDQvATKIIELED 142
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
1269-1449 7.00e-09

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 60.13  E-value: 7.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1269 TLF----KNSGKILLDGVDICDYN-LKDLRNLFSIVSQE----------PMLFNmSIYENIKFGKENATREDVKRACKFA 1333
Cdd:PRK10982  293 TLFgireKSAGTITLHGKKINNHNaNEAINHGFALVTEErrstgiyaylDIGFN-SLISNIRNYKNKVGLLDNSRMKSDT 371
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1334 --AIDEFIESLPNQYdTNVGpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKaDKTII 1411
Cdd:PRK10982  372 qwVIDSMRVKTPGHR-TQIG----SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGII 445
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 156095386 1412 TIAHRIAS-IKRSDKIVVFNNPDRTGSFVQAQGTHEELL 1449
Cdd:PRK10982  446 IISSEMPElLGITDRILVMSNGLVAGIVDTKTTTQNEIL 484
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
389-445 8.40e-09

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: 57.54  E-value: 8.40e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 156095386  389 RFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIIN 445
Cdd:cd03220    26 LGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVR 82
ABC_6TM_Tm288_like cd18547
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ...
825-1097 8.66e-09

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: 58.57  E-value: 8.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  825 IAIIALSIMVAGGLY-PLF------ALLYAKYVGTLFDFANLeansNKYSLYILVIAIAMFISETLKNYYNNVIGEKVEK 897
Cdd:cd18547     3 LVIILAIISTLLSVLgPYLlgkaidLIIEGLGGGGGVDFSGL----LRILLLLLGLYLLSALFSYLQNRLMARVSQRTVY 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  898 TMKLRLFENIMYQEISFFDQdsHAPG-LLSAHINrDVHLLKTGLVNNIVIFTHFIVLFLVSTVMSFYFCP---IVAAVLT 973
Cdd:cd18547    79 DLRKDLFEKLQRLPLSYFDT--HSHGdIMSRVTN-DVDNISQALSQSLTQLISSILTIVGTLIMMLYISPlltLIVLVTV 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  974 GTYFIFMRVFAIRARIAAnkdveKKRVNQPG--TAFvynsddeifkdpsflIQEAFYNMNTVIIYGLEDY----FCTLIE 1047
Cdd:cd18547   156 PLSLLVTKFIAKRSQKYF-----RKQQKALGelNGY---------------IEEMISGQKVVKAFNREEEaieeFDEINE 215
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 156095386 1048 KAIDYSNKGQKRKTLINSMLwgfsqsaqFFINSFAY----WFGSFLIRRGTIQV 1097
Cdd:cd18547   216 ELYKASFKAQFYSGLLMPIM--------NFINNLGYvlvaVVGGLLVINGALTV 261
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
404-611 1.10e-08

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 57.28  E-value: 1.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  404 LNFTLT--EGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDS-HNLKDVNlkwwRSKIGVVSQDPLLFSN-SIKNN 479
Cdd:PRK10771   16 MRFDLTveRGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQdHTTTPPS----RRPVSMLFQENNLFSHlTVAQN 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  480 IKYSLY-SLKdleaLSEESNEdgfssqsdsnsrnscrakcagdlndmiqttdsteliqvrknyetiedsEVVSVSKKVLI 558
Cdd:PRK10771   92 IGLGLNpGLK----LNAAQRE------------------------------------------------KLHAIARQMGI 119
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 156095386  559 HDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:PRK10771  120 EDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEPFSALD 161
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
399-611 1.17e-08

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 58.56  E-value: 1.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  399 EIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDViindSHNLKDVNLKWWRS-KIGVVSQDPLLFSN-SI 476
Cdd:PRK10851   16 QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHI----RFHGTDVSRLHARDrKVGFVFQHYALFRHmTV 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  477 KNNIKYSLYSLKDLEALSeesnedgfssqsdsnsRNSCRAKCAgDLNDMIQttdsteliqvrknyetiedsevvsvskkv 556
Cdd:PRK10851   92 FDNIAFGLTVLPRRERPN----------------AAAIKAKVT-QLLEMVQ----------------------------- 125
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 156095386  557 LIHdfvsaLPDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:PRK10851  126 LAH-----LADRY-------PAQLSGGQKQRVALARALAVEPQILLLDEPFGALD 168
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
386-625 1.25e-08

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 57.77  E-value: 1.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  386 KNVRFHYDTRkdvEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINdSHNLKDVnlkwwRSKIGVV 465
Cdd:PRK11247   16 NAVSKRYGER---TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAG-TAPLAEA-----REDTRLM 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  466 SQDP-LLFSNSIKNNIKYSL---YSLKDLEALSEESNEDgfssqsdsnsrnscRAkcagdlndmiqttdsteliqvrkny 541
Cdd:PRK11247   87 FQDArLLPWKKVIDNVGLGLkgqWRDAALQALAAVGLAD--------------RA------------------------- 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  542 etiedsevvsvskkvliHDFVSALpdkyetlvgsnasklSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKT 621
Cdd:PRK11247  128 -----------------NEWPAAL---------------SGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDL 175

                  ....
gi 156095386  622 INNL 625
Cdd:PRK11247  176 IESL 179
ABC_6TM_YknU_like cd18542
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ...
825-1118 1.31e-08

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: 57.83  E-value: 1.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  825 IAIIALSIMVAgglyplFALLYAKYVGTLFDFANLEANSN---KYSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMKL 901
Cdd:cd18542     3 LAILALLLATA------LNLLIPLLIRRIIDSVIGGGLREllwLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRN 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  902 RLFENIMYQEISFFDqdsHAP-GLLSAHINRDV----HLLKTGL---VNNIVIFT-HFIVLFLVSTVMSFY---FCPIVa 969
Cdd:cd18542    77 DLYDHLQRLSFSFHD---KARtGDLMSRCTSDVdtirRFLAFGLvelVRAVLLFIgALIIMFSINWKLTLIslaIIPFI- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  970 avltgtyFIFMRVFAIRARiaankdvekkrvnqpgtafvynsddEIFKDpsflIQEAFYNMNTVI---IYG--------L 1038
Cdd:cd18542   153 -------ALFSYVFFKKVR-------------------------PAFEE----IREQEGELNTVLqenLTGvrvvkafaR 196
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1039 EDYfctLIEKaIDYSNKGQKRKTLINSMLWGFSQSAQFFINSFA----YWFGSFLIRRGTIQVDDfmksLFTFLftgSYA 1114
Cdd:cd18542   197 EDY---EIEK-FDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQivlvLWVGGYLVINGEITLGE----LVAFI---SYL 265

                  ....
gi 156095386 1115 GKLM 1118
Cdd:cd18542   266 WMLI 269
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
1356-1388 1.38e-08

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 57.77  E-value: 1.38e-08
                          10        20        30
                  ....*....|....*....|....*....|...
gi 156095386 1356 SLSGGQKQRIAIARALLREPKILLLDEATSSLD 1388
Cdd:PRK10419  151 QLSGGQLQRVCLARALAVEPKLLILDEAVSNLD 183
cbiO PRK13643
energy-coupling factor transporter ATPase;
1164-1415 1.51e-08

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 57.82  E-value: 1.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYlsRPNVPIYK----DLTFSCESKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfkneqtgeSSKEQM 1239
Cdd:PRK13643    2 IKFEKVNYTY--QPNSPFASralfDIDLEVKKGSYTALIGHTGSGKSTLLQHL---------------------NGLLQP 58
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1240 QQGdeEQNVGMKNANEFSSSKEgadgqsstlfknsgkilldgvdicdynLKDLRNLFSIVSQEP--MLFNMSIYENIKFG 1317
Cdd:PRK13643   59 TEG--KVTVGDIVVSSTSKQKE---------------------------IKPVRKKVGVVFQFPesQLFEETVLKDVAFG 109
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1318 KEN--ATREDVKR--ACKFAAI---DEFIESLPNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSN 1390
Cdd:PRK13643  110 PQNfgIPKEKAEKiaAEKLEMVglaDEFWEKSPFE-----------LSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPK 178
                         250       260
                  ....*....|....*....|....*
gi 156095386 1391 SEKLIEKTIVDIKdKADKTIITIAH 1415
Cdd:PRK13643  179 ARIEMMQLFESIH-QSGQTVVLVTH 202
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
383-670 1.55e-08

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 57.89  E-value: 1.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHYDTRKDVEiykDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDSHNLKDVNLKwwRSKI 462
Cdd:PRK13537    8 IDFRNVEKRYGDKLVVD---GLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA--RQRV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  463 GVVSQ-DPLLFSNSIKNNIK-YSLYSlkdlealseesnedGFSSQSdsnsrnsCRAKCAGDLndmiqttdsteliqvrkn 540
Cdd:PRK13537   83 GVVPQfDNLDPDFTVRENLLvFGRYF--------------GLSAAA-------ARALVPPLL------------------ 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  541 yetiedsevvsvskkvlihDFvSALPDKYETLVGsnasKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQK 620
Cdd:PRK13537  124 -------------------EF-AKLENKADAKVG----ELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWE 179
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156095386  621 TINNLKGNENRITII---------IAHRLSTIRYANTI-----FVLSNRENGSTVdVDVLGEDP 670
Cdd:PRK13537  180 RLRSLLARGKTILLTthfmeeaerLCDRLCVIEEGRKIaegapHALIESEIGCDV-IEIYGPDP 242
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
1179-1434 1.56e-08

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 59.35  E-value: 1.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1179 VPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfkneqtgesskeqmqqgdeeqnvgmknanefss 1258
Cdd:PRK10535   21 VEVLKGISLDIYAGEMVAIVGASGSGKSTLMNIL---------------------------------------------- 54
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1259 skeGADGQSStlfknSGKILLDGVDICDYNLKDL----RNLFSIVSQE-PMLFNMSIYENIKF-----GKENATREdvKR 1328
Cdd:PRK10535   55 ---GCLDKPT-----SGTYRVAGQDVATLDADALaqlrREHFGFIFQRyHLLSHLTAAQNVEVpavyaGLERKQRL--LR 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1329 ACKFAA---IDEFIESLPNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDK 1405
Cdd:PRK10535  125 AQELLQrlgLEDRVEYQPSQ-----------LSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDR 193
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 156095386 1406 ADKTIITI--------AHRIASIKrsDKIVVFNNPDR 1434
Cdd:PRK10535  194 GHTVIIVThdpqvaaqAERVIEIR--DGEIVRNPPAQ 228
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
1338-1443 1.75e-08

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: 55.79  E-value: 1.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1338 FIESLPNQYDTNVG--PYGK---SLSGGQKQRIAIARALLREPK--ILLLDEATSSLDSNS-EKLIE--KTIVDIKDkad 1407
Cdd:cd03238    64 FIDQLQFLIDVGLGylTLGQklsTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDiNQLLEviKGLIDLGN--- 140
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 156095386 1408 kTIITIAHRIASIKRSDKIVVFN-NPDRTGSFVQAQG 1443
Cdd:cd03238   141 -TVILIEHNLDVLSSADWIIDFGpGSGKSGGKVVFSG 176
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
1307-1384 1.76e-08

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 58.88  E-value: 1.76e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1307 NMSIYENI---------KFGKENATREDvkrackfAAIDEFIESL----PNQyDTNVGpygkSLSGGQKQRIAIARALLR 1373
Cdd:COG1129   344 DLSIRENItlasldrlsRGGLLDRRRER-------ALAEEYIKRLriktPSP-EQPVG----NLSGGNQQKVVLAKWLAT 411
                          90
                  ....*....|.
gi 156095386 1374 EPKILLLDEAT 1384
Cdd:COG1129   412 DPKVLILDEPT 422
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
1356-1389 1.81e-08

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 56.99  E-value: 1.81e-08
                          10        20        30
                  ....*....|....*....|....*....|....
gi 156095386 1356 SLSGGQKQRIAIARALLREPKILLLDEATSSLDS 1389
Cdd:PRK11247  133 ALSGGQKQRVALARALIHRPGLLLLDEPLGALDA 166
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
1274-1387 1.90e-08

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


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 56.81  E-value: 1.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1274 SGKILLDGVDICDYNL-KDLRNLFSIVSQEPMLFN-MSIYENIKFGKENATREDVKRAckfaaIDEFIESLPNQYDTNVG 1351
Cdd:PRK11614   59 SGRIVFDGKDITDWQTaKIMREAVAIVPEGRRVFSrMTVEENLAMGGFFAERDQFQER-----IKWVYELFPRLHERRIQ 133
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 156095386 1352 PYGkSLSGGQKQRIAIARALLREPKILLLDEATSSL 1387
Cdd:PRK11614  134 RAG-TMSGGEQQMLAIGRALMSQPRLLLLDEPSLGL 168
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
1184-1431 2.29e-08

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 58.56  E-value: 2.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1184 DLTFSCESKKTTAIVGETGSGKS----TVMSLLmrfydlkndhhivfkneqtgESSKEQMQQGDeeqnvgmknanefsss 1259
Cdd:PRK15134   27 DVSLQIEAGETLALVGESGSGKSvtalSILRLL--------------------PSPPVVYPSGD---------------- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1260 kegadgqsstlfknsgkILLDGVDICDYNLKDLR----NLFSIVSQEPM-----LFNM--SIYENIKFGKeNATREdvkr 1328
Cdd:PRK15134   71 -----------------IRFHGESLLHASEQTLRgvrgNKIAMIFQEPMvslnpLHTLekQLYEVLSLHR-GMRRE---- 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1329 ackfAAIDEFIESLP----NQYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKD 1404
Cdd:PRK15134  129 ----AARGEILNCLDrvgiRQAAKRLTDYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQ 204
                         250       260
                  ....*....|....*....|....*...
gi 156095386 1405 KADKTIITIAHRIASIKR-SDKIVVFNN 1431
Cdd:PRK15134  205 ELNMGLLFITHNLSIVRKlADRVAVMQN 232
ABC_6TM_TmrB_like cd18541
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ...
99-307 2.40e-08

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: 57.04  E-value: 2.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   99 IIFSLVLIGIFQFILSFISSFCMDVVTTKILKTLKIEFLKSVFYQDGQFHDNNP-G---SKLTSDLDFyLEQVnAGIGTK 174
Cdd:cd18541    42 YALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLFAHLLTLSPSFYQKNRtGdlmARATNDLNA-VRMA-LGPGIL 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  175 FI--TIFTYASAFlglyIWSLFKNARLTLCITCVFPLIYICGVICNKKV-----KINKKTSLLYNnntmsIIEEALVGIR 247
Cdd:cd18541   120 YLvdALFLGVLVL----VMMFTISPKLTLIALLPLPLLALLVYRLGKKIhkrfrKVQEAFSDLSD-----RVQESFSGIR 190
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 156095386  248 TVVSYCGENTILKKF-NLSEKLYSKyTLKANLMESLHIGMINGFILASYAFGFWYGTRIII 307
Cdd:cd18541   191 VIKAFVQEEAEIERFdKLNEEYVEK-NLRLARVDALFFPLIGLLIGLSFLIVLWYGGRLVI 250
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
387-611 3.19e-08

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: 58.16  E-value: 3.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  387 NVRFHYDTRkDVEIYKDLNFTLTEGKTYAFVGESGCGKS----TILKLIERLYDPTEGDVIINDsHNLKDVNLKWWR--- 459
Cdd:COG4172    13 SVAFGQGGG-TVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDG-QDLLGLSERELRrir 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  460 -SKIGVVSQDPL-----LFSnsIKNNIKYSLySLKdlEALSeesnedgfssqsdsnsRNSCRAKCAgDLndmiqttdste 533
Cdd:COG4172    91 gNRIAMIFQEPMtslnpLHT--IGKQIAEVL-RLH--RGLS----------------GAAARARAL-EL----------- 137
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156095386  534 LIQVRknyetiedsevvsvskkvlihdfvsaLPDKyETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:COG4172   138 LERVG--------------------------IPDP-ERRLDAYPHQLSGGQRQRVMIAMALANEPDLLIADEPTTALD 188
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
392-654 3.31e-08

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 56.73  E-value: 3.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  392 YDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDSHNLKDvNLKWWRSKIGVVSQDP-- 469
Cdd:PRK13652   11 YSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKE-NIREVRKFVGLVFQNPdd 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  470 LLFSNSIKNNIKYSLYSLkdleALSEesnedgfssqsdsnsrnscrakcagdlndmiqttdsteliqvrknyETIEdSEV 549
Cdd:PRK13652   90 QIFSPTVEQDIAFGPINL----GLDE----------------------------------------------ETVA-HRV 118
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  550 VSVSKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNE 629
Cdd:PRK13652  119 SSALHMLGLEELRDRVP-----------HHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETY 187
                         250       260
                  ....*....|....*....|....*.
gi 156095386  630 NRITIIIAHRLSTI-RYANTIFVLSN 654
Cdd:PRK13652  188 GMTVIFSTHQLDLVpEMADYIYVMDK 213
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
1298-1446 3.43e-08

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 57.75  E-value: 3.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1298 IVSQEPMLF-NMSIYENIKFG--KENATREDVKrackfaaidEFIESLPNQYDTNVGpyGKSLSGGQKQRIAIARALLRE 1374
Cdd:PRK15439   90 LVPQEPLLFpNLSVKENILFGlpKRQASMQKMK---------QLLAALGCQLDLDSS--AGSLEVADRQIVEILRGLMRD 158
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156095386 1375 PKILLLDEATSSLD-SNSEKLIEKtIVDIKDKaDKTIITIAHRIASIKR-SDKIVVFnnpdRTGSFVQAQGTHE 1446
Cdd:PRK15439  159 SRILILDEPTASLTpAETERLFSR-IRELLAQ-GVGIVFISHKLPEIRQlADRISVM----RDGTIALSGKTAD 226
ycf16 CHL00131
sulfate ABC transporter protein; Validated
396-638 3.46e-08

sulfate ABC transporter protein; Validated


Pssm-ID: 214372 [Multi-domain]  Cd Length: 252  Bit Score: 56.19  E-value: 3.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  396 KDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLI--ERLYDPTEGDVIINDShNLKDVNLKWwRSKIGVVsqdpLLFS 473
Cdd:CHL00131   18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIagHPAYKILEGDILFKGE-SILDLEPEE-RAHLGIF----LAFQ 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  474 NSIKnnikyslyslkdleaLSEESNEDGFssqsdsnsRNSCRAKcagdlndmiqttdsteliqvRKNYETIEDSEVvsvs 553
Cdd:CHL00131   92 YPIE---------------IPGVSNADFL--------RLAYNSK--------------------RKFQGLPELDPL---- 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  554 kkvlihDFVSALPDKYEtLVGSNASKL--------SGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNL 625
Cdd:CHL00131  125 ------EFLEIINEKLK-LVGMDPSFLsrnvnegfSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKL 197
                         250
                  ....*....|...
gi 156095386  626 KGNENRItIIIAH 638
Cdd:CHL00131  198 MTSENSI-ILITH 209
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
1190-1415 3.90e-08

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 55.56  E-value: 3.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1190 ESKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknEQTGESS--KEQMQQGDEEQNVGMKNANEfssskeGADGQS 1267
Cdd:PRK10584   34 KRGETIALIGESGSGKSTLLAILAGLDD-----------GSSGEVSlvGQPLHQMDEEARAKLRAKHV------GFVFQS 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1268 STLFKNsgkilldgvdicdynLKDLRNLfsivsQEPMLfnmsiyenIKFGKENATREDVKRACKFAAIDEFIESLPNQyd 1347
Cdd:PRK10584   97 FMLIPT---------------LNALENV-----ELPAL--------LRGESSRQSRNGAKALLEQLGLGKRLDHLPAQ-- 146
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156095386 1348 tnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH 1415
Cdd:PRK10584  147 ---------LSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTH 205
3a01203 TIGR00954
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...
403-647 4.07e-08

Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 273360 [Multi-domain]  Cd Length: 659  Bit Score: 57.84  E-value: 4.07e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   403 DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYdPTEGDVIINDShnlkdvnlkwwRSKIGVVSQDPLLFSNSIKNNIKY 482
Cdd:TIGR00954  470 SLSFEVPSGNNLLICGPNGCGKSSLFRILGELW-PVYGGRLTKPA-----------KGKLFYVPQRPYMTLGTLRDQIIY 537
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   483 SLYSlkdlealsEESNEDGFSSQsdsnsrnscrakcagDLNDMIQTTDSTELIQVRKNYETIED-SEVvsvskkvlihdf 561
Cdd:TIGR00954  538 PDSS--------EDMKRRGLSDK---------------DLEQILDNVQLTHILEREGGWSAVQDwMDV------------ 582
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   562 vsalpdkyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEylvQKTINNLKgnENRITII-IAHRL 640
Cdd:TIGR00954  583 ------------------LSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVE---GYMYRLCR--EFGITLFsVSHRK 639

                   ....*..
gi 156095386   641 STIRYAN 647
Cdd:TIGR00954  640 SLWKYHE 646
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
1268-1428 4.51e-08

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: 54.84  E-value: 4.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1268 STLFK----------NSGKILLDGVDICDynlkdlrnlfsivsqepmlfnMSIYENIKFG-----KENATREDVKrackf 1332
Cdd:cd03217    40 STLAKtimghpkyevTEGEILFKGEDITD---------------------LPPEERARLGiflafQYPPEIPGVK----- 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1333 aaIDEFIESLpnqydtNVGpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKaDKTIIT 1412
Cdd:cd03217    94 --NADFLRYV------NEG-----FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREE-GKSVLI 159
                         170
                  ....*....|....*...
gi 156095386 1413 IAH--RIASIKRSDKIVV 1428
Cdd:cd03217   160 ITHyqRLLDYIKPDRVHV 177
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
399-631 5.16e-08

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 55.59  E-value: 5.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  399 EIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDShnlkdvnlkwwrskigvvsqdPLlfsNSIKN 478
Cdd:PRK11629   23 DVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQ---------------------PM---SKLSS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  479 NIKYSLyslkdlealseESNEDGFSSQ-----SDSNSrnscrakcagdlndmIQTTDSTELIQVRKNYETIEDSevvsvs 553
Cdd:PRK11629   79 AAKAEL-----------RNQKLGFIYQfhhllPDFTA---------------LENVAMPLLIGKKKPAEINSRA------ 126
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156095386  554 kkvliHDFVSALpdKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSeylvQKTINNLKGNENR 631
Cdd:PRK11629  127 -----LEMLAAV--GLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARN----ADSIFQLLGELNR 193
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
1268-1436 5.46e-08

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 55.27  E-value: 5.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1268 STLFK--------NSGKILLDGVDICDYNLKDL----RNLFSIVSQEPMLFNMSIYENIKFGK--ENATREDVKRACKfA 1333
Cdd:PRK10908   42 STLLKlicgierpSAGKIWFSGHDITRLKNREVpflrRQIGMIFQDHHLLMDRTVYDNVAIPLiiAGASGDDIRRRVS-A 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1334 AIDEF-----IESLPNQydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIkDKADK 1408
Cdd:PRK10908  121 ALDKVglldkAKNFPIQ-----------LSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEF-NRVGV 188
                         170       180
                  ....*....|....*....|....*....
gi 156095386 1409 TIITIAHRIASI-KRSDKIVVFNNPDRTG 1436
Cdd:PRK10908  189 TVLMATHDIGLIsRRSYRMLTLSDGHLHG 217
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
1353-1433 6.03e-08

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: 57.12  E-value: 6.03e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1353 YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRI---------ASIKRS 1423
Cdd:TIGR03269  424 YPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMdfvldvcdrAALMRD 503
                           90
                   ....*....|
gi 156095386  1424 DKIVVFNNPD 1433
Cdd:TIGR03269  504 GKIVKIGDPE 513
ABC_6TM_ABCB8_like cd18574
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ...
890-1101 6.34e-08

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: 56.01  E-value: 6.34e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  890 VIGEKVEKTMKLRLFENIMYQEISFFDQdsHAPGLLSAHINRDVHLLKT--------GLVNNIVIFTHFIVLFLVSTVMS 961
Cdd:cd18574    68 VVGERVAARLRNDLFSSLLRQDIAFFDT--HRTGELVNRLTADVQEFKSsfkqcvsqGLRSVTQTVGCVVSLYLISPKLT 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  962 FYFCPIV-AAVLTGTYF-IFMRVFAIRAriaankdveKKRVNQP-GTAFvynsddeifkdpsfliqEAFYNMNTVIIYGL 1038
Cdd:cd18574   146 LLLLVIVpVVVLVGTLYgSFLRKLSRRA---------QAQVAKAtGVAD-----------------EALGNIRTVRAFAM 199
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1039 EDYFCTLiekaidYSNKGQKRKTLiNSML---WGFSQS-AQFFINSFA---YWFGSFLIRRGTIQVDDFM 1101
Cdd:cd18574   200 EDRELEL------YEEEVEKAAKL-NEKLglgIGIFQGlSNLALNGIVlgvLYYGGSLVSRGELTAGDLM 262
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
400-654 8.41e-08

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 55.02  E-value: 8.41e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDshnlkdvnlkwwrskigvvsqdpllfsnsiknn 479
Cdd:PRK11231   17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGD--------------------------------- 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  480 ikyslyslKDLEALSeesnedgfssqsdsnSRNSCRAkcagdLNDMIQTTDSTELIQVRKNYE-------------TIED 546
Cdd:PRK11231   64 --------KPISMLS---------------SRQLARR-----LALLPQHHLTPEGITVRELVAygrspwlslwgrlSAED 115
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  547 SEVVSVSkkvlIHDF-VSALPDKyetlvgsNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNL 625
Cdd:PRK11231  116 NARVNQA----MEQTrINHLADR-------RLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMREL 184
                         250       260       270
                  ....*....|....*....|....*....|
gi 156095386  626 KgNENRITIIIAHRLS-TIRYANTIFVLSN 654
Cdd:PRK11231  185 N-TQGKTVVTVLHDLNqASRYCDHLVVLAN 213
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
1274-1418 9.12e-08

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 56.57  E-value: 9.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1274 SGKILLDGVDICDYNLKDLRNL-FSIVSQEPMLF----NMSIYENIKFGkenatREDVKRACK-----FAAIDEFIESLP 1343
Cdd:COG3845   312 SGSIRLDGEDITGLSPRERRRLgVAYIPEDRLGRglvpDMSVAENLILG-----RYRRPPFSRggfldRKAIRAFAEELI 386
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1344 NQYD---TNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDK--------AD-KTII 1411
Cdd:COG3845   387 EEFDvrtPGPDTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAgaavllisEDlDEIL 466

                  ....*..
gi 156095386 1412 TIAHRIA 1418
Cdd:COG3845   467 ALSDRIA 473
GguA NF040905
sugar ABC transporter ATP-binding protein;
403-673 1.02e-07

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 56.34  E-value: 1.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  403 DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYdPT---EGDVI----------INDSHnlkdvnlkwwRSKIGVVSQD- 468
Cdd:NF040905   19 DVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILfdgevcrfkdIRDSE----------ALGIVIIHQEl 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  469 ---PLLfsnSIKNNIkyslyslkdleALSEESNEDGFSSQSDSNSRnscrakcagdlndmiqttdSTELIqvrknyetie 545
Cdd:NF040905   88 aliPYL---SIAENI-----------FLGNERAKRGVIDWNETNRR-------------------ARELL---------- 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  546 dsevvsvsKKVlihdfvsALPDKYETLVgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSL-DNKSEYLVQkTINN 624
Cdd:NF040905  125 --------AKV-------GLDESPDTLV----TDIGVGKQQLVEIAKALSKDVKLLILDEPTAALnEEDSAALLD-LLLE 184
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 156095386  625 LKgnENRIT-IIIAHRLSTIRY-ANTIFVLsnrENGSTVD-VDVLGEDPTKD 673
Cdd:NF040905  185 LK--AQGITsIIISHKLNEIRRvADSITVL---RDGRTIEtLDCRADEVTED 231
ABC_6TM_bac_exporter_ABCB8_10_like cd18575
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ...
826-1114 1.25e-07

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: 54.80  E-value: 1.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  826 AIIALsIMVAGGLyplFALLYAkyVGTLFDFANLEANS---NKYSLYILVIAIAMFISETLKNYYNNVIGEKVekTMKLR 902
Cdd:cd18575     1 ALIAL-LIAAAAT---LALGQG--LRLLIDQGFAAGNTallNRAFLLLLAVALVLALASALRFYLVSWLGERV--VADLR 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  903 --LFENIMYQEISFFDqdSHAPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSTVMSFYFCP--------IVAAVL 972
Cdd:cd18575    73 kaVFAHLLRLSPSFFE--TTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPkltllvllVIPLVV 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  973 tgtyfIFMRVFAIRARIAAnkdvekkRVNQPGTAfvynsddeifkDPSFLIQEAFYNMNTVIIYGLEDY----FCTLIEK 1048
Cdd:cd18575   151 -----LPIILFGRRVRRLS-------RASQDRLA-----------DLSAFAEETLSAIKTVQAFTREDAerqrFATAVEA 207
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156095386 1049 AIDYSnkgqKRKTLINSMLWGFSQSAQFFINSFAYWFGSFLIRRGTIQVDDfmksLFTFLFtgsYA 1114
Cdd:cd18575   208 AFAAA----LRRIRARALLTALVIFLVFGAIVFVLWLGAHDVLAGRMSAGE----LSQFVF---YA 262
ABC_6TM_TAP cd18572
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ...
829-1109 1.27e-07

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: 54.86  E-value: 1.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  829 ALSIMVaggLYPLFALLYAKYVGTLFDFANLEANSNK--YSLYILVIAIAMF-ISETLKNYYNNVIGEKVEKTMKLRLFE 905
Cdd:cd18572     1 AFVFLV---VAALSELAIPHYTGAVIDAVVADGSREAfyRAVLLLLLLSVLSgLFSGLRGGCFSYAGTRLVRRLRRDLFR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  906 NIMYQEISFFDQdsHAPGLLSAHINRDV--------HLLKTGLVNNIVIFTHFIVLFLVS---TVMSFYFCPIVAAVlTG 974
Cdd:cd18572    78 SLLRQDIAFFDA--TKTGELTSRLTSDCqkvsdplsTNLNVFLRNLVQLVGGLAFMFSLSwrlTLLAFITVPVIALI-TK 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  975 TYFIFMRVFA--IRARIA-ANKDVEkkrvnqpgtafvynsddeifkdpsfliqEAFYNMNTVIIYGLEDYFCTLIEKAID 1051
Cdd:cd18572   155 VYGRYYRKLSkeIQDALAeANQVAE----------------------------EALSNIRTVRSFATEEREARRYERALD 206
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 156095386 1052 -YSNKGQKRKTLINSMLWgFSQSAQFFINSFAYWFGSFLIRRGTIQVDdfmkSLFTFLF 1109
Cdd:cd18572   207 kALKLSVRQALAYAGYVA-VNTLLQNGTQVLVLFYGGHLVLSGRMSAG----QLVTFML 260
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
390-656 1.29e-07

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 54.63  E-value: 1.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  390 FHYdtrKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIIN-DSHNLKDVNLKWWRSKIGVVSQD 468
Cdd:PRK13638    9 FRY---QDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQgKPLDYSKRGLLALRQQVATVFQD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  469 P--LLFSNSIKNNIKYSLYSLKDLEalseesnedgfssqsdsnsrnscrAKCAGDLNDMIQTTDSTELIQvrknyETIEd 546
Cdd:PRK13638   86 PeqQIFYTDIDSDIAFSLRNLGVPE------------------------AEITRRVDEALTLVDAQHFRH-----QPIQ- 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  547 sevvsvskkvlihdfvsalpdkyetlvgsnasKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLK 626
Cdd:PRK13638  136 --------------------------------CLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIV 183
                         250       260       270
                  ....*....|....*....|....*....|.
gi 156095386  627 GNENRItIIIAHRLSTI-RYANTIFVLSNRE 656
Cdd:PRK13638  184 AQGNHV-IISSHDIDLIyEISDAVYVLRQGQ 213
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
569-649 1.36e-07

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: 53.10  E-value: 1.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  569 YETLvGSNASKLSGGQKQRISIARAIIRNPK--ILILDEATSSLDNKSEYLVQKTINNLKGNENRItIIIAHRLSTIRYA 646
Cdd:cd03238    78 YLTL-GQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTV-ILIEHNLDVLSSA 155

                  ...
gi 156095386  647 NTI 649
Cdd:cd03238   156 DWI 158
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
1353-1430 1.39e-07

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 56.02  E-value: 1.39e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 156095386 1353 YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVVFN 1430
Cdd:PRK10261  460 YPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERiSHRVAVMY 538
SufC COG0396
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ...
397-638 1.41e-07

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


Pssm-ID: 440165 [Multi-domain]  Cd Length: 245  Bit Score: 54.30  E-value: 1.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  397 DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLI---ERlYDPTEGDVIindshnLKDVNLKWW----RSK--IGVVSQ 467
Cdd:COG0396    12 GKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmghPK-YEVTSGSIL------LDGEDILELspdeRARagIFLAFQ 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  468 DPLlfsnSIKNnikyslYSLKDLeaLSEESNEDGFSSQSDSNSRNSCRAKCAgDLN---DMIqttdsteliqvrknyeti 544
Cdd:COG0396    85 YPV----EIPG------VSVSNF--LRTALNARRGEELSAREFLKLLKEKMK-ELGldeDFL------------------ 133
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  545 eDSEVvsvskkvlihdfvsalpdkyetlvgsNASkLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINN 624
Cdd:COG0396   134 -DRYV--------------------------NEG-FSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNK 185
                         250
                  ....*....|....
gi 156095386  625 LKgNENRITIIIAH 638
Cdd:COG0396   186 LR-SPDRGILIITH 198
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
571-641 1.48e-07

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


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 56.21  E-value: 1.48e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 156095386   571 TLVGSNASK--LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLkGNENRITIIIAHRLS 641
Cdd:TIGR00955  156 TRIGVPGRVkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGL-AQKGKTIICTIHQPS 227
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
1181-1388 1.52e-07

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 54.05  E-value: 1.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1181 IYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFyDLKNDHHIVFKNEQTgesskeqmqqgdeeqnvgmknaNEFSSSK 1260
Cdd:PRK11629   24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGL-DTPTSGDVIFNGQPM----------------------SKLSSAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1261 EGadgqsstlfknsgkilldgvdicdynlkDLRN--LFSIVSQEPMLFNMSIYENIKF----GKENATREDVKRACKFAA 1334
Cdd:PRK11629   81 KA----------------------------ELRNqkLGFIYQFHHLLPDFTALENVAMplliGKKKPAEINSRALEMLAA 132
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 156095386 1335 IDefIESLPNQYDTnvgpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLD 1388
Cdd:PRK11629  133 VG--LEHRANHRPS-------ELSGGERQRVAIARALVNNPRLVLADEPTGNLD 177
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
580-654 1.73e-07

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: 53.30  E-value: 1.73e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156095386  580 LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgNENRITIIIAHRLSTIRY--ANTIFVLSN 654
Cdd:cd03217   105 FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLR-EEGKSVLIITHYQRLLDYikPDRVHVLYD 180
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
1357-1417 1.76e-07

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 53.94  E-value: 1.76e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 156095386 1357 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRI 1417
Cdd:PRK11248  129 LSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDI 189
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
415-641 1.78e-07

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 54.33  E-value: 1.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  415 AFVGESGCGKSTILKLIERLYDPTEG-----DVIINDSHNLKDVNLKWWRSKIGVVSQDPLLFSNSIKNNIKYSLYSLKd 489
Cdd:PRK14271   51 SLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRDVLEFRRRVGMLFQRPNPFPMSIMDNVLAGVRAHK- 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  490 lealseesnedgfssqsdsnsrnscrakcagdlndmiqttdstelIQVRKNYETIEDSEVVSVSKKVLIHDFVSALPdky 569
Cdd:PRK14271  130 ---------------------------------------------LVPRKEFRGVAQARLTEVGLWDAVKDRLSDSP--- 161
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 156095386  570 etlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgneNRIT-IIIAHRLS 641
Cdd:PRK14271  162 --------FRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLA---DRLTvIIVTHNLA 223
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
1176-1399 1.80e-07

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 53.34  E-value: 1.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1176 RPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFydLKNDH-HIVFKNEQTGESS-KEQMQQgdeeqnVGMKNA 1253
Cdd:PRK13539   12 RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGL--LPPAAgTIKLDGGDIDDPDvAEACHY------LGHRNA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1254 nefssskegadgqsstlfknsgkilldgvdicdynLKDlrnlfsivsqepmlfNMSIYENIKFGKE--NATREDVKRACK 1331
Cdd:PRK13539   84 -----------------------------------MKP---------------ALTVAENLEFWAAflGGEELDIAAALE 113
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156095386 1332 FAAIDEfIESLPNQYdtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTI 1399
Cdd:PRK13539  114 AVGLAP-LAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELI 170
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
403-669 1.90e-07

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 55.32  E-value: 1.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  403 DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYdPT---EGDVIINDS----HNLKDVNlkwwRSKIGVVSQDPLLFSN- 474
Cdd:PRK13549   23 NVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEelqaSNIRDTE----RAGIAIIHQELALVKEl 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  475 SIKNNIkyslyslkdleALSEESNEDGFSsqsdsnsrnscrakcagDLNDMIQTTDsTELIQVRKNyetiedsevVSVSK 554
Cdd:PRK13549   98 SVLENI-----------FLGNEITPGGIM-----------------DYDAMYLRAQ-KLLAQLKLD---------INPAT 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  555 KVlihdfvsalpdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgNENRITI 634
Cdd:PRK13549  140 PV---------------------GNLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLK-AHGIACI 197
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 156095386  635 IIAHRLSTI-RYANTIFVLSNRENGSTVDVDVLGED 669
Cdd:PRK13549  198 YISHKLNEVkAISDTICVIRDGRHIGTRPAAGMTED 233
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
1268-1449 2.34e-07

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 54.02  E-value: 2.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1268 STLFK--------NSGKILLDGVDICDYNLKDL-RNLFSIVSQEPMLFNMSIYENI------------KFGKENatREDV 1326
Cdd:PRK10575   51 STLLKmlgrhqppSEGEILLDAQPLESWSSKAFaRKVAYLPQQLPAAEGMTVRELVaigrypwhgalgRFGAAD--REKV 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1327 KRACKFAAIDEFIESLPNqydtnvgpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKA 1406
Cdd:PRK10575  129 EEAISLVGLKPLAHRLVD-----------SLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQER 197
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 156095386 1407 DKTIITIAHRIASIKR-SDKIVVFnnpdRTGSFVqAQGTHEELL 1449
Cdd:PRK10575  198 GLTVIAVLHDINMAARyCDYLVAL----RGGEMI-AQGTPAELM 236
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
400-652 2.46e-07

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 53.84  E-value: 2.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIInDSHNLKDVNLKWWRSKIGVVSQDPllfsnSIKNN 479
Cdd:PRK10253   22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWL-DGEHIQHYASKEVARRIGLLAQNA-----TTPGD 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  480 IkyslySLKDLEALSEESNEDGFSsqsdsnsrnscrakcagdlndmiqttdsteliQVRKnyetiEDSEVVSVSKKvlih 559
Cdd:PRK10253   96 I-----TVQELVARGRYPHQPLFT--------------------------------RWRK-----EDEEAVTKAMQ---- 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  560 dfVSALPDkyetLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHR 639
Cdd:PRK10253  130 --ATGITH----LADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHD 203
                         250
                  ....*....|....
gi 156095386  640 LS-TIRYANTIFVL 652
Cdd:PRK10253  204 LNqACRYASHLIAL 217
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
570-655 2.68e-07

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: 51.61  E-value: 2.68e-07
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386    570 ETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTIN-----NLKGNENRITIIIAHRLSTIR 644
Cdd:smart00382   51 LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrlllLLKSEKNLTVILTTNDEKDLG 130
                            90
                    ....*....|.
gi 156095386    645 YANTIFVLSNR 655
Cdd:smart00382  131 PALLRRRFDRR 141
SapD COG4170
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
405-652 3.23e-07

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


Pssm-ID: 443330 [Multi-domain]  Cd Length: 331  Bit Score: 54.14  E-value: 3.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  405 NFTLTEGKTYAFVGESGCGKSTILKLIERLYDPtegDVIIN-DSHNLKDVNL---------KWWRSKIGVVSQDPLLF-- 472
Cdd:COG4170    27 SLTLNEGEIRGLVGESGSGKSLIAKAICGITKD---NWHVTaDRFRWNGIDLlklsprerrKIIGREIAMIFQEPSSCld 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  473 -SNSIKNNIKyslyslkdlEALSEESNEDGFSSqsdsnsrnscRAkcagdlndmiqttdsteliQVRKNYetiedseVVS 551
Cdd:COG4170   104 pSAKIGDQLI---------EAIPSWTFKGKWWQ----------RF-------------------KWRKKR-------AIE 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  552 VSKKVLIHDfvsalpdkYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLkgNENR 631
Cdd:COG4170   139 LLHRVGIKD--------HKDIMNSYPHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARL--NQLQ 208
                         250       260
                  ....*....|....*....|....
gi 156095386  632 ITII--IAHRLSTI-RYANTIFVL 652
Cdd:COG4170   209 GTSIllISHDLESIsQWADTITVL 232
urea_trans_UrtE TIGR03410
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ...
580-635 3.27e-07

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: 52.91  E-value: 3.27e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 156095386   580 LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgNENRITII 635
Cdd:TIGR03410  132 LSGGQQQQLAIARALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLR-AEGGMAIL 186
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
1164-1453 3.32e-07

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 53.62  E-value: 3.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFrylSRPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfkneqtgesskeqmqqgd 1243
Cdd:PRK11831    8 VDMRGVSF---TRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLI------------------------------- 53
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 eeqnvgmknanefssskegaDGQsstLFKNSGKILLDGVDI---CDYNLKDLRNLFSIVSQEPMLF-NMSIYENIKFGKE 1319
Cdd:PRK11831   54 --------------------GGQ---IAPDHGEILFDGENIpamSRSRLYTVRKRMSMLFQSGALFtDMNVFDNVAYPLR 110
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1320 NATR--EDVKRACKFAAidefIESLPNQYDTNVGPygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEK 1397
Cdd:PRK11831  111 EHTQlpAPLLHSTVMMK----LEAVGLRGAAKLMP--SELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVK 184
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 156095386 1398 TIVDIKDKADKTIITIAH---RIASIKRSDKIVvfnnpdrTGSFVQAQGTHEELLSVQD 1453
Cdd:PRK11831  185 LISELNSALGVTCVVVSHdvpEVLSIADHAYIV-------ADKKIVAHGSAQALQANPD 236
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
1355-1430 3.53e-07

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: 53.11  E-value: 3.53e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156095386 1355 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVVFN 1430
Cdd:cd03267   152 RQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEAlARRVLVID 228
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
1268-1454 4.31e-07

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 54.41  E-value: 4.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1268 STLFK--------NSGKILLDGVDICDYNLKDLRNL-FSIVSQEPMLFN-MSIYENIKFGKeNATRE-------DVKRAC 1330
Cdd:PRK09700   45 STLMKvlsgihepTKGTITINNINYNKLDHKLAAQLgIGIIYQELSVIDeLTVLENLYIGR-HLTKKvcgvniiDWREMR 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1331 KFAAIDEFIESLPNQYDTNVGpygkSLSGGQKQRIAIARALLREPKILLLDEATSSL-DSNSEKLIekTIVDIKDKADKT 1409
Cdd:PRK09700  124 VRAAMMLLRVGLKVDLDEKVA----NLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLtNKEVDYLF--LIMNQLRKEGTA 197
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 156095386 1410 IITIAHRIASIKR-SDKIVVFNNPDRTGSFVQAQGTHEELLSVQDG 1454
Cdd:PRK09700  198 IVYISHKLAEIRRiCDRYTVMKDGSSVCSGMVSDVSNDDIVRLMVG 243
PTZ00243 PTZ00243
ABC transporter; Provisional
385-654 4.76e-07

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 54.78  E-value: 4.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  385 FKNVRFHYdtRKDVE-IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINdSHNLKDVNLKWWRSKIG 463
Cdd:PTZ00243 1311 FEGVQMRY--REGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVN-GREIGAYGLRELRRQFS 1387
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  464 VVSQDPLLFSNSIKNNIkyslyslkD--LEALSEEsnedgfssqsdsnsrnscrakcagdlndmiqTTDSTELIQVRKny 541
Cdd:PTZ00243 1388 MIPQDPVLFDGTVRQNV--------DpfLEASSAE-------------------------------VWAALELVGLRE-- 1426
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  542 etiedsEVVSVSKKVlihdfvsalpdkyETLVGSNASKLSGGQKQRISIARAIIRNPKILIL-DEATSSLDNKSEYLVQK 620
Cdd:PTZ00243 1427 ------RVASESEGI-------------DSRVLEGGSNYSVGQRQLMCMARALLKKGSGFILmDEATANIDPALDRQIQA 1487
                         250       260       270
                  ....*....|....*....|....*....|....
gi 156095386  621 TINNLKGNENRITiiIAHRLSTIRYANTIFVLSN 654
Cdd:PTZ00243 1488 TVMSAFSAYTVIT--IAHRLHTVAQYDKIIVMDH 1519
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
411-614 4.85e-07

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 52.47  E-value: 4.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  411 GKTYAFVGESGCGKSTILKLIERLYDPTEGDVII--NDSHNLKDVNLKWWRSK-IGVVSQDPLLFS--NSIKNnikysly 485
Cdd:PRK10584   36 GETIALIGESGSGKSTLLAILAGLDDGSSGEVSLvgQPLHQMDEEARAKLRAKhVGFVFQSFMLIPtlNALEN------- 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  486 slKDLEALseesnedgFSSQSDSNSRNSCRakcagdlndmiqttdstELIqvrknyetiedsEVVSVSKKvLIHdfvsaL 565
Cdd:PRK10584  109 --VELPAL--------LRGESSRQSRNGAK-----------------ALL------------EQLGLGKR-LDH-----L 143
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 156095386  566 PdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS 614
Cdd:PRK10584  144 P-----------AQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQT 181
PRK10522 PRK10522
multidrug transporter membrane component/ATP-binding component; Provisional
377-473 5.23e-07

multidrug transporter membrane component/ATP-binding component; Provisional


Pssm-ID: 236707 [Multi-domain]  Cd Length: 547  Bit Score: 54.21  E-value: 5.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  377 LKDIKKIQFKNVRFHYDTRK-DVeiyKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIInDSHNLKDVNL 455
Cdd:PRK10522  317 FPDWQTLELRNVTFAYQDNGfSV---GPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILL-DGKPVTAEQP 392
                          90
                  ....*....|....*...
gi 156095386  456 KWWRSKIGVVSQDPLLFS 473
Cdd:PRK10522  393 EDYRKLFSAVFTDFHLFD 410
ABC_6TM_TmrB_like cd18541
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ...
825-1100 5.94e-07

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: 52.80  E-value: 5.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  825 IAIIALsIMVAgglypLFALLYAKYVGTLFD-FANLEANSN---KYSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMK 900
Cdd:cd18541     3 LGILFL-ILVD-----LLQLLIPRIIGRAIDaLTAGTLTASqllRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLR 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  901 LRLFENIMYQEISFFDQdsHAPGLLSAHINRDVHLLK--TG-----LVNNIVIFThFIVLFLVS-----TVMSFYFCPIV 968
Cdd:cd18541    77 NDLFAHLLTLSPSFYQK--NRTGDLMARATNDLNAVRmaLGpgilyLVDALFLGV-LVLVMMFTispklTLIALLPLPLL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  969 AAVLtgtyFIFMRVfaIRARIaankdvekkRVNQpgtafvynsddEIFKDPSFLIQEAFYNMNTVIIYGLEDYFCTLIEK 1048
Cdd:cd18541   154 ALLV----YRLGKK--IHKRF---------RKVQ-----------EAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDK 207
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 156095386 1049 AidysNKGQKRKTLINSMLWGFSQSAQFFINSFAY----WFGSFLIRRGTIQVDDF 1100
Cdd:cd18541   208 L----NEEYVEKNLRLARVDALFFPLIGLLIGLSFlivlWYGGRLVIRGTITLGDL 259
GguA NF040905
sugar ABC transporter ATP-binding protein;
1177-1428 5.96e-07

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 54.03  E-value: 5.96e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1177 PNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYdlkndhhivfkneqtgesskeqmQQGDEEqnvgmknanef 1256
Cdd:NF040905   12 PGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-----------------------PHGSYE----------- 57
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1257 ssskegadgqsstlfknsGKILLDGvDICDYnlKDLRNlfS------IVSQE----PMLfnmSIYENIKFGKENATR--- 1323
Cdd:NF040905   58 ------------------GEILFDG-EVCRF--KDIRD--SealgivIIHQElaliPYL---SIAENIFLGNERAKRgvi 111
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1324 ---EDVKRACKFAAIDEFIESlPnqyDTNVgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSL-DSNSEKLIEkTI 1399
Cdd:NF040905  112 dwnETNRRARELLAKVGLDES-P---DTLV----TDIGVGKQQLVEIAKALSKDVKLLILDEPTAALnEEDSAALLD-LL 182
                         250       260       270
                  ....*....|....*....|....*....|
gi 156095386 1400 VDIKDKADKTIItIAHRIASIKR-SDKIVV 1428
Cdd:NF040905  183 LELKAQGITSII-ISHKLNEIRRvADSITV 211
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
1347-1415 6.04e-07

ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.


Pssm-ID: 274744 [Multi-domain]  Cd Length: 552  Bit Score: 53.79  E-value: 6.04e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 156095386  1347 DTNVGpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkadkTIITIAH 1415
Cdd:TIGR03719  156 DADVT----KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPG----TVVAVTH 216
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
1333-1428 6.36e-07

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 53.30  E-value: 6.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1333 AAIDEFIE--SLPNQYDTNVGpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTI 1410
Cdd:PRK13536  151 AVIPSLLEfaRLESKADARVS----DLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARG-KTI 225
                          90
                  ....*....|....*....
gi 156095386 1411 ITIAHRIASIKR-SDKIVV 1428
Cdd:PRK13536  226 LLTTHFMEEAERlCDRLCV 244
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
1262-1450 6.64e-07

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 52.70  E-value: 6.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1262 GADG-QSSTLFKN--------SGKILLDG--VDICDYNLKDLRNLFSIVSQEP--MLFNMSIYENIKFGKEN---ATRED 1325
Cdd:PRK13638   34 GANGcGKSTLFMNlsgllrpqKGAVLWQGkpLDYSKRGLLALRQQVATVFQDPeqQIFYTDIDSDIAFSLRNlgvPEAEI 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1326 VKRackfaaIDEFIESLPNQYDTNvGPYgKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDK 1405
Cdd:PRK13638  114 TRR------VDEALTLVDAQHFRH-QPI-QCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQ 185
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 156095386 1406 ADKTIITiAHRIASIKR-SDKIVVFnnpdRTGSfVQAQGTHEELLS 1450
Cdd:PRK13638  186 GNHVIIS-SHDIDLIYEiSDAVYVL----RQGQ-ILTHGAPGEVFA 225
ABC_6TM_T1SS_like cd18555
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ...
825-1095 6.80e-07

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: 52.90  E-value: 6.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  825 IAIIALSIMVAgglypLFALLYAKYVGTLFDFANLEANSNKYSLYILVIAIAM---FISETLKNYYNNVIGEKVEKTMKL 901
Cdd:cd18555     5 ISILLLSLLLQ-----LLTLLIPILTQYVIDNVIVPGNLNLLNVLGIGILILFllyGLFSFLRGYIIIKLQTKLDKSLMS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  902 RLFENIMYQEISFFDQDShaPGLLSAHINRDVHL-------LKTGLVNNIVIFTHFIVLFLVSTVMSFYfcpivaaVLTG 974
Cdd:cd18555    80 DFFEHLLKLPYSFFENRS--SGDLLFRANSNVYIrqilsnqVISLIIDLLLLVIYLIYMLYYSPLLTLI-------VLLL 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  975 TYFIFMRVFAIRARIaankdvekKRVNQpgTAFVYNSddeifKDPSFLIqEAFYNMNTVIIYGLEDYFCT----LIEKAI 1050
Cdd:cd18555   151 GLLIVLLLLLTRKKI--------KKLNQ--EEIVAQT-----KVQSYLT-ETLYGIETIKSLGSEKNIYKkwenLFKKQL 214
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 156095386 1051 DYSnkgqKRKTLINSMLWGFSQSAQFFINSFAYWFGSFLIRRGTI 1095
Cdd:cd18555   215 KAF----KKKERLSNILNSISSSIQFIAPLLILWIGAYLVINGEL 255
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
580-652 6.85e-07

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 51.47  E-value: 6.85e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 156095386  580 LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGnENRITIIIAHRLSTIRYANTIFVL 652
Cdd:NF040873  120 LSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHA-RGATVVVVTHDLELVRRADPCVLL 191
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
1307-1454 6.92e-07

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 52.89  E-value: 6.92e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1307 NMSIYENIK-----FGKENAT-REDVKRACKFAaidefieSLPNQYDTNVGpygkSLSGGQKQRIAIARALLREPKILLL 1380
Cdd:PRK13537   94 DFTVRENLLvfgryFGLSAAAaRALVPPLLEFA-------KLENKADAKVG----ELSGGMKRRLTLARALVNDPDVLVL 162
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156095386 1381 DEATSSLDSNSEKLIEKTIVDIKdKADKTIITIAHRIASIKR-SDKIVVFNNPDRTgsfvqAQGTHEELLSVQDG 1454
Cdd:PRK13537  163 DEPTTGLDPQARHLMWERLRSLL-ARGKTILLTTHFMEEAERlCDRLCVIEEGRKI-----AEGAPHALIESEIG 231
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...
403-652 7.11e-07

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: 52.35  E-value: 7.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  403 DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDshnlKDVN-LK-WWRSKIGVVS--QDPLLFSN-SIK 477
Cdd:COG0411    22 DVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDG----RDITgLPpHRIARLGIARtfQNPRLFPElTVL 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  478 NNIKYSLYSlkdleALSEESNEDGFSSQSDSNSRNSCRAKCAgdlndmiqttdstELIqvrknyetiedsevvsvskkvl 557
Cdd:COG0411    98 ENVLVAAHA-----RLGRGLLAALLRLPRARREEREARERAE-------------ELL---------------------- 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  558 ihDFVSaLPDKYETLVGSnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNK-SEYLVQkTINNLKGNENrITI-I 635
Cdd:COG0411   138 --ERVG-LADRADEPAGN----LSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEeTEELAE-LIRRLRDERG-ITIlL 208
                         250
                  ....*....|....*...
gi 156095386  636 IAHRLSTI-RYANTIFVL 652
Cdd:COG0411   209 IEHDMDLVmGLADRIVVL 226
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
386-607 7.20e-07

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: 51.91  E-value: 7.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  386 KNVRFHYDtrkDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDshnlKDV-NLKWW---RSK 461
Cdd:COG0410     7 ENLHAGYG---GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDG----EDItGLPPHriaRLG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  462 IGVVSQDPLLFSN-SIKNNIKYSLYSLKDLEALSEesnedgfssqsdsnsrnscrakcagdlndmiqttdsteliqvrkn 540
Cdd:COG0410    80 IGYVPEGRRIFPSlTVEENLLLGAYARRDRAEVRA--------------------------------------------- 114
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156095386  541 yeTIEDsevvsvskkvlIHDFVSALPDKYETLVGSnaskLSGGQKQRISIARAIIRNPKILILDEAT 607
Cdd:COG0410   115 --DLER-----------VYELFPRLKERRRQRAGT----LSGGEQQMLAIGRALMSRPKLLLLDEPS 164
ABC_6TM_TmrA_like cd18544
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ...
825-1117 7.21e-07

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: 52.78  E-value: 7.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  825 IAIIALSIMVAGGLYPLFALLYA--KY-VGTLFDFANLeansNKYSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMKL 901
Cdd:cd18544     3 LALLLLLLATALELLGPLLIKRAidDYiVPGQGDLQGL----LLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  902 RLFENIMYQEISFFDQdsHAPGLLSAHINRDVHLLKTGLVNNIV-IFTHFIVLFLVSTVMsFYFCPIVAAVLTGT---YF 977
Cdd:cd18544    79 DLFSHIQRLPLSFFDR--TPVGRLVTRVTNDTEALNELFTSGLVtLIGDLLLLIGILIAM-FLLNWRLALISLLVlplLL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  978 IFMRVFAIRARiAANKDVEKK--RVNqpgtAFvynsddeifkdpsflIQEAFYNMNTVIIYGLEDYFctliEKAIDYSNK 1055
Cdd:cd18544   156 LATYLFRKKSR-KAYREVREKlsRLN----AF---------------LQESISGMSVIQLFNREKRE----FEEFDEINQ 211
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156095386 1056 GQKRKTLINSMLWGFSQSAQFFINSFAY----WFGSFLIRRGTIQVDdfmkSLFTFLftgSYAGKL 1117
Cdd:cd18544   212 EYRKANLKSIKLFALFRPLVELLSSLALalvlWYGGGQVLSGAVTLG----VLYAFI---QYIQRF 270
PLN03073 PLN03073
ABC transporter F family; Provisional
1355-1415 7.61e-07

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 53.71  E-value: 7.61e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 156095386 1355 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVdikdKADKTIITIAH 1415
Cdd:PLN03073  343 KTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLL----KWPKTFIVVSH 399
TauB COG4525
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
383-611 8.71e-07

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


Pssm-ID: 443596 [Multi-domain]  Cd Length: 262  Bit Score: 52.17  E-value: 8.71e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHYD-TRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDshnlkdVNLKWWRSK 461
Cdd:COG4525     4 LTVRHVSVRYPgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDG------VPVTGPGAD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  462 IGVVSQ-DPLLFSNSIKNNIKYSLySLKDLealseesnedgfssqsdsnSRNSCRAKCAgdlndmiqttdstELIQvrkn 540
Cdd:COG4525    78 RGVVFQkDALLPWLNVLDNVAFGL-RLRGV-------------------PKAERRARAE-------------ELLA---- 120
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 156095386  541 yetiedsevvsvskKVLIHDFVSALPdkYEtlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:COG4525   121 --------------LVGLADFARRRI--WQ---------LSGGMRQRVGIARALAADPRFLLMDEPFGALD 166
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
1193-1439 9.48e-07

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 53.08  E-value: 9.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1193 KTTAIVGETGSGKSTVMSLLMRFYDlKNDHHIVFKNEQTgesskeqmqqgdeeqnvgmknanEFSSSKegaDGQSSTLfk 1272
Cdd:PRK10762   31 RVMALVGENGAGKSTMMKVLTGIYT-RDAGSILYLGKEV-----------------------TFNGPK---SSQEAGI-- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1273 nsgkilldgvdicdynlkdlrnlfSIVSQEPMLF-NMSIYENIKFGKENAT---REDVKRAckFAAIDEFIESLPNQY-- 1346
Cdd:PRK10762   82 ------------------------GIIHQELNLIpQLTIAENIFLGREFVNrfgRIDWKKM--YAEADKLLARLNLRFss 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1347 DTNVGpygkSLSGGQKQRIAIARALLREPKILLLDEATSSL-DSNSEKLIeKTIVDIKDKaDKTIITIAHRIASI-KRSD 1424
Cdd:PRK10762  136 DKLVG----ELSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTETESLF-RVIRELKSQ-GRGIVYISHRLKEIfEICD 209
                         250
                  ....*....|....*
gi 156095386 1425 KIVVFnnpdRTGSFV 1439
Cdd:PRK10762  210 DVTVF----RDGQFI 220
ABC_6TM_LmrA_like cd18551
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ...
62-358 9.74e-07

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: 52.05  E-value: 9.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   62 LGVSFVCATISGGT---LPFFVsvfGVIMKNMNLGENVNDIIFSLVLIGIFQFILSFISSFCMDVVTTKILKTLKIEFLK 138
Cdd:cd18551     1 LILALLLSLLGTAAslaQPLLV---KNLIDALSAGGSSGGLLALLVALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  139 SVFYQDGQFHDNN-PG---SKLTSDldfyLEQVNAGIGTKFITIFTYASAFLGLYIWSLFKNARLTLCITCVFPLIYICG 214
Cdd:cd18551    78 RLLRLPVSFFDRRrSGdlvSRVTND----TTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLII 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  215 VICNKKVkinKKTSLLYNNNT---MSIIEEALVGIRTVVSYCGENTILKKFN-LSEKLYsKYTLKANLMESLHIGMINGF 290
Cdd:cd18551   154 LPLGRRI---RKASKRAQDALgelSAALERALSAIRTVKASNAEERETKRGGeAAERLY-RAGLKAAKIEALIGPLMGLA 229
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156095386  291 ILASYAFGFWYGT-RIIISDLSnqqpnndfhggsvisilLGVLIS--MFMLTIILP------NITEYMKSLEATNNL 358
Cdd:cd18551   230 VQLALLVVLGVGGaRVASGALT-----------------VGTLVAflLYLFQLITPlsqlssFFTQLQKALGALERI 289
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
383-654 9.94e-07

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


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 52.42  E-value: 9.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHYDTRKDVeiyKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDsHNLKDVNlkwwRSKI 462
Cdd:COG4152     2 LELKGLTKRFGDKTAV---DDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDG-EPLDPED----RRRI 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  463 GVVSQDPLLFSN-SIKNNIKYsLYSLKDLealseesnedgfssqsdsnSRNSCRAKcagdLNDMIQTTDstelIQVRKNy 541
Cdd:COG4152    74 GYLPEERGLYPKmKVGEQLVY-LARLKGL-------------------SKAEAKRR----ADEWLERLG----LGDRAN- 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  542 etiedsevvsvsKKVlihdfvsalpdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLD--NKSeyLVQ 619
Cdd:COG4152   125 ------------KKV---------------------EELSKGNQQKVQLIAALLHDPELLILDEPFSGLDpvNVE--LLK 169
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 156095386  620 KTINNLKgnENRITIIIA-HRLSTI-RYANTIFVLSN 654
Cdd:COG4152   170 DVIRELA--AKGTTVIFSsHQMELVeELCDRIVIINK 204
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
386-626 9.98e-07

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 51.82  E-value: 9.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  386 KNVRFHYDTRKDVEiykDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDshnlKDVNL----KWWRSK 461
Cdd:PRK10895    7 KNLAKAYKGRRVVE---DVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDD----EDISLlplhARARRG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  462 IGVVSQDPLLFSN-SIKNNIKYSLYSLKDLealSEESNEDgfssqsdsnsrnscRAKcagdlndmiqttdsteliqvrkn 540
Cdd:PRK10895   80 IGYLPQEASIFRRlSVYDNLMAVLQIRDDL---SAEQRED--------------RAN----------------------- 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  541 yETIEDSEVvsvskkvlihdfvsalpdkyETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQK 620
Cdd:PRK10895  120 -ELMEEFHI--------------------EHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKR 178

                  ....*.
gi 156095386  621 TINNLK 626
Cdd:PRK10895  179 IIEHLR 184
ABC_6TM_LmrA_like cd18551
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ...
827-1109 1.14e-06

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: 52.05  E-value: 1.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  827 IIALSIMVAGGLyplFALLYAKYVGTLFDFANLEANSNKYSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMKLRLFEN 906
Cdd:cd18551     2 ILALLLSLLGTA---ASLAQPLLVKNLIDALSAGGSSGGLLALLVALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWRR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  907 IMYQEISFFDQdsHAPGLLSAHINRDVHLLKTGLVNNIV-IFTH-------FIVLFLVSTVMSFyfcpIVAAVLTGTYFI 978
Cdd:cd18551    79 LLRLPVSFFDR--RRSGDLVSRVTNDTTLLRELITSGLPqLVTGvltvvgaVVLMFLLDWVLTL----VTLAVVPLAFLI 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  979 FMRVFAIRARIAANkdvekkrvNQPGTAfVYNSDdeifkdpsflIQEAFYNMNTVIIYGLEDYFCTLIEKAIDYSNKGQK 1058
Cdd:cd18551   153 ILPLGRRIRKASKR--------AQDALG-ELSAA----------LERALSAIRTVKASNAEERETKRGGEAAERLYRAGL 213
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 156095386 1059 RKTLINSMLWGFSQSAQFFINSFAYWFGSFLIRRGTIQVDDFMkSLFTFLF 1109
Cdd:cd18551   214 KAAKIEALIGPLMGLAVQLALLVVLGVGGARVASGALTVGTLV-AFLLYLF 263
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
580-655 1.32e-06

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 52.61  E-value: 1.32e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156095386  580 LSGGQKQRISIARAIIRNPKILILDEATSSLDNK-SEYLVqKTINNLKgNENRITIIIAHRLstiryaNTIFVLSNR 655
Cdd:PRK11288  141 LSIGQRQMVEIAKALARNARVIAFDEPTSSLSAReIEQLF-RVIRELR-AEGRVILYVSHRM------EEIFALCDA 209
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
1347-1415 1.46e-06

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 52.81  E-value: 1.46e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 156095386 1347 DTNVGPygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkadkTIITIAH 1415
Cdd:PRK11819  158 DAKVTK----LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPG----TVVAVTH 218
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
1272-1396 1.46e-06

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: 50.57  E-value: 1.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1272 KNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKENATREDVKRACKFAAIDEFiESLPNQYdtnvg 1351
Cdd:cd03231    52 PLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENLRFWHADHSDEQVEEALARVGLNGF-EDRPVAQ----- 125
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 156095386 1352 pygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIE 1396
Cdd:cd03231   126 -----LSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFA 165
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
1355-1416 1.87e-06

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


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 50.73  E-value: 1.87e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 156095386 1355 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHR 1416
Cdd:COG2401   135 KELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATHH 196
PLN03211 PLN03211
ABC transporter G-25; Provisional
1355-1419 1.94e-06

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 52.57  E-value: 1.94e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156095386 1355 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTIITIAHRIAS 1419
Cdd:PLN03211  205 RGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKG-KTIVTSMHQPSS 268
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
399-614 2.05e-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: 52.24  E-value: 2.05e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   399 EIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDSHnlkdvnlkwwrsKIGVVSQDPLLFSN-SIK 477
Cdd:TIGR03719   19 EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGI------------KVGYLPQEPQLDPTkTVR 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   478 NNIKYSLYSLKDLEALSEESNEDGFSSQSDSNSRnscrAKCAGDLNDMIQTTDSTELiqvrknyetieDSEVvSVSKKVL 557
Cdd:TIGR03719   87 ENVEEGVAEIKDALDRFNEISAKYAEPDADFDKL----AAEQAELQEIIDAADAWDL-----------DSQL-EIAMDAL 150
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 156095386   558 ihdfvsALPDKyetlvGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS 614
Cdd:TIGR03719  151 ------RCPPW-----DADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES 196
ABC_6TM_YknV_like cd18545
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ...
866-1097 2.19e-06

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: 51.31  E-value: 2.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  866 YSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMKLRLFENIMYQEISFFdqDSHAPG-LLSAHINrDVH----LLKTGL 940
Cdd:cd18545    42 IALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFF--DSRPVGkILSRVIN-DVNslsdLLSNGL 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  941 VNnivIFTHFIVLFLVSTVMsFYF-------CPIVAAVLtgtyFIFMRVFAIRARIAAnKDVEKKRVNQpgTAFvynsdd 1013
Cdd:cd18545   119 IN---LIPDLLTLVGIVIIM-FSLnvrlalvTLAVLPLL----VLVVFLLRRRARKAW-QRVRKKISNL--NAY------ 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1014 eifkdpsflIQEAFYNMNTVIIYGLEDYFCTLIEKAIDYSNKGQKRKTLINSMLWGFSQSAQFFINSFAYWFGSFLIRRG 1093
Cdd:cd18545   182 ---------LHESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLNALFWPLVELISALGTALVYWYGGKLVLGG 252

                  ....
gi 156095386 1094 TIQV 1097
Cdd:cd18545   253 AITV 256
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
1173-1422 2.25e-06

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 52.26  E-value: 2.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1173 YLSRPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDLkNDHHIVFKNEQTgESSKEQMQQGDEEQNVgmkn 1252
Cdd:PRK11147   10 WLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLL-DDGRIIYEQDLI-VARLQQDPPRNVEGTV---- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1253 aneFSSSKEGADGQSSTLfKNSGKILLD-GVDICDYNLKDLRNLfsivsQEpmlfnmsiyeniKFGKENATREDVKrack 1331
Cdd:PRK11147   84 ---YDFVAEGIEEQAEYL-KRYHDISHLvETDPSEKNLNELAKL-----QE------------QLDHHNLWQLENR---- 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1332 faaIDEFIESLPNQYDTNVGpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkadkTII 1411
Cdd:PRK11147  139 ---INEVLAQLGLDPDAALS----SLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQG----SII 207
                         250
                  ....*....|.
gi 156095386 1412 TIAHRIASIKR 1422
Cdd:PRK11147  208 FISHDRSFIRN 218
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
579-652 2.32e-06

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 51.28  E-value: 2.32e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156095386  579 KLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTI-RYANTIFVL 652
Cdd:PRK11022  153 QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVaEAAHKIIVM 227
ABC_6TM_exporter_like cd18778
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
825-1109 2.45e-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: 51.00  E-value: 2.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  825 IAIIALSIMVAGGLYPlfallyAKYVGTLFDFANLEANS----NKYSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMK 900
Cdd:cd18778     3 LTLLCALLSTLLGLVP------PWLIRELVDLVTIGSKSlgllLGLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADLR 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  901 LRLFENIMYQEISFFDQdsHAPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSTVMSFYFCPIVAAV-LTGTYFI- 978
Cdd:cd18778    77 SDLYDKLQRLSLRYFDD--RQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLtLIPIPFLa 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  979 -FMRVFAIRARIAAnkdvekkRVNQpgtafvynsddEIFKDPSFLIQEAFYNMNTVIIYGLEDYfctliEKAiDYSNKGQ 1057
Cdd:cd18778   155 lGAWLYSKKVRPRY-------RKVR-----------EALGELNALLQDNLSGIREIQAFGREEE-----EAK-RFEALSR 210
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 156095386 1058 K-RKTLINSM-LWGFSQSAQFFINSFAY----WFGSFLIRRGTIQVDDfmksLFTFLF 1109
Cdd:cd18778   211 RyRKAQLRAMkLWAIFHPLMEFLTSLGTvlvlGFGGRLVLAGELTIGD----LVAFLL 264
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
1308-1450 2.53e-06

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: 51.75  E-value: 2.53e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1308 MSIYENIKFG--KENATREDVKRACKFAAIDEFIESLPNQYDTNVGPYGkSLSGGQKQRIAIARALLREPKILLLDEATS 1385
Cdd:TIGR02633  354 LGVGKNITLSvlKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLPIG-RLSGGNQQKAVLAKMLLTNPRVLILDEPTR 432
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156095386  1386 SLDSNSEKLIEKTIVDIKDKAdKTIITIAHRIASI-KRSDKIVVFNNPDRTGSFVQAQGTHEELLS 1450
Cdd:TIGR02633  433 GVDVGAKYEIYKLINQLAQEG-VAIIVVSSELAEVlGLSDRVLVIGEGKLKGDFVNHALTQEQVLA 497
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
383-638 2.81e-06

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 52.03  E-value: 2.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHYDT-RKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEG-------DVIINDSHNLKDVN 454
Cdd:PRK10535    5 LELKDIRRSYPSgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGtyrvagqDVATLDADALAQLR 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  455 lkwwRSKIGVVSQdpllfsnsiknniKYSLyslkdLEALSEESNedgfssqsdsnsrnscrakcagdlndmiqttdstel 534
Cdd:PRK10535   85 ----REHFGFIFQ-------------RYHL-----LSHLTAAQN------------------------------------ 106
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  535 IQVRKNYETIEDSEVVSVSKKVLIHdfvSALPDKyetlVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS 614
Cdd:PRK10535  107 VEVPAVYAGLERKQRLLRAQELLQR---LGLEDR----VEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHS 179
                         250       260
                  ....*....|....*....|....
gi 156095386  615 EYLVQKTINNLKgNENRITIIIAH 638
Cdd:PRK10535  180 GEEVMAILHQLR-DRGHTVIIVTH 202
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
383-640 3.34e-06

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 50.11  E-value: 3.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHYDTRKdveIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGdvIINDSHNLKdvnlkwwrskI 462
Cdd:PRK09544    5 VSLENVSVSFGQRR---VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEG--VIKRNGKLR----------I 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  463 GVVSQdpllfsnsiknniKYSLyslkdlealseesnedgfssqsdsnsrnscrakcagdlnDMIQTTDSTELIQVRKNye 542
Cdd:PRK09544   70 GYVPQ-------------KLYL---------------------------------------DTTLPLTVNRFLRLRPG-- 95
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  543 tIEDSEVVSVSKKVlihdfvsalpdKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI 622
Cdd:PRK09544   96 -TKKEDILPALKRV-----------QAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLI 163
                         250
                  ....*....|....*...
gi 156095386  623 NNLKGNENRITIIIAHRL 640
Cdd:PRK09544  164 DQLRRELDCAVLMVSHDL 181
PLN03211 PLN03211
ABC transporter G-25; Provisional
571-653 3.77e-06

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 51.42  E-value: 3.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  571 TLVGSNASK-LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLkGNENRITIIIAHRLSTIRYA--N 647
Cdd:PLN03211  197 TIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSL-AQKGKTIVTSMHQPSSRVYQmfD 275

                  ....*.
gi 156095386  648 TIFVLS 653
Cdd:PLN03211  276 SVLVLS 281
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
1335-1431 4.01e-06

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


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 50.47  E-value: 4.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1335 IDEFIE--SLPNQYDTNVgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIIT 1412
Cdd:COG4586   135 LDELVEllDLGELLDTPV----RQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILL 210
                          90       100
                  ....*....|....*....|
gi 156095386 1413 IAHRIASIKR-SDKIVVFNN 1431
Cdd:COG4586   211 TSHDMDDIEAlCDRVIVIDH 230
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
394-622 4.68e-06

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 49.10  E-value: 4.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  394 TRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDSHnlkdvnlkwwrskigvvSQDPLLFS 473
Cdd:PRK13539   11 VRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGD-----------------IDDPDVAE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  474 NSI----KNNIKyslyslkdlEALSEESNEDGFssqsdsnsrnscrAKCAGDLNDMIqttdsteliqvrknYETIEDsev 549
Cdd:PRK13539   74 ACHylghRNAMK---------PALTVAENLEFW-------------AAFLGGEELDI--------------AAALEA--- 114
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 156095386  550 vsvskkVLIHDfVSALPDKYetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI 622
Cdd:PRK13539  115 ------VGLAP-LAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELI 170
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
394-654 5.43e-06

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 50.61  E-value: 5.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  394 TRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVII--NDSHNLKDVNLKwwrSKIGVVSQD-PL 470
Cdd:PRK09536   12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVagDDVEALSARAAS---RRVASVPQDtSL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  471 LFSNSIKNNIkyslyslkdlealseesnEDGfssqsdsnsRNSCRAKCAgdlndmiqTTDSTELIQVRKNYETIEdsevv 550
Cdd:PRK09536   89 SFEFDVRQVV------------------EMG---------RTPHRSRFD--------TWTETDRAAVERAMERTG----- 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  551 svskkvlihdfVSALPDKYETlvgsnasKLSGGQKQRISIARAIIRNPKILILDEATSSLDnkseylVQKTINNLK---- 626
Cdd:PRK09536  129 -----------VAQFADRPVT-------SLSGGERQRVLLARALAQATPVLLLDEPTASLD------INHQVRTLElvrr 184
                         250       260       270
                  ....*....|....*....|....*....|
gi 156095386  627 -GNENRITIIIAHRLS-TIRYANTIFVLSN 654
Cdd:PRK09536  185 lVDDGKTAVAAIHDLDlAARYCDELVLLAD 214
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
579-611 5.82e-06

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 49.31  E-value: 5.82e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 156095386  579 KLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:PRK11248  128 QLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
404-640 5.88e-06

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: 51.17  E-value: 5.88e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   404 LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDshnlKDV--NLKWWRSKIGVVSQDPLLFsnsikNNIK 481
Cdd:TIGR01257  949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGG----KDIetNLDAVRQSLGMCPQHNILF-----HHLT 1019
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   482 YSLYSLkdlealseesnedgFSSQSDSNSRNSCRAkcagDLNDMIQTTDstelIQVRKNYEtiedsevvsvskkvlihdf 561
Cdd:TIGR01257 1020 VAEHIL--------------FYAQLKGRSWEEAQL----EMEAMLEDTG----LHHKRNEE------------------- 1058
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 156095386   562 vsalpdkyetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTInnLKGNENRITIIIAHRL 640
Cdd:TIGR01257 1059 ---------------AQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHM 1120
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
1322-1418 7.14e-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: 50.55  E-value: 7.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1322 TREDVKRACKFAAIDEFIE--SLPNQYDTNVgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLD----SNSEKLI 1395
Cdd:COG1245   180 VRELLEKVDERGKLDELAEklGLENILDRDI----SELSGGELQRVAIAAALLRDADFYFFDEPSSYLDiyqrLNVARLI 255
                          90       100
                  ....*....|....*....|...
gi 156095386 1396 EKTIvdikdKADKTIITIAHRIA 1418
Cdd:COG1245   256 RELA-----EEGKYVLVVEHDLA 273
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
1164-1431 7.77e-06

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 50.45  E-value: 7.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1164 IEIMDVNFRYlsrPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMrfydlkndhhivfkneqtgesskeqmqqGD 1243
Cdd:COG0488   316 LELEGLSKSY---GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLA----------------------------GE 364
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1244 EEqnvgmknanefssskegADgqsstlfknSGKILLdGVdicdyNLKdlrnlFSIVSQEPMLF--NMSIYENIKFGKENA 1321
Cdd:COG0488   365 LE-----------------PD---------SGTVKL-GE-----TVK-----IGYFDQHQEELdpDKTVLDELRDGAPGG 407
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1322 TREDVkRAckfaaideFIESL---PNQYDTNVGpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKT 1398
Cdd:COG0488   408 TEQEV-RG--------YLGRFlfsGDDAFKPVG----VLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEA 474
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 156095386 1399 IVDIkdkaDKTIITIAH------RIAsikrsDKIVVFNN 1431
Cdd:COG0488   475 LDDF----PGTVLLVSHdryfldRVA-----TRILEFED 504
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
580-658 7.93e-06

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: 48.37  E-value: 7.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  580 LSGGQKQ------RISIARAIIRNPKILILDEATSSLD--NKSEYLVQkTINNLKGNENRITIIIAHRLSTIRYANTIFV 651
Cdd:cd03240   116 CSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDeeNIEESLAE-IIEERKSQKNFQLIVITHDEELVDAADHIYR 194

                  ....*..
gi 156095386  652 LSNRENG 658
Cdd:cd03240   195 VEKDGRQ 201
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
578-669 8.34e-06

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: 50.21  E-value: 8.34e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   578 SKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNeNRITIIIAHRLSTIR-YANTIFVLSNRE 656
Cdd:TIGR02633  140 GDYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKaVCDTICVIRDGQ 218
                           90
                   ....*....|...
gi 156095386   657 NGSTVDVDVLGED 669
Cdd:TIGR02633  219 HVATKDMSTMSED 231
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
382-651 8.79e-06

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 49.31  E-value: 8.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  382 KIQFKNVRFHYDTRKDVEI--YKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDV--IINDSHNLKDVNLKW 457
Cdd:PRK13651    2 QIKVKNIVKIFNKKLPTELkaLDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewIFKDEKNKKKTKEKE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  458 W---------------------RSKIGVVSQ--DPLLFSNSIKNNIKYSLYSLKdleALSEESNEdgfssqsdsnsrnsc 514
Cdd:PRK13651   82 KvleklviqktrfkkikkikeiRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMG---VSKEEAKK--------------- 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  515 RAKcagdlnDMIqttdsteliqvrknyetiedsEVVsvskkvlihdfvsALPDKYetlVGSNASKLSGGQKQRISIARAI 594
Cdd:PRK13651  144 RAA------KYI---------------------ELV-------------GLDESY---LQRSPFELSGGQKRRVALAGIL 180
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  595 IRNPKILILDEATSSLDNKSEYLVQKTINNLkgNENRITIIIA-HRL-STIRYAN-TIFV 651
Cdd:PRK13651  181 AMEPDFLVFDEPTAGLDPQGVKEILEIFDNL--NKQGKTIILVtHDLdNVLEWTKrTIFF 238
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
1357-1415 9.00e-06

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 48.96  E-value: 9.00e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 156095386 1357 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH 1415
Cdd:PRK09544  121 LSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSH 179
ABC_6TM_HetC_like cd18568
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ...
76-309 9.12e-06

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: 49.10  E-value: 9.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   76 LPFFVSVF--GVIM-KNMNLgenVNDIIFSLVLIGIFQFILSFISSFCMDVVTTKILKTLKIEFLKSVF---------YQ 143
Cdd:cd18568    21 LPLFTQIIldRVLVhKNISL---LNLILIGLLIVGIFQILLSAVRQYLLDYFANRIDLSLLSDFYKHLLslplsffasRK 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  144 DG----QFHDNNpgsKLTSDLdfyleqVNAGIGT--KFITIFTYASAFLglyiwslFKNARLTLCITCVFPLIYICGVIC 217
Cdd:cd18568    98 VGdiitRFQENQ---KIRRFL------TRSALTTilDLLMVFIYLGLMF-------YYNLQLTLIVLAFIPLYVLLTLLS 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  218 NKKVKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGENTILKKFnlsEKLYSKYtLKANL-MESLHI--GMINGFI-LA 293
Cdd:cd18568   162 SPKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAERPIRWRW---ENKFAKA-LNTRFrGQKLSIvlQLISSLInHL 237
                         250
                  ....*....|....*.
gi 156095386  294 SYAFGFWYGTRIIISD 309
Cdd:cd18568   238 GTIAVLWYGAYLVISG 253
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
1357-1459 9.27e-06

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


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 48.83  E-value: 9.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1357 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHR---IASIkrSDKIVVFNNpd 1433
Cdd:PRK11300  154 LAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDmklVMGI--SDRIYVVNQ-- 229
                          90       100
                  ....*....|....*....|....*.
gi 156095386 1434 rtGSFVqAQGTHEELLSVQDgVYKKY 1459
Cdd:PRK11300  230 --GTPL-ANGTPEEIRNNPD-VIKAY 251
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
1353-1428 9.80e-06

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 49.35  E-value: 9.80e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156095386 1353 YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKRS-DKIVV 1428
Cdd:PRK11022  150 YPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAaHKIIV 226
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
580-654 9.82e-06

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: 47.81  E-value: 9.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  580 LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIahrLST-----IRYANTIFVLSN 654
Cdd:cd03215   105 LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRELA--DAGKAVLL---ISSeldelLGLCDRILVMYE 179
ABC_6TM_YknV_like cd18545
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ...
99-337 1.01e-05

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: 49.00  E-value: 1.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   99 IIFSLVLIGIFQFILSFISSFCMDVVTTKILKTLKIEFLKSVFYQDGQFHDNNP-G---SKLTSDLDFYLEQVNAGIGTK 174
Cdd:cd18545    42 IALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFDSRPvGkilSRVINDVNSLSDLLSNGLINL 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  175 FITIFTyasaFLGLYIWSLFKNARLTLCITCVFPLIYICGVICNKKV-----KINKKTSLLYnnntmSIIEEALVGIRTV 249
Cdd:cd18545   122 IPDLLT----LVGIVIIMFSLNVRLALVTLAVLPLLVLVVFLLRRRArkawqRVRKKISNLN-----AYLHESISGIRVI 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  250 VSYCGENTILKKF-NLSEKLYSKYtLKANLMESLH---IGMINGFilaSYAFGFWYGTRIIISDlsnqqpnndfhggsvi 325
Cdd:cd18545   193 QSFAREDENEEIFdELNRENRKAN-MRAVRLNALFwplVELISAL---GTALVYWYGGKLVLGG---------------- 252
                         250
                  ....*....|..
gi 156095386  326 SILLGVLISMFM 337
Cdd:cd18545   253 AITVGVLVAFIG 264
PRK10522 PRK10522
multidrug transporter membrane component/ATP-binding component; Provisional
1274-1415 1.05e-05

multidrug transporter membrane component/ATP-binding component; Provisional


Pssm-ID: 236707 [Multi-domain]  Cd Length: 547  Bit Score: 49.97  E-value: 1.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1274 SGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIyenikfGKENATREDvkrackfAAIDEFIESLPNQYDTNVGPy 1353
Cdd:PRK10522  377 SGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLFDQLL------GPEGKPANP-------ALVEKWLERLKMAHKLELED- 442
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156095386 1354 GK----SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH 1415
Cdd:PRK10522  443 GRisnlKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISH 508
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
570-645 1.10e-05

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: 48.52  E-value: 1.10e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156095386  570 ETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRItIIIAHRLSTIRY 645
Cdd:cd03236   130 RHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRELAEDDNYV-LVVEHDLAVLDY 204
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
371-484 1.10e-05

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 48.99  E-value: 1.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  371 NQDGKKLKDIKKIQFknvrfhydTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDSH-- 448
Cdd:PRK11831    1 EQSVANLVDMRGVSF--------TRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENip 72
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 156095386  449 NLKDVNLKWWRSKIGVVSQDPLLFSN-SIKNNIKYSL 484
Cdd:PRK11831   73 AMSRSRLYTVRKRMSMLFQSGALFTDmNVFDNVAYPL 109
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
1322-1418 1.29e-05

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 49.81  E-value: 1.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1322 TREDVKRACKFAAIDEFIE--SLPNQYDTNVgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTI 1399
Cdd:PRK13409  180 VRELLKKVDERGKLDEVVErlGLENILDRDI----SELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLI 255
                          90
                  ....*....|....*....
gi 156095386 1400 VDIKDkaDKTIITIAHRIA 1418
Cdd:PRK13409  256 RELAE--GKYVLVVEHDLA 272
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
578-652 1.30e-05

Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 49.78  E-value: 1.30e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156095386  578 SKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLkGNENRITIIIAHRLSTIRY-ANTIFVL 652
Cdd:COG1245   211 SELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIREL-AEEGKYVLVVEHDLAILDYlADYVHIL 285
ABC_6TM_T1SS_like cd18555
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ...
94-341 2.28e-05

Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.


Pssm-ID: 349999 [Multi-domain]  Cd Length: 294  Bit Score: 47.89  E-value: 2.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   94 ENVNDIIFSLVLIGIFQFILSFISSFCMDVVTTKILKTLKIEFLKSVFYQDGQFHDNNPgsklTSDLDF------YLEQV 167
Cdd:cd18555    39 NLLNVLGIGILILFLLYGLFSFLRGYIIIKLQTKLDKSLMSDFFEHLLKLPYSFFENRS----SGDLLFransnvYIRQI 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  168 nagIGTKFITIFTYASAFLGLYIWSLFKNARLTLCITCVFPLIYICGVICNKKVKINKKTSLLYNNNTMSIIEEALVGIR 247
Cdd:cd18555   115 ---LSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLLLLLTRKKIKKLNQEEIVAQTKVQSYLTETLYGIE 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  248 TVVSYCGENTILKKFnlsEKLYSK---YTLKANLMESLHIGMINGFILASYAFGFWYGTRIIIsdlsnqqpNNDFHGGSV 324
Cdd:cd18555   192 TIKSLGSEKNIYKKW---ENLFKKqlkAFKKKERLSNILNSISSSIQFIAPLLILWIGAYLVI--------NGELTLGEL 260
                         250
                  ....*....|....*..
gi 156095386  325 ISILlgVLISMFMLTII 341
Cdd:cd18555   261 IAFS--SLAGSFLTPIV 275
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
404-611 2.30e-05

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 47.86  E-value: 2.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  404 LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDsHNLKDVNLKWWRSKIGVVSQD-PLLFSNSIKNNIKY 482
Cdd:PRK10575   30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDA-QPLESWSSKAFARKVAYLPQQlPAAEGMTVRELVAI 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  483 SLYSLKDleALSEESNEDgfssqsdsnsrnscrakcagdlndmiqttdsteliqvrknYETIEDSeVVSVSKKVLIHDFV 562
Cdd:PRK10575  109 GRYPWHG--ALGRFGAAD----------------------------------------REKVEEA-ISLVGLKPLAHRLV 145
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 156095386  563 SAlpdkyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:PRK10575  146 DS---------------LSGGERQRAWIAMLVAQDSRCLLLDEPTSALD 179
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
1272-1442 2.47e-05

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 48.57  E-value: 2.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1272 KNSGKILLDGVDICDYNLKD-LRNLFSIVSQE-PMLFNMSIYENIKFGK---------ENATREDVKrackfAAIDEFie 1340
Cdd:PRK10982   50 KDSGSILFQGKEIDFKSSKEaLENGISMVHQElNLVLQRSVMDNMWLGRyptkgmfvdQDKMYRDTK-----AIFDEL-- 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1341 slpnqyDTNVGPYGK--SLSGGQKQRIAIARALLREPKILLLDEATSSLdsnSEKLIE---KTIVDIKDKAdKTIITIAH 1415
Cdd:PRK10982  123 ------DIDIDPRAKvaTLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL---TEKEVNhlfTIIRKLKERG-CGIVYISH 192
                         170       180
                  ....*....|....*....|....*...
gi 156095386 1416 RIASIKR-SDKIVVFnnpdRTGSFVQAQ 1442
Cdd:PRK10982  193 KMEEIFQlCDEITIL----RDGQWIATQ 216
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
406-611 2.60e-05

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 48.79  E-value: 2.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  406 FTLTEGKTYAFVGESGCGKSTILKLI--ERLYDptEGDVIINdshnlKDVnlkwwrskigVVS---QDPllfsnsiKNNI 480
Cdd:PRK11147   24 LHIEDNERVCLVGRNGAGKSTLMKILngEVLLD--DGRIIYE-----QDL----------IVArlqQDP-------PRNV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  481 KYSLYS------------LKDLEALSEESNEDgfssQSDSNsrnscrakcagdLNDMIQttdstelIQvrknyETIEDSE 548
Cdd:PRK11147   80 EGTVYDfvaegieeqaeyLKRYHDISHLVETD----PSEKN------------LNELAK-------LQ-----EQLDHHN 131
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 156095386  549 VVSVSKKvlIHDFVSAL---PDKyetlvgsNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:PRK11147  132 LWQLENR--INEVLAQLgldPDA-------ALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD 188
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
580-625 2.71e-05

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 48.39  E-value: 2.71e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 156095386  580 LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNL 625
Cdd:PRK13549  406 LSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQL 451
cbiO PRK13644
energy-coupling factor transporter ATPase;
383-652 2.74e-05

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 47.67  E-value: 2.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  383 IQFKNVRFHYDtrKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDSHNLKDVNLKWWRSKI 462
Cdd:PRK13644    2 IRLENVSYSYP--DGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  463 GVVSQDPllfsnsiknnikyslyslkDLEALSEESNED-GFSSQsdsnsrNSCRAKcagdlndmiqttdstelIQVRKNY 541
Cdd:PRK13644   80 GIVFQNP-------------------ETQFVGRTVEEDlAFGPE------NLCLPP-----------------IEIRKRV 117
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  542 ETiedsevvsvskkvlihdfvsALPD-KYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQK 620
Cdd:PRK13644  118 DR--------------------ALAEiGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLE 177
                         250       260       270
                  ....*....|....*....|....*....|..
gi 156095386  621 TINNLKgNENRITIIIAHRLSTIRYANTIFVL 652
Cdd:PRK13644  178 RIKKLH-EKGKTIVYITHNLEELHDADRIIVM 208
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
580-654 2.78e-05

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 47.46  E-value: 2.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  580 LSGGQKQRISIARAIIR------NPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLS-TIRYANTIFVL 652
Cdd:PRK13548  135 LSGGEQQRVQLARVLAQlwepdgPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNlAARYADRIVLL 214

                  ..
gi 156095386  653 SN 654
Cdd:PRK13548  215 HQ 216
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
566-645 3.08e-05

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: 47.02  E-value: 3.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  566 PDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTIRY 645
Cdd:cd03237   102 PLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDY 181
3a01203 TIGR00954
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...
1357-1421 3.27e-05

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: 48.59  E-value: 3.27e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156095386  1357 LSGGQKQRIAIARALLREPKILLLDEATS--SLDsnseklIEKTIVDIKDKADKTIITIAHRIASIK 1421
Cdd:TIGR00954  583 LSGGEKQRIAMARLFYHKPQFAILDECTSavSVD------VEGYMYRLCREFGITLFSVSHRKSLWK 643
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
1357-1420 4.12e-05

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 47.18  E-value: 4.12e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156095386 1357 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTIITIAHRIASI 1420
Cdd:PRK15056  143 LSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEG-KTMLVSTHNLGSV 205
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
1274-1417 4.55e-05

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: 48.47  E-value: 4.55e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1274 SGKILLDGVDIcDYNLKDLRNLFSIVSQEPMLFN-MSIYENIKFGKENATREDVKRACKFAAIdefIESLPNQYDTNvgP 1352
Cdd:TIGR01257  984 SGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHhLTVAEHILFYAQLKGRSWEEAQLEMEAM---LEDTGLHHKRN--E 1057
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156095386  1353 YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIvdIKDKADKTIITIAHRI 1417
Cdd:TIGR01257 1058 EAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHM 1120
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
400-639 4.92e-05

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


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 46.10  E-value: 4.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLY--DPTEGDVIINDshnlkdvnLKWWRSKIGVvsqdpllfsnsik 477
Cdd:COG2401    45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPD--------NQFGREASLI------------- 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  478 nnikyslyslkdlealseesneDGFSSQSDsnsrnscrakcagdlndmiqTTDSTELIQVRKNyetiedSEVVSVSKKVl 557
Cdd:COG2401   104 ----------------------DAIGRKGD--------------------FKDAVELLNAVGL------SDAVLWLRRF- 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  558 ihdfvsalpdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLkGNENRITIIIA 637
Cdd:COG2401   135 --------------------KELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKL-ARRAGITLVVA 193

                  ...
gi 156095386  638 -HR 639
Cdd:COG2401   194 tHH 196
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
570-607 5.24e-05

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 47.71  E-value: 5.24e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 156095386  570 ETLVGSnaskLSGGQKQRISIARAIIRNPKILILDEAT 607
Cdd:COG1129   389 EQPVGN----LSGGNQQKVVLAKWLATDPKVLILDEPT 422
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
386-611 5.29e-05

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 46.46  E-value: 5.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  386 KNVRFHYDTRKDVEiykDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVI-------INDSHNLKDVNLKW- 457
Cdd:PRK11701   10 RGLTKLYGPRKGCR---DVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHyrmrdgqLRDLYALSEAERRRl 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  458 WRSKIGVVSQDP---LLFSNSIKNNIKYSLYSLKDlealseesnedgfssqsdsnsRNSCRakcagdlndmIQTTDSTEL 534
Cdd:PRK11701   87 LRTEWGFVHQHPrdgLRMQVSAGGNIGERLMAVGA---------------------RHYGD----------IRATAGDWL 135
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156095386  535 IQVRKNYETIEDsevvsvskkvlihdfvsaLPDKYetlvgsnasklSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:PRK11701  136 ERVEIDAARIDD------------------LPTTF-----------SGGMQQRLQIARNLVTHPRLVFMDEPTGGLD 183
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
402-649 5.38e-05

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: 48.09  E-value: 5.38e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   402 KDLNFTLTEGKTYAFVGESGCGKSTILK------LIERLY----DPTEGDVIINDSHnlkdvnlkwwRSKIGVVSQDPLL 471
Cdd:TIGR00630  625 KNITVSIPLGLFTCITGVSGSGKSTLINdtlypaLANRLNgaktVPGRYTSIEGLEH----------LDKVIHIDQSPIG 694
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   472 FSnSIKNNIKYS--LYSLKDLEALSEESNEDGFSsqsdsNSRNS-------CrAKCAGD---------LNDMIQTTDS-- 531
Cdd:TIGR00630  695 RT-PRSNPATYTgvFDEIRELFAETPEAKVRGYT-----PGRFSfnvkggrC-EACQGDgvikiemhfLPDVYVPCEVck 767
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   532 -----TELIQVRKNYETIEDSEVVSVSKKvliHDFVSALPD---KYETLV---------GSNASKLSGGQKQRISIARAI 594
Cdd:TIGR00630  768 gkrynRETLEVKYKGKNIADVLDMTVEEA---YEFFEAVPSisrKLQTLCdvglgyirlGQPATTLSGGEAQRIKLAKEL 844
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 156095386   595 IR---NPKILILDEATSSLD----NKSEYLVQKTINnlKGNEnriTIIIAHRLSTIRYANTI 649
Cdd:TIGR00630  845 SKrstGRTLYILDEPTTGLHfddiKKLLEVLQRLVD--KGNT---VVVIEHNLDVIKTADYI 901
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
579-645 5.88e-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: 45.26  E-value: 5.88e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156095386  579 KLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTIRY 645
Cdd:cd03222    71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDY 137
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
575-636 6.04e-05

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


Pssm-ID: 440752 [Multi-domain]  Cd Length: 240  Bit Score: 46.18  E-value: 6.04e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 156095386  575 SNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIII 636
Cdd:COG1137   132 SKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRHLK--ERGIGVLI 191
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
403-611 6.58e-05

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 47.81  E-value: 6.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  403 DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVII----NDSHNLKDvnlkwwRSKIGVVSQdpllfsnsikn 478
Cdd:NF033858  284 HVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLfgqpVDAGDIAT------RRRVGYMSQ----------- 346
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  479 niKYSLYS-------LkDLEA----LSEEsnedgfssqsDSNSRnscrakcagdLNDMIQTTDsteliqvrknyetieds 547
Cdd:NF033858  347 --AFSLYGeltvrqnL-ELHArlfhLPAA----------EIAAR----------VAEMLERFD----------------- 386
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156095386  548 evvsvskkvlIHDFVSALPDKyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:NF033858  387 ----------LADVADALPDS-----------LPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
578-625 6.59e-05

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: 47.13  E-value: 6.59e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 156095386   578 SKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNL 625
Cdd:TIGR02633  402 GRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQL 449
ABC_6TM_PCAT1_LagD_like cd18570
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ...
59-309 7.44e-05

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: 46.28  E-value: 7.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   59 RKLLGVSFVCAtisggtlpFFVSVFGVIMK-----------NMNLGENVNDIIFSLVLIGIFQFILSFISSFCMDVVTTK 127
Cdd:cd18570     1 KKLLILILLLS--------LLITLLGIAGSfffqiliddiiPSGDINLLNIISIGLILLYLFQSLLSYIRSYLLLKLSQK 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  128 ILKTLKIEFLKSVFYQDGQFHDNNPGSKLTS---DLDFYLEQVNAGIGTKFITIFT--YASAFLGLYIWSLFknarltlC 202
Cdd:cd18570    73 LDIRLILGYFKHLLKLPLSFFETRKTGEIISrfnDANKIREAISSTTISLFLDLLMviISGIILFFYNWKLF-------L 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  203 ITCVFPLIYICGVICNKKV--KINKKTSLLYNNNTMSIIeEALVGIRTVVSYCGENTILKKFnlsEKLYSKYtLKANLME 280
Cdd:cd18570   146 ITLLIIPLYILIILLFNKPfkKKNREVMESNAELNSYLI-ESLKGIETIKSLNAEEQFLKKI---EKKFSKL-LKKSFKL 220
                         250       260       270
                  ....*....|....*....|....*....|....
gi 156095386  281 SLhIGMINGFI--LASYAFG---FWYGTRIIISD 309
Cdd:cd18570   221 GK-LSNLQSSIkgLISLIGSlliLWIGSYLVIKG 253
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
570-655 7.72e-05

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 47.11  E-value: 7.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  570 ETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTIRYanti 649
Cdd:PRK13409  444 ERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDY---- 519

                  ....*.
gi 156095386  650 fvLSNR 655
Cdd:PRK13409  520 --ISDR 523
ABC_6TM_exporter_like cd18563
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
826-989 8.29e-05

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: 46.35  E-value: 8.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  826 AIIALSIMVAGglyPLFALLYAKYVGTLFD--FANLEANSNKYSLYILVIA-----IAMFISETLKNYYNNVIGEKVEKT 898
Cdd:cd18563     1 LILGFLLMLLG---TALGLVPPYLTKILIDdvLIQLGPGGNTSLLLLLVLGlagayVLSALLGILRGRLLARLGERITAD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  899 MKLRLFENIMYQEISFFdqDSHAPGLLSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSTVMSFYFCPIVA-AVLTGTYF 977
Cdd:cd18563    78 LRRDLYEHLQRLSLSFF--DKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLAlLVLIPVPL 155
                         170
                  ....*....|..
gi 156095386  978 IFMRVFAIRARI 989
Cdd:cd18563   156 VVWGSYFFWKKI 167
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
1356-1448 8.50e-05

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: 47.32  E-value: 8.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1356 SLSGGQKQRIAIARALLRE---PKILLLDEATSSL---DSNseKLIEkTIVDIKDKADkTIITIAHRIASIKRSDKIVVF 1429
Cdd:TIGR00630  829 TLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLhfdDIK--KLLE-VLQRLVDKGN-TVVVIEHNLDVIKTADYIIDL 904
                           90       100
                   ....*....|....*....|.
gi 156095386  1430 nNPD--RTGSFVQAQGTHEEL 1448
Cdd:TIGR00630  905 -GPEggDGGGTVVASGTPEEV 924
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
575-651 9.41e-05

Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 47.09  E-value: 9.41e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156095386  575 SNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTIRY-ANTIFV 651
Cdd:COG1245   451 KNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYiSDRLMV 528
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
1356-1450 9.49e-05

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 46.85  E-value: 9.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1356 SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKdKADKTIITIAHRIASI-KRSDKIVVFNNPDR 1434
Cdd:PRK13549  405 RLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLV-QQGVAIIVISSELPEVlGLSDRVLVMHEGKL 483
                          90
                  ....*....|....*.
gi 156095386 1435 TGSFVQAQGTHEELLS 1450
Cdd:PRK13549  484 KGDLINHNLTQEQVME 499
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
1170-1429 9.53e-05

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: 45.60  E-value: 9.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1170 NFRYLSRPNVPIYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDLkndhhivfkneqtgesskeqmqqgdeeqnvg 1249
Cdd:cd03220    26 LGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPP------------------------------- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1250 mknanefssskegadgqsstlfkNSGKILLDGvdicdynlkDLRNLFSI-VSQEPMLfnmSIYENIKFgkeNATREDVKR 1328
Cdd:cd03220    75 -----------------------DSGTVTVRG---------RVSSLLGLgGGFNPEL---TGRENIYL---NGRLLGLSR 116
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1329 ACKFAAIDEFIE--SLPNQYDTNVgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSN-SEKLIEKtIVDIKDK 1405
Cdd:cd03220   117 KEIDEKIDEIIEfsELGDFIDLPV----KTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAfQEKCQRR-LRELLKQ 191
                         250       260
                  ....*....|....*....|....*
gi 156095386 1406 AdKTIITIAHRIASIKR-SDKIVVF 1429
Cdd:cd03220   192 G-KTVILVSHDPSSIKRlCDRALVL 215
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
579-643 9.91e-05

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 46.03  E-value: 9.91e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156095386  579 KLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgNENRITIIIAHRLSTI 643
Cdd:PRK15056  142 ELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELR-DEGKTMLVSTHNLGSV 205
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
569-654 1.06e-04

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 46.65  E-value: 1.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  569 YETLVGSnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTIRYANT 648
Cdd:PRK10982  385 HRTQIGS----LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDR 460

                  ....*.
gi 156095386  649 IFVLSN 654
Cdd:PRK10982  461 ILVMSN 466
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
395-611 1.13e-04

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: 44.66  E-value: 1.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   395 RKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDSHnLKDVNLKWWRSkigvvsqdpLLF-- 472
Cdd:TIGR01189   10 RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTP-LAEQRDEPHEN---------ILYlg 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   473 -SNSIKNnikyslyslkdleALSEESNEDGFSSQSDSNSRNSCRAKCAGDLNDmiqttdsteliqvrknyetIEDsevvs 551
Cdd:TIGR01189   80 hLPGLKP-------------ELSALENLHFWAAIHGGAQRTIEDALAAVGLTG-------------------FED----- 122
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   552 vskkvlihdfvsaLPdkyetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:TIGR01189  123 -------------LP----------AAQLSAGQQRRLALARLWLSRRPLWILDEPTTALD 159
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
1322-1446 1.32e-04

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: 45.44  E-value: 1.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1322 TREDVKRACKFAAIDEFIE--SLPNQYDTNVgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDS----NSEKLI 1395
Cdd:cd03236   107 VGELLKKKDERGKLDELVDqlELRHVLDRNI----DQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIkqrlNAARLI 182
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 156095386 1396 EKTIVDikdkaDKTIITIAHRIASIKR-SDKI-VVFNNPDRTGSFVQAQGTHE 1446
Cdd:cd03236   183 RELAED-----DNYVLVVEHDLAVLDYlSDYIhCLYGEPGAYGVVTLPKSVRE 230
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
580-611 1.87e-04

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 45.76  E-value: 1.87e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 156095386  580 LSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:PRK10762  396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
1356-1396 2.20e-04

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: 43.89  E-value: 2.20e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 156095386  1356 SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIE 1396
Cdd:TIGR01189  127 QLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLA 167
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
398-643 2.24e-04

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 45.49  E-value: 2.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  398 VEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDshnlKDVNLKwwRSK------IGVVSQD-PL 470
Cdd:PRK10982   11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQG----KEIDFK--SSKealengISMVHQElNL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  471 LFSNSIKNNIKYSLYSLKDLEAlseesnedgfssqsdsnsrnscrakcagDLNDMIQTTdsteliqvrknyETIEDSEVV 550
Cdd:PRK10982   85 VLQRSVMDNMWLGRYPTKGMFV----------------------------DQDKMYRDT------------KAIFDELDI 124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  551 SVSKKVLIhdfvsalpdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnEN 630
Cdd:PRK10982  125 DIDPRAKV-------------------ATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKLK--ER 183
                         250
                  ....*....|....
gi 156095386  631 RITII-IAHRLSTI 643
Cdd:PRK10982  184 GCGIVyISHKMEEI 197
ABCG_PDR_domain2 cd03232
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...
580-625 2.60e-04

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: 43.77  E-value: 2.60e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 156095386  580 LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNL 625
Cdd:cd03232   109 LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKL 154
PLN03073 PLN03073
ABC transporter F family; Provisional
1356-1396 2.83e-04

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 45.62  E-value: 2.83e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 156095386 1356 SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNS-EKLIE 1396
Cdd:PLN03073  627 TLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAvEALIQ 668
YbjD COG3593
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ...
380-499 2.94e-04

Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];


Pssm-ID: 442812 [Multi-domain]  Cd Length: 359  Bit Score: 44.99  E-value: 2.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  380 IKKIQFKNVRfhydtrkdveIYKDLNFTLTEGKTyAFVGESGCGKSTILKLIERLYDPTEGDVI-INDSHNLKDVNLK-- 456
Cdd:COG3593     3 LEKIKIKNFR----------SIKDLSIELSDDLT-VLVGENNSGKSSILEALRLLLGPSSSRKFdEEDFYLGDDPDLPei 71
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 156095386  457 ----WWRSKIGVVSQDplLFSNSIKNNIKYSLYSLKdlEALSEESNE 499
Cdd:COG3593    72 eielTFGSLLSRLLRL--LLKEEDKEELEEALEELN--EELKEALKA 114
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
570-652 3.00e-04

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 45.18  E-value: 3.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  570 ETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLkgNENRITIIIAHRLSTIRY-ANT 648
Cdd:PRK13409  203 ENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIREL--AEGKYVLVVEHDLAVLDYlADN 280

                  ....
gi 156095386  649 IFVL 652
Cdd:PRK13409  281 VHIA 284
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
577-643 3.02e-04

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


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 44.21  E-value: 3.02e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 156095386  577 ASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTI 643
Cdd:PRK11300  151 AGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLV 217
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
557-663 3.02e-04

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 44.15  E-value: 3.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  557 LIHDFVSALpdKYETLVGSNASKLSGGQKQRISIARAIIR-----NP--KILILDEATSSLDNKSEYLVQKTINNL--KG 627
Cdd:PRK03695  106 ALNEVAEAL--GLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdiNPagQLLLLDEPMNSLDVAQQAALDRLLSELcqQG 183
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 156095386  628 nenrITIIIA-HRLS-TIRYANTIFVLSNRE---NGSTVDV 663
Cdd:PRK03695  184 ----IAVVMSsHDLNhTLRHADRVWLLKQGKllaSGRRDEV 220
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
1319-1389 4.21e-04

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


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 45.10  E-value: 4.21e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 156095386  1319 ENATREDvkRACKFAAIDEFIESLPNQYDTNVG-PYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDS 1389
Cdd:TIGR00956  173 DGVSREE--YAKHIADVYMATYGLSHTRNTKVGnDFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLDS 242
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
1358-1388 4.79e-04

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 43.76  E-value: 4.79e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 156095386 1358 SGGQKQRIAIARALLREPKILLLDEATSSLD 1388
Cdd:PRK11701  153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLD 183
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
1270-1388 4.79e-04

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 43.38  E-value: 4.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1270 LFKNSGKILLDGVDICDYNLKDL---RNLFSivSQEPMLFNMSIYENIKFGKENATREDVKRAckfaAIDEFIES--LPN 1344
Cdd:PRK03695   45 LLPGSGSIQFAGQPLEAWSAAELarhRAYLS--QQQTPPFAMPVFQYLTLHQPDKTRTEAVAS----ALNEVAEAlgLDD 118
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 156095386 1345 QYDTNVGpygkSLSGGQKQRIAIARALLR-------EPKILLLDEATSSLD 1388
Cdd:PRK03695  119 KLGRSVN----QLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSLD 165
hmuV PRK13547
heme ABC transporter ATP-binding protein;
570-663 5.05e-04

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 43.66  E-value: 5.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  570 ETLVGSNASKLSGGQKQRISIARAI---------IRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRL 640
Cdd:PRK13547  136 TALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDP 215
                          90       100
                  ....*....|....*....|....*..
gi 156095386  641 S-TIRYANTIFVLSNRE---NGSTVDV 663
Cdd:PRK13547  216 NlAARHADRIAMLADGAivaHGAPADV 242
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
577-611 5.16e-04

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 44.73  E-value: 5.16e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 156095386  577 ASKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:NF033858  134 AGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVD 168
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
1306-1422 5.33e-04

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


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 43.53  E-value: 5.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1306 FNMSI--YENIKFgkeNA-----TREDVKRacKFAAIDEFIEsLPNQYDTNVgpygKSLSGGQKQRIAIARALLREPKIL 1378
Cdd:COG1134    99 FHPELtgRENIYL---NGrllglSRKEIDE--KFDEIVEFAE-LGDFIDQPV----KTYSSGMRARLAFAVATAVDPDIL 168
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 156095386 1379 LLDEATSSLDSN-SEKLIEKtIVDIKDKAdKTIITIAHRIASIKR 1422
Cdd:COG1134   169 LVDEVLAVGDAAfQKKCLAR-IRELRESG-RTVIFVSHSMGAVRR 211
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
1355-1401 5.73e-04

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 44.56  E-value: 5.73e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 156095386 1355 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVD 1401
Cdd:PRK11147  439 KALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDS 485
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
1181-1450 6.32e-04

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 43.44  E-value: 6.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1181 IYKDLTFSCESKKTTAIVGETGSGKSTVMSLLMRFYDLKNDHhiVFKNeqtgessKEQMQQgdeeqnvgmknanefSSSK 1260
Cdd:PRK10253   22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGH--VWLD-------GEHIQH---------------YASK 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1261 EGAdgqsstlfKNSGKILLDGVDICDYNLKDL--RNLFSivsQEPMLfnmsiyenIKFGKENAtrEDVKRACKFAAIDEf 1338
Cdd:PRK10253   78 EVA--------RRIGLLAQNATTPGDITVQELvaRGRYP---HQPLF--------TRWRKEDE--EAVTKAMQATGITH- 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1339 iesLPNQ-YDTnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRI 1417
Cdd:PRK10253  136 ---LADQsVDT--------LSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDL 204
                         250       260       270
                  ....*....|....*....|....*....|....
gi 156095386 1418 ASIKR-SDKIVVFnnpdRTGSFVqAQGTHEELLS 1450
Cdd:PRK10253  205 NQACRyASHLIAL----REGKIV-AQGAPKEIVT 233
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
394-635 6.55e-04

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


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 43.54  E-value: 6.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  394 TRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIIN--DSHNLKDVNLKwwrsKIGVV----SQ 467
Cdd:COG4586    31 EYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLgyVPFKRRKEFAR----RIGVVfgqrSQ 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  468 dpLLFsnsiknnikyslyslkDLEALseesnedgfssqsdsnsrnscrakcagdlndmiqttDSTELIqvRKNYEtIEDS 547
Cdd:COG4586   107 --LWW----------------DLPAI------------------------------------DSFRLL--KAIYR-IPDA 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  548 EVvsvskKVLIHDFVSAL--PDKYETLVgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNL 625
Cdd:COG4586   130 EY-----KKRLDELVELLdlGELLDTPV----RQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEY 200
                         250
                  ....*....|
gi 156095386  626 KgNENRITII 635
Cdd:COG4586   201 N-RERGTTIL 209
PLN03140 PLN03140
ABC transporter G family member; Provisional
580-624 7.40e-04

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 44.45  E-value: 7.40e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 156095386  580 LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINN 624
Cdd:PLN03140 1020 LSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRN 1064
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
1360-1415 7.65e-04

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 43.73  E-value: 7.65e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 156095386 1360 GQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEktivDIKDKADKTIITIAH 1415
Cdd:PRK15064  159 GWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLE----DVLNERNSTMIIISH 210
PRK15093 PRK15093
peptide ABC transporter ATP-binding protein SapD;
579-652 7.95e-04

peptide ABC transporter ATP-binding protein SapD;


Pssm-ID: 185049 [Multi-domain]  Cd Length: 330  Bit Score: 43.25  E-value: 7.95e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 156095386  579 KLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTI-RYANTIFVL 652
Cdd:PRK15093  158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLsQWADKINVL 232
PLN03140 PLN03140
ABC transporter G family member; Provisional
1325-1413 8.33e-04

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 44.07  E-value: 8.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1325 DVKRACKFAAIDEFIE--SLPNQYDTNVG-PYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVD 1401
Cdd:PLN03140  985 EVSKEEKMMFVDEVMElvELDNLKDAIVGlPGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRN 1064
                          90
                  ....*....|..
gi 156095386 1402 IKDKADKTIITI 1413
Cdd:PLN03140 1065 TVDTGRTVVCTI 1076
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
571-643 9.06e-04

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 43.45  E-value: 9.06e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156095386  571 TLVGsnasKLSGGQKQRISIARAIIRNPKILILDEATSSL-DNKSEYLVqKTINNLKgNENRITIIIAHRLSTI 643
Cdd:PRK10762  137 KLVG----ELSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTETESLF-RVIRELK-SQGRGIVYISHRLKEI 204
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
1307-1459 9.11e-04

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: 43.85  E-value: 9.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1307 NMSIYENIKFgKENATREDVKRACKFAAIDEFIESLpnQYDTNVG-PY------GKSLSGGQKQRIAIARAL-------- 1371
Cdd:TIGR00630  435 ELSIREAHEF-FNQLTLTPEEKKIAEEVLKEIRERL--GFLIDVGlDYlslsraAGTLSGGEAQRIRLATQIgsgltgvl 511
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1372 --LREPKILLLDEATssldsnsEKLIEkTIVDIKDKADkTIITIAHRIASIKRSDKIVvfnnpD------RTGSFVQAQG 1443
Cdd:TIGR00630  512 yvLDEPSIGLHQRDN-------RRLIN-TLKRLRDLGN-TLIVVEHDEDTIRAADYVI-----DigpgagEHGGEVVASG 577
                          170
                   ....*....|....*.
gi 156095386  1444 THEELLSVQDGVYKKY 1459
Cdd:TIGR00630  578 TPEEILANPDSLTGQY 593
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
555-649 1.07e-03

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 43.66  E-value: 1.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  555 KVLIHDFVSALPdkyetlVGSNASKLSGGQKQRISIARAIIRNPK---ILILDEATSSLDNKSEYLVQKTINNLKgNENR 631
Cdd:PRK00635 1681 QALIDNGLGYLP------LGQNLSSLSLSEKIAIKIAKFLYLPPKhptLFLLDEIATSLDNQQKSALLVQLRTLV-SLGH 1753
                          90
                  ....*....|....*...
gi 156095386  632 ITIIIAHRLSTIRYANTI 649
Cdd:PRK00635 1754 SVIYIDHDPALLKQADYL 1771
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
382-442 1.13e-03

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 43.40  E-value: 1.13e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156095386  382 KIQF--KNVRFHYDTRKDVeiyKDLNFTLTEGKTYAFVGESGCGKSTILKL-IERLyDPTEGDV 442
Cdd:PRK11147  317 KIVFemENVNYQIDGKQLV---KDFSAQVQRGDKIALIGPNGCGKTTLLKLmLGQL-QADSGRI 376
ycf16 CHL00131
sulfate ABC transporter protein; Validated
1358-1415 1.24e-03

sulfate ABC transporter protein; Validated


Pssm-ID: 214372 [Multi-domain]  Cd Length: 252  Bit Score: 42.32  E-value: 1.24e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 156095386 1358 SGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKaDKTIITIAH 1415
Cdd:CHL00131  153 SGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTS-ENSIILITH 209
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
1310-1460 1.26e-03

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 43.66  E-value: 1.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1310 IYENIKFGKE-NATREDVkrACKFAAIDEFIESLPNQYDTNVG--PYGK---SLSGGQKQRIAIARALL---REPKILLL 1380
Cdd:PRK00635 1649 VYEGKHFGQLlQTPIEEV--AETFPFLKKIQKPLQALIDNGLGylPLGQnlsSLSLSEKIAIKIAKFLYlppKHPTLFLL 1726
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1381 DEATSSLDSNSEKLIEK---TIVDIkdkaDKTIITIAHRIASIKRSDKIVVFN-NPDRTGSFVQAQGTHEELLSVQDGVY 1456
Cdd:PRK00635 1727 DEIATSLDNQQKSALLVqlrTLVSL----GHSVIYIDHDPALLKQADYLIEMGpGSGKTGGKILFSGPPKDISASKDSLL 1802

                  ....
gi 156095386 1457 KKYV 1460
Cdd:PRK00635 1803 KTYM 1806
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
1357-1391 1.32e-03

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: 41.86  E-value: 1.32e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 156095386 1357 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNS 1391
Cdd:cd03233   119 ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSST 153
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
570-625 1.36e-03

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


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 43.56  E-value: 1.36e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 156095386   570 ETLVGSNASKLSGGQKQRISIARAIIRNPKILI-LDEATSSLDNKSEYLVQKTINNL 625
Cdd:TIGR00956  892 DAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKL 948
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
1356-1402 1.50e-03

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 43.08  E-value: 1.50e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 156095386 1356 SLSGGQkQRIA-IARALLREPKILLLDEATSSLDSNSEKLIeKTIVDI 1402
Cdd:PRK10938  401 SLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLV-RRFVDV 446
ABC_6TM_PrtD_LapB_HlyB_like cd18566
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ...
824-1097 1.61e-03

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: 42.18  E-value: 1.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  824 DIAIIALSIMVAGGLYPLFAL-LYAKYVGtlfdfanleaNSNKYSLYILVIAIAM-FISET----LKNYYNNVIGEKVEK 897
Cdd:cd18566     6 QVLLASLFINILALATPLFILqVYDRVIP----------NESIPTLQVLVIGVVIaILLESllrlLRSYILAWIGARFDH 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  898 TMKLRLFENIMYQEISFFDQDSHapgllSAHINR--DVHLLK---TGLVNNIVIFTHFIVLFLVstVMSFY-----FCPI 967
Cdd:cd18566    76 RLSNAAFEHLLSLPLSFFEREPS-----GAHLERlnSLEQIReflTGQALLALLDLPFVLIFLG--LIWYLggklvLVPL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  968 VAAVLtgtyFIFMRVF---AIRARIAANKDVEKKRVNqpgtafvynsddeifkdpsFLIqEAFYNMNTVIIYGLEDYFC- 1043
Cdd:cd18566   149 VLLGL----FVLVAILlgpILRRALKERSRADERRQN-------------------FLI-ETLTGIHTIKAMAMEPQMLr 204
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 156095386 1044 ---TLIEKAIDYSNKGQKRKTLINSMLWGFSQSAQFFInsfaYWFGSFLIRRGTIQV 1097
Cdd:cd18566   205 ryeRLQANAAYAGFKVAKINAVAQTLGQLFSQVSMVAV----VAFGALLVINGDLTV 257
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
580-638 1.68e-03

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 42.69  E-value: 1.68e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 156095386  580 LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAH 638
Cdd:PRK10938  402 LSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSH 460
ABC_6TM_ABCB8_like cd18574
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ...
99-311 2.05e-03

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: 41.76  E-value: 2.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   99 IIFSLVLIGIFQFI-LSFISSFCMDVVTTkilktLKIEFLKSVFYQDGQFHDNNPG----SKLTSDL-DF--YLEQVnAG 170
Cdd:cd18574    48 LLGLYLLQSLLTFAyISLLSVVGERVAAR-----LRNDLFSSLLRQDIAFFDTHRTgelvNRLTADVqEFksSFKQC-VS 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  171 IGTKFITIFtyASAFLGLYIWSlfknARLTLCITCVFPLIYICGVICNKKVKINKKTSLLYNNNTMSIIEEALVGIRTVV 250
Cdd:cd18574   122 QGLRSVTQT--VGCVVSLYLIS----PKLTLLLLVIVPVVVLVGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVR 195
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 156095386  251 SYCGENTILKKFNLSEKLYSKytLKANLmeSLHIGM--------INGFILASYAFGfwyGTRIIISDLS 311
Cdd:cd18574   196 AFAMEDRELELYEEEVEKAAK--LNEKL--GLGIGIfqglsnlaLNGIVLGVLYYG---GSLVSRGELT 257
sufC PRK09580
cysteine desulfurase ATPase component; Reviewed
581-651 2.40e-03

cysteine desulfurase ATPase component; Reviewed


Pssm-ID: 181965 [Multi-domain]  Cd Length: 248  Bit Score: 41.32  E-value: 2.40e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 156095386  581 SGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgNENRITIIIAHRLSTIRYANTIFV 651
Cdd:PRK09580  147 SGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLR-DGKRSFIIVTHYQRILDYIKPDYV 216
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
1355-1399 2.50e-03

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 40.94  E-value: 2.50e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 156095386 1355 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTI 1399
Cdd:PRK13538  128 RQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEALL 172
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
1269-1388 2.51e-03

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 42.35  E-value: 2.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1269 TLF----KNSGKILLDGVDICDYNLKDL-----------RNLFSIVSQEPMLFNMS--IYENIKF----GKENATREDVK 1327
Cdd:PRK15439  308 TLYglrpARGGRIMLNGKEINALSTAQRlarglvylpedRQSSGLYLDAPLAWNVCalTHNRRGFwikpARENAVLERYR 387
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 156095386 1328 RA--CKFAAIDEFIeslpnqydtnvgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLD 1388
Cdd:PRK15439  388 RAlnIKFNHAEQAA---------------RTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD 435
PLN03073 PLN03073
ABC transporter F family; Provisional
400-442 2.71e-03

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 42.15  E-value: 2.71e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 156095386  400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDV 442
Cdd:PLN03073  524 LFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV 566
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
1356-1412 2.77e-03

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: 42.31  E-value: 2.77e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 156095386  1356 SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIIT 1412
Cdd:TIGR01257 2070 TYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLT 2126
PRK15093 PRK15093
peptide ABC transporter ATP-binding protein SapD;
1352-1428 3.03e-03

peptide ABC transporter ATP-binding protein SapD;


Pssm-ID: 185049 [Multi-domain]  Cd Length: 330  Bit Score: 41.71  E-value: 3.03e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156095386 1352 PYgkSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASI-KRSDKIVV 1428
Cdd:PRK15093  156 PY--ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLsQWADKINV 231
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
578-614 3.48e-03

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 41.64  E-value: 3.48e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 156095386  578 SKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS 614
Cdd:PRK11819  162 TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
1326-1413 3.78e-03

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


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 42.02  E-value: 3.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  1326 VKRACKFAAIDEFIESLP-NQY-DTNVGPYGKSLSGGQKQRIAIARALLREPKILL-LDEATSSLDSNSEKLIEKTIVDI 1402
Cdd:TIGR00956  869 VSKSEKMEYVEEVIKLLEmESYaDAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKL 948
                           90
                   ....*....|.
gi 156095386  1403 KDKADKTIITI 1413
Cdd:TIGR00956  949 ADHGQAILCTI 959
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
569-616 3.81e-03

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


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 42.02  E-value: 3.81e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 156095386   569 YETLVGSNASK-LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEY 616
Cdd:TIGR00956  198 RNTKVGNDFVRgVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSATAL 246
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
578-611 5.44e-03

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: 39.94  E-value: 5.44e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 156095386  578 SKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:cd03233   117 RGISGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
374-447 5.58e-03

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: 41.07  E-value: 5.58e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 156095386   374 GKKLKDiKKIQFKNVRFHYDTRKdveIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDS 447
Cdd:TIGR03719  315 GPRLGD-KVIEAENLTKAFGDKL---LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGET 384
AAA_15 pfam13175
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
380-685 5.88e-03

AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.


Pssm-ID: 433011 [Multi-domain]  Cd Length: 392  Bit Score: 40.66  E-value: 5.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   380 IKKIQFKNVRFHydtrKDVEIYKDLNFTLtegktyaFVGESGCGKSTILKLIERLYDPTEgdviindSHNLKDVNLKWWR 459
Cdd:pfam13175    3 IKSIIIKNFRCL----KDTEIDLDEDLTV-------LIGKNNSGKSSILEALDIFLNNKE-------KFFEDDFLVLYLK 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   460 SKIGVVSQDPLLFSNSIKNN---IKYSLYSLKDLEALSEESNEDGFSSQSDSNSRNSCRAKCAGDLNDMIQTTDSTelIQ 536
Cdd:pfam13175   65 DVIKIDKEDLNIFENISFSIdieIDVEFLLILFGYLEIKKKYLCLASKGKAKEYEKTLHPKGANKADLLLELKISD--LK 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   537 VRKNYETIEDSEVVSVSKKVLIHDFVSALPDKYETLVGSNASKlsggqkqrisiaraiirnPKILILDEATSSLDNKSEY 616
Cdd:pfam13175  143 KYLKQFKIYIYNNYYLDEKKNVFDKKSKYELPSLKEEFLNSEK------------------EEIKVDKEDLKKLINELEK 204
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 156095386   617 LVQKTINNLKGNENRITIIIAHRlstiryantifvlSNRENGSTVDVDVLGEDPTKDSNEKNEKHDKQE 685
Cdd:pfam13175  205 SINYHENVLENLQIKKLLISADR-------------NASDEDSEKINSLLGALKQRIFEEALQEELELT 260
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
400-615 6.04e-03

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: 39.78  E-value: 6.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDVIINDShNLKDVNLKWWRSKIGVVSQdpllfsnsikNN 479
Cdd:cd03231    15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGG-PLDFQRDSIARGLLYLGHA----------PG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  480 IKYSLYSLKDLEALSeesnedgfssqsDSNSRNSCRakcagdlndmiqttdsTELIQVrkNYETIEDSEVVSvskkvlih 559
Cdd:cd03231    84 IKTTLSVLENLRFWH------------ADHSDEQVE----------------EALARV--GLNGFEDRPVAQ-------- 125
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 156095386  560 dfvsalpdkyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSE 615
Cdd:cd03231   126 --------------------LSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGV 161
ABC_6TM_exporter_like cd18778
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
62-309 6.42e-03

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: 40.21  E-value: 6.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386   62 LGVSFVCATISGGTLPFFVSVFGVIMKNMNLGENVNDII--FSLVLIGIF--QFILSFISSFCMDVVTTKI--------- 128
Cdd:cd18778     1 LILTLLCALLSTLLGLVPPWLIRELVDLVTIGSKSLGLLlgLALLLLGAYllRALLNFLRIYLNHVAEQKVvadlrsdly 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  129 --LKTLKIEFlksvfyqdgqFHDNNPG---SKLTSDLDfYLEQVNA-GIGTKFITIFTyasaFLGLYIWSLFKNARLTLc 202
Cdd:cd18778    81 dkLQRLSLRY----------FDDRQTGdlmSRVINDVA-NVERLIAdGIPQGITNVLT----LVGVAIILFSINPKLAL- 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  203 ITCV-FPLIYICGVICNKKV----KINKKTSLLYNnntmSIIEEALVGIRTVVSYCGENTILKKFN-LSEKlYSKYTLKA 276
Cdd:cd18778   145 LTLIpIPFLALGAWLYSKKVrpryRKVREALGELN----ALLQDNLSGIREIQAFGREEEEAKRFEaLSRR-YRKAQLRA 219
                         250       260       270
                  ....*....|....*....|....*....|...
gi 156095386  277 NLMESLHIGMINGFILASYAFGFWYGTRIIISD 309
Cdd:cd18778   220 MKLWAIFHPLMEFLTSLGTVLVLGFGGRLVLAG 252
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
1293-1388 6.65e-03

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 40.88  E-value: 6.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1293 RNLFsivsqePMLfnmSIYENIKF-----GKENATREdvkrackfAAIDEFIESlpnqydTNVGPY-----GKsLSGGQK 1362
Cdd:NF033858   87 KNLY------PTL---SVFENLDFfgrlfGQDAAERR--------RRIDELLRA------TGLAPFadrpaGK-LSGGMK 142
                          90       100
                  ....*....|....*....|....*.
gi 156095386 1363 QRIAIARALLREPKILLLDEATSSLD 1388
Cdd:NF033858  143 QKLGLCCALIHDPDLLILDEPTTGVD 168
ABC_6TM_Tm287_like cd18548
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ...
192-346 6.80e-03

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: 40.07  E-value: 6.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  192 SLFKNARLTLCITCVFPLIYICGVICNKKV-----KINKKTSLLynNNtmsIIEEALVGIRTVVSYCGENTILKKFNLSE 266
Cdd:cd18548   134 AFRINPKLALILLVAIPILALVVFLIMKKAiplfkKVQKKLDRL--NR---VVRENLTGIRVIRAFNREDYEEERFDKAN 208
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  267 KLYSKYTLKAN-LMESLHIGM---INGFILASYAFGfwyGTRIIISDLSNqqpnndfhgGSVISI---LLGVLISMFMLT 339
Cdd:cd18548   209 DDLTDTSLKAGrLMALLNPLMmliMNLAIVAILWFG---GHLINAGSLQV---------GDLVAFinyLMQILMSLMMLS 276

                  ....*..
gi 156095386  340 IILPNIT 346
Cdd:cd18548   277 MVFVMLP 283
ABC_6TM_Tm287_like cd18548
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ...
865-1101 7.10e-03

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: 40.07  E-value: 7.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  865 KYSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMKLRLFENIMYQEISFFDQDShAPGLlsahINR---DVHLLKTGLV 941
Cdd:cd18548    40 RTGLLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFEKIQSFSFAEIDKFG-TSSL----ITRltnDVTQVQNFVM 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  942 NNIVIFTHFIVLFLVSTVMSFY--------FCPIVAAVLTGTYFIFMRVFAIRARIAANKDvekkRVNQpgtafvynsdd 1013
Cdd:cd18548   115 MLLRMLVRAPIMLIGAIIMAFRinpklaliLLVAIPILALVVFLIMKKAIPLFKKVQKKLD----RLNR----------- 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1014 eifkdpsfLIQEAFYNMNTVIIYGLEDYFCTLIEKAidysNKGQKRKTLINSMLWGFSQSAQFFINSFA----YWFGSFL 1089
Cdd:cd18548   180 --------VVRENLTGIRVIRAFNREDYEEERFDKA----NDDLTDTSLKAGRLMALLNPLMMLIMNLAivaiLWFGGHL 247
                         250
                  ....*....|..
gi 156095386 1090 IRRGTIQVDDFM 1101
Cdd:cd18548   248 INAGSLQVGDLV 259
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
580-611 7.38e-03

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 40.80  E-value: 7.38e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 156095386  580 LSGGQKQRISIARAIIRNPKILILDEATSSLD 611
Cdd:PRK15439  404 LSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD 435
ABC_6TM_ABCC_D2 cd18580
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ...
825-1055 7.45e-03

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: 40.18  E-value: 7.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  825 IAIIALSIMVAGGLYpLFALLYAKYVGTLFDFANLEANSNKYSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMKLRLF 904
Cdd:cd18580     1 VLLLLLLLLLLAFLS-QFSNIWLDWWSSDWSSSPNSSSGYYLGVYAALLVLASVLLVLLRWLLFVLAGLRASRRLHDKLL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  905 ENIMYQEISFFDqdSHAPGLLsahINR---DVHLLKTGLVNNIVIFTHFIVLFLVSTVMSFYFCP---IVAAVLTGTYFI 978
Cdd:cd18580    80 RSVLRAPMSFFD--TTPSGRI---LNRfskDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPyflIVLPPLLVVYYL 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 156095386  979 FMRVFairarIAANKDVekKRVnqpgtafvynsdDEIFKDPSF-LIQEAFYNMNTVIIYGLEDYFCTLIEKAIDYSNK 1055
Cdd:cd18580   155 LQRYY-----LRTSRQL--RRL------------ESESRSPLYsHFSETLSGLSTIRAFGWQERFIEENLRLLDASQR 213
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
574-614 7.51e-03

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 40.49  E-value: 7.51e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 156095386  574 GSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKS 614
Cdd:NF000106  139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRT 179
ABC_6TM_exporter_like cd18550
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
825-991 8.19e-03

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: 40.16  E-value: 8.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  825 IAIIALSIMVAGGLYPLFALLYAKyvgtLFDFANLEANS---NKYSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMKL 901
Cdd:cd18550     1 LALVLLLILLSALLGLLPPLLLRE----IIDDALPQGDLgllVLLALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  902 RLFENIMYQEISFFdqDSHAPGLLSAHINRDVHLLK-------TGLVNN--IVIFThFIVLFLVS---TVMSFYFCPIva 969
Cdd:cd18550    77 QLYAHLQRMSLAFF--TRTRTGEIQSRLNNDVGGAQsvvtgtlTSVVSNvvTLVAT-LVAMLALDwrlALLSLVLLPL-- 151
                         170       180
                  ....*....|....*....|....
gi 156095386  970 avltgtyFIFM--RVFAIRARIAA 991
Cdd:cd18550   152 -------FVLPtrRVGRRRRKLTR 168
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
1355-1452 8.59e-03

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 40.65  E-value: 8.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386 1355 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSeklIEkTIVDIKDKADKTIITIAH----------RIASIKrSD 1424
Cdd:PRK15064  437 KVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMES---IE-SLNMALEKYEGTLIFVSHdrefvsslatRIIEIT-PD 511
                          90       100
                  ....*....|....*....|....*...
gi 156095386 1425 KIVVFnnpdrtgsfvqaQGTHEELLSVQ 1452
Cdd:PRK15064  512 GVVDF------------SGTYEEYLRSQ 527
ABC_6TM_exporter_like cd18540
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
186-308 8.68e-03

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: 39.77  E-value: 8.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  186 LGLYIWSLFKNARLTLCITCVFPLIYICGVICNKKV--------KINKKTSLLYNnntmsiieEALVGIRTVVSYCGENT 257
Cdd:cd18540   131 IGILIVMLILNWKLALIVLAVVPVLAVVSIYFQKKIlkayrkvrKINSRITGAFN--------EGITGAKTTKTLVREEK 202
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 156095386  258 ILKKF-NLSEKLYsKYTLKANLMESLHIGMINGFILASYAFGFWYGTRIIIS 308
Cdd:cd18540   203 NLREFkELTEEMR-RASVRAARLSALFLPIVLFLGSIATALVLWYGGILVLA 253
ABC_6TM_ABCC_D1 cd18579
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ...
841-1078 9.16e-03

Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 1 (TMD1)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. ABC transporters typically consist 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: 350023 [Multi-domain]  Cd Length: 289  Bit Score: 39.78  E-value: 9.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  841 LFALLY--AKYVGTLF-----DFANLEANSNKYSLYILVIAI--AMFISETLKNYYN---NVIGEKV---------EKTM 899
Cdd:cd18579     4 LLKLLEdlLSLAQPLLlglliSYLSSYPDEPLSEGYLLALALflVSLLQSLLLHQYFflsFRLGMRVrsalssliyRKAL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  900 KLrlfenimyqeiSFFDQDSHAPG----LLSAHINRdvhllktglVNNIVIFTHFIVLFLVSTVMSFY----------FC 965
Cdd:cd18579    84 RL-----------SSSARQETSTGeivnLMSVDVQR---------IEDFFLFLHYLWSAPLQIIVALYllyrllgwaaLA 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  966 PIVAAVLT--GTYFIFMRVFAIRARIAANKDvekKRVNqpgtafvynsddeifkdpsfLIQEAFYNMNTVIIYGLEDYFC 1043
Cdd:cd18579   144 GLGVLLLLipLQAFLAKLISKLRKKLMKATD---ERVK--------------------LTNEILSGIKVIKLYAWEKPFL 200
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 156095386 1044 TLIEKAIDYSNKGQKRKTLINSMLWGFSQSAQFFI 1078
Cdd:cd18579   201 KRIEELRKKELKALRKFGYLRALNSFLFFSTPVLV 235
ABC_6TM_PrtD_LapB_HlyB_like cd18783
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ...
824-986 9.71e-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: 39.81  E-value: 9.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  824 DIAIIALSIMVagglyplFALLYAKYVGTLFDFA-NLEANSNKYSLYILVIAIAMFisET----LKNYYNNVIGEKVEKT 898
Cdd:cd18783     6 DVAIASLILHV-------LALAPPIFFQIVIDKVlVHQSYSTLYVLTIGVVIALLF--EGilgyLRRYLLLVATTRIDAR 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 156095386  899 MKLRLFENIMYQEISFFDQdsHAPGLLSAHIN-----RDV---HLLKTGL-VNNIVIFthFIVLFLVSTVMSFY---FCP 966
Cdd:cd18783    77 LALRTFDRLLSLPIDFFER--TPAGVLTKHMQqieriRQFltgQLFGTLLdATSLLVF--LPVLFFYSPTLALVvlaFSA 152
                         170       180
                  ....*....|....*....|
gi 156095386  967 IVAAVLtgtyFIFMRVFAIR 986
Cdd:cd18783   153 LIALII----LAFLPPFRRR 168
 
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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