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Conserved domains on  [gi|2506117|sp|P36370|]
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RecName: Full=Antigen peptide transporter 1; Short=APT1; AltName: Full=ATP-binding cassette sub-family B member 2; AltName: Full=Peptide transporter TAP1

Protein Classification

ABC transporter permease/ATP-binding protein( domain architecture ID 11490025)

ABC transporter family protein containing permease (a six-transmembrane helical domain) and ATP-binding components functions as an ATP-dependent transporter, similar to ABC transporter B (ABCB) family members

CATH:  3.40.50.300
EC:  7.5.2.-
SCOP:  4003976
TCDB:  3.A.1

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
2-717 0e+00

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


:

Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 1028.51  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117      2 AAHAWPTAALLLLLVDWLLLRPVLPGIFSLLVP-EVPLLRVWAVGLSRWAILGLGVRGVLGVTAGarGWLAALQPLVAAL 80
Cdd:TIGR00958   1 AALAYLLPWFSLLLVDWALLRDLLQGIFGLLLPfEKGLYVLWLEGTLRLGVLWLGALGILLNKAG--GLLAAVKPLVAAL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117     81 GLALPGLASFRKLSAWGALREGDNAGLLHWNsrldAFVLSYVAALPAAALWHKLGGFWAP-----SGHKGAGDMLCRMLG 155
Cdd:TIGR00958  79 CLATPSLSSLRALAFWEALDPAVRVALGLWS----WFVWSYGAALPAAALWAVLSSAGASekeaeQGQSETADLLFRLLG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    156 FLDSKKGRLHLVLVLLILSCLGEMAIPFFTGRITDWILQDKTAPSFARNMWLMCILTIASTVLEFAGDGIYNITMGHMHS 235
Cdd:TIGR00958 155 LSGRDWPWLISAFVFLTLSSLGEMFIPFYTGRVIDTLGGDKGPPALASAIFFMCLLSIASSVSAGLRGGSFNYTMARINL 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    236 RVHGEVFRAVLHQETGFFLKNPTGSITSRVTEDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTVVTLLSLPLL 315
Cdd:TIGR00958 235 RIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTMVTLINLPLV 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    316 FLLPRRLGKVYQSLAVKVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKEALAYVTEVWTMSVS 395
Cdd:TIGR00958 315 FLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRKALAYAGYLWTTSVL 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    396 GMLLKVGILYLGGQLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKIFEYLDRTPCSPLSGSLAPLN 475
Cdd:TIGR00958 395 GMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLDRKPNIPLTGTLAPLN 474
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    476 MKGLVKFQDVSFAYPNHPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLH 555
Cdd:TIGR00958 475 LEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLH 554
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    556 TQVAAVGQEPLLFGRSFRENIAYGLTRTPtMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALI 635
Cdd:TIGR00958 555 RQVALVGQEPVLFSGSVRENIAYGLTDTP-DEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALV 633
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    636 RKPRLLILDDATSALDAgnqlRVQRLLYESPEWASRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLMERGGCYRS 715
Cdd:TIGR00958 634 RKPRVLILDEATSALDA----ECEQLLQESRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKH 709

                  ..
gi 2506117    716 MV 717
Cdd:TIGR00958 710 LV 711
 
Name Accession Description Interval E-value
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
2-717 0e+00

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 1028.51  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117      2 AAHAWPTAALLLLLVDWLLLRPVLPGIFSLLVP-EVPLLRVWAVGLSRWAILGLGVRGVLGVTAGarGWLAALQPLVAAL 80
Cdd:TIGR00958   1 AALAYLLPWFSLLLVDWALLRDLLQGIFGLLLPfEKGLYVLWLEGTLRLGVLWLGALGILLNKAG--GLLAAVKPLVAAL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117     81 GLALPGLASFRKLSAWGALREGDNAGLLHWNsrldAFVLSYVAALPAAALWHKLGGFWAP-----SGHKGAGDMLCRMLG 155
Cdd:TIGR00958  79 CLATPSLSSLRALAFWEALDPAVRVALGLWS----WFVWSYGAALPAAALWAVLSSAGASekeaeQGQSETADLLFRLLG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    156 FLDSKKGRLHLVLVLLILSCLGEMAIPFFTGRITDWILQDKTAPSFARNMWLMCILTIASTVLEFAGDGIYNITMGHMHS 235
Cdd:TIGR00958 155 LSGRDWPWLISAFVFLTLSSLGEMFIPFYTGRVIDTLGGDKGPPALASAIFFMCLLSIASSVSAGLRGGSFNYTMARINL 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    236 RVHGEVFRAVLHQETGFFLKNPTGSITSRVTEDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTVVTLLSLPLL 315
Cdd:TIGR00958 235 RIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTMVTLINLPLV 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    316 FLLPRRLGKVYQSLAVKVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKEALAYVTEVWTMSVS 395
Cdd:TIGR00958 315 FLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRKALAYAGYLWTTSVL 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    396 GMLLKVGILYLGGQLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKIFEYLDRTPCSPLSGSLAPLN 475
Cdd:TIGR00958 395 GMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLDRKPNIPLTGTLAPLN 474
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    476 MKGLVKFQDVSFAYPNHPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLH 555
Cdd:TIGR00958 475 LEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLH 554
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    556 TQVAAVGQEPLLFGRSFRENIAYGLTRTPtMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALI 635
Cdd:TIGR00958 555 RQVALVGQEPVLFSGSVRENIAYGLTDTP-DEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALV 633
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    636 RKPRLLILDDATSALDAgnqlRVQRLLYESPEWASRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLMERGGCYRS 715
Cdd:TIGR00958 634 RKPRVLILDEATSALDA----ECEQLLQESRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKH 709

                  ..
gi 2506117    716 MV 717
Cdd:TIGR00958 710 LV 711
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
178-719 1.58e-143

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 432.28  E-value: 1.58e-143
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  178 EMAIPFFTGRITDWILQDKTAPSFARNMWLMCILTIASTVLEFAGDGIYNITMGHMHSRVHGEVFRAVLHQETGFFLKNP 257
Cdd:COG1132  37 ELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRR 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  258 TGSITSRVTEDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQSLAVKVQESL 337
Cdd:COG1132 117 TGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEAL 196
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  338 AKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKEALAYVTEVWTMSVSGMLLKVGILYLGGQLVVRGAVS 417
Cdd:COG1132 197 AELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLT 276
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  418 SGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKIFEYLDRTP-CSPLSGSLAPLNMKGLVKFQDVSFAYPnhPNVQ 496
Cdd:COG1132 277 VGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPeIPDPPGAVPLPPVRGEIEFENVSFSYP--GDRP 354
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  497 VLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQVAAVGQEPLLFGRSFRENI 576
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENI 434
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  577 AYGLtRTPTMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQL 656
Cdd:COG1132 435 RYGR-PDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEA 513
                       490       500       510       520       530       540
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2506117  657 RVQRLLYEspEWASRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLMERGGCYRSMVEA 719
Cdd:COG1132 514 LIQEALER--LMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLARGGLYARLYRL 574
ABC_6TM_TAP1 cd18589
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ...
177-455 1.97e-136

Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.


Pssm-ID: 350033 [Multi-domain]  Cd Length: 289  Bit Score: 403.39  E-value: 1.97e-136
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  177 GEMAIPFFTGRITDWILQDKTAPSFARNMWLMCILTIASTVLEFAGDGIYNITMGHMHSRVHGEVFRAVLHQETGFFLKN 256
Cdd:cd18589  11 GEMAIPYYTGRMTDWIMNKDAPEAFTAAITVMSLLTIASAVSEFVCDLIYNITMSRIHSRLQGLVFAAVLRQEIAFFDSN 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  257 PTGSITSRVTEDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQSLAVKVQES 336
Cdd:cd18589  91 QTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQQSLAVQVQKS 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  337 LAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKEALAYVTEVWTMSVSGMLLKVGILYLGGQLVVRGAV 416
Cdd:cd18589 171 LARANQVAVETFSAMKTVRSFANEEGEAQRYRQRLQKTYRLNKKEAAAYAVSMWTSSFSGLALKVGILYYGGQLVTAGTV 250
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 2506117  417 SSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKI 455
Cdd:cd18589 251 SSGDLVTFVLYELQFTSAVEVLLSYYPSVMKAVGSSEKI 289
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
227-713 8.31e-70

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 239.15  E-value: 8.31e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   227 NITMgHMHSRVhgevFRAVLHQETGFFLKNPTGSITSRVTEDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTV 306
Cdd:PRK11176  95 KVVM-TMRRRL----FGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSL 169
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   307 VTLLSLPLLFLLPRRLGKVYQSLAVKVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKEALAYV 386
Cdd:PRK11176 170 ILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRQQGMKMVSASS 249
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   387 TEVWTMSVSGMLLKVGILYLGGQLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKIFEYLDRTPcSP 466
Cdd:PRK11176 250 ISDPIIQLIASLALAFVLYAASFPSVMDTLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFAILDLEQ-EK 328
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   467 LSGSLAPLNMKGLVKFQDVSFAYP--NHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGE 544
Cdd:PRK11176 329 DEGKRVIERAKGDIEFRNVTFTYPgkEVP---ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGH 405
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   545 PLVQYDHHYLHTQVAAVGQEPLLFGRSFRENIAYGLTRTPTMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQ 624
Cdd:PRK11176 406 DLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQ 485
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   625 RQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEwaSRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHL 704
Cdd:PRK11176 486 RQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHA 563

                 ....*....
gi 2506117   705 QLMERGGCY 713
Cdd:PRK11176 564 ELLAQNGVY 572
ABC_membrane pfam00664
ABC transporter transmembrane region; This family represents a unit of six transmembrane ...
177-435 4.00e-55

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: 190.16  E-value: 4.00e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    177 GEMAIPFFTGRITDWILQDKTAPSFARNMWLMC--ILTIASTVLEFAGDGIYNITMGHMHSRVHGEVFRAVLHQETGFFL 254
Cdd:pfam00664  14 ISPAFPLVLGRILDVLLPDGDPETQALNVYSLAllLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLFKKILRQPMSFFD 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    255 KNPTGSITSRVTEDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQSLAVKVQ 334
Cdd:pfam00664  94 TNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVFAKILRKLSRKEQ 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    335 ESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKEALAYVTEVWTMSVSGMLLKVGILYLGGQLVVRG 414
Cdd:pfam00664 174 KAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYALALWFGAYLVISG 253
                         250       260
                  ....*....|....*....|.
gi 2506117    415 AVSSGNLVSFVLYQLQFTRAV 435
Cdd:pfam00664 254 ELSVGDLVAFLSLFAQLFGPL 274
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
488-692 2.20e-22

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 95.38  E-value: 2.20e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   488 AYPNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVlldgeplvqydHHYLHTQVAAVGQ---E 564
Cdd:NF040873   1 GYGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV-----------RRAGGARVAYVPQrseV 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   565 PLLFGRSFRENIAYG------LTRTPTMEEITAV--AMES-GAHDFIsgfpqgyDTEVGEtgnqLSGGQRQAVALARALI 635
Cdd:NF040873  67 PDSLPLTVRDLVAMGrwarrgLWRRLTRDDRAAVddALERvGLADLA-------GRQLGE----LSGGQRQRALLAQGLA 135
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 2506117   636 RKPRLLILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQLSLAERAHHILFL 692
Cdd:NF040873 136 QEADLLLLDEPTTGLDAESRERIIALLAEEHA-RGATVVVVTHDLELVRRADPCVLL 191
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
507-678 1.51e-12

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: 65.86  E-value: 1.51e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117     507 PGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVL-LDGEPLVQYDHHYLHtqvaavgqepllfgrsfreniaygltrtpt 585
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIyIDGEDILEEVLDQLL------------------------------ 50
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117     586 meeitavamesgahdfisgfpqgyDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQ-----R 660
Cdd:smart00382  51 ------------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleelR 106
                          170
                   ....*....|....*...
gi 2506117     661 LLYESPEWASRTVLLITQ 678
Cdd:smart00382 107 LLLLLKSEKNLTVILTTN 124
GguA NF040905
sugar ABC transporter ATP-binding protein;
474-650 6.05e-10

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 62.11  E-value: 6.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   474 LNMKGLVKfqdvSFaypnhPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYqPTG---GKVLLDGEP----- 545
Cdd:NF040905   2 LEMRGITK----TF-----PGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHGsyeGEILFDGEVcrfkd 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   546 LVQYDHH---YLHTQVAAVgqePLLfgrSFRENI-------AYGL-----TRTPTMEEITAVamesgahdfisGFPQGYD 610
Cdd:NF040905  72 IRDSEALgivIIHQELALI---PYL---SIAENIflgneraKRGVidwneTNRRARELLAKV-----------GLDESPD 134
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 2506117   611 TEVGETGNqlsgGQRQAVALARALIRKPRLLILDDATSAL 650
Cdd:NF040905 135 TLVTDIGV----GKQQLVEIAKALSKDVKLLILDEPTAAL 170
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
468-711 8.40e-05

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 45.50  E-value: 8.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   468 SGSLAPLNMKGLVKfqdvsfaypNHPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTvAALLQNLYQPTGGKvlldgEP-- 545
Cdd:NF000106   8 NGARNAVEVRGLVK---------HFGEVKAVDGVDLDVREGTVLGVLGP*GAA**R-GALPAHV*GPDAGR-----RPwr 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   546 LVQYDHHYLHTQVAAVGQEPLLFGR----SFRENIaYGLTRTPTMEEITAVAMesgAHDFISGFpqGYDTEVGETGNQLS 621
Cdd:NF000106  73 F*TWCANRRALRRTIG*HRPVR*GRresfSGRENL-YMIGR*LDLSRKDARAR---ADELLERF--SLTEAAGRAAAKYS 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   622 GGQRQAVALARALIRKPRLLILDDATSALDAgnqlRVQRLLYESPEWASR---TVLLITQQLSLAER-AHHILFLKEGSV 697
Cdd:NF000106 147 GGMRRRLDLAASMIGRPAVLYLDEPTTGLDP----RTRNEVWDEVRSMVRdgaTVLLTTQYMEEAEQlAHELTVIDRGRV 222
                        250
                 ....*....|....
gi 2506117   698 CEQGTHLQLMERGG 711
Cdd:NF000106 223 IADGKVDELKTKVG 236
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
480-712 4.92e-04

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 43.57  E-value: 4.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   480 VKFQDVSFAYPNhpnVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLqnlyqpTGGKVLLDGEPLV----QYDHHYLh 555
Cdd:NF033858   2 ARLEGVSHRYGK---TVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLI------AGARKIQQGRVEVlggdMADARHR- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   556 tqvAAVGQE----PLLFGR------SFRENIA-----YGLTRTPTMEEITAVAMESGAHDFISGfPQGydtevgetgnQL 620
Cdd:NF033858  72 ---RAVCPRiaymPQGLGKnlyptlSVFENLDffgrlFGQDAAERRRRIDELLRATGLAPFADR-PAG----------KL 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   621 SGGQRQAVALARALIRKPRLLILDDATSALD--AGNQ-------LRVQRllyespewASRTVLLITQQLSLAERAHHILF 691
Cdd:NF033858 138 SGGMKQKLGLCCALIHDPDLLILDEPTTGVDplSRRQfwelidrIRAER--------PGMSVLVATAYMEEAERFDWLVA 209
                        250       260
                 ....*....|....*....|.
gi 2506117   692 LKEGSVCEQGTHLQLMERGGC 712
Cdd:NF033858 210 MDAGRVLATGTPAELLARTGA 230
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
515-651 5.69e-04

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 43.19  E-value: 5.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   515 GPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLvqyDHHYLHT--QVAAVGQEPLLFGR-SFRENIA-----YGLTRTPTM 586
Cdd:NF033858 299 GSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV---DAGDIATrrRVGYMSQAFSLYGElTVRQNLElharlFHLPAAEIA 375
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2506117   587 EEITAVAMESGAHDFISGFPqgydtevgetgNQLSGGQRQAVALARALIRKPRLLILDDATSALD 651
Cdd:NF033858 376 ARVAEMLERFDLADVADALP-----------DSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
 
Name Accession Description Interval E-value
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
2-717 0e+00

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 1028.51  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117      2 AAHAWPTAALLLLLVDWLLLRPVLPGIFSLLVP-EVPLLRVWAVGLSRWAILGLGVRGVLGVTAGarGWLAALQPLVAAL 80
Cdd:TIGR00958   1 AALAYLLPWFSLLLVDWALLRDLLQGIFGLLLPfEKGLYVLWLEGTLRLGVLWLGALGILLNKAG--GLLAAVKPLVAAL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117     81 GLALPGLASFRKLSAWGALREGDNAGLLHWNsrldAFVLSYVAALPAAALWHKLGGFWAP-----SGHKGAGDMLCRMLG 155
Cdd:TIGR00958  79 CLATPSLSSLRALAFWEALDPAVRVALGLWS----WFVWSYGAALPAAALWAVLSSAGASekeaeQGQSETADLLFRLLG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    156 FLDSKKGRLHLVLVLLILSCLGEMAIPFFTGRITDWILQDKTAPSFARNMWLMCILTIASTVLEFAGDGIYNITMGHMHS 235
Cdd:TIGR00958 155 LSGRDWPWLISAFVFLTLSSLGEMFIPFYTGRVIDTLGGDKGPPALASAIFFMCLLSIASSVSAGLRGGSFNYTMARINL 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    236 RVHGEVFRAVLHQETGFFLKNPTGSITSRVTEDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTVVTLLSLPLL 315
Cdd:TIGR00958 235 RIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTMVTLINLPLV 314
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    316 FLLPRRLGKVYQSLAVKVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKEALAYVTEVWTMSVS 395
Cdd:TIGR00958 315 FLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRKALAYAGYLWTTSVL 394
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    396 GMLLKVGILYLGGQLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKIFEYLDRTPCSPLSGSLAPLN 475
Cdd:TIGR00958 395 GMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLDRKPNIPLTGTLAPLN 474
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    476 MKGLVKFQDVSFAYPNHPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLH 555
Cdd:TIGR00958 475 LEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLH 554
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    556 TQVAAVGQEPLLFGRSFRENIAYGLTRTPtMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALI 635
Cdd:TIGR00958 555 RQVALVGQEPVLFSGSVRENIAYGLTDTP-DEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALV 633
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    636 RKPRLLILDDATSALDAgnqlRVQRLLYESPEWASRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLMERGGCYRS 715
Cdd:TIGR00958 634 RKPRVLILDEATSALDA----ECEQLLQESRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKH 709

                  ..
gi 2506117    716 MV 717
Cdd:TIGR00958 710 LV 711
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
178-719 1.58e-143

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 432.28  E-value: 1.58e-143
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  178 EMAIPFFTGRITDWILQDKTAPSFARNMWLMCILTIASTVLEFAGDGIYNITMGHMHSRVHGEVFRAVLHQETGFFLKNP 257
Cdd:COG1132  37 ELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRR 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  258 TGSITSRVTEDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQSLAVKVQESL 337
Cdd:COG1132 117 TGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEAL 196
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  338 AKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKEALAYVTEVWTMSVSGMLLKVGILYLGGQLVVRGAVS 417
Cdd:COG1132 197 AELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLT 276
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  418 SGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKIFEYLDRTP-CSPLSGSLAPLNMKGLVKFQDVSFAYPnhPNVQ 496
Cdd:COG1132 277 VGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPeIPDPPGAVPLPPVRGEIEFENVSFSYP--GDRP 354
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  497 VLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQVAAVGQEPLLFGRSFRENI 576
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENI 434
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  577 AYGLtRTPTMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQL 656
Cdd:COG1132 435 RYGR-PDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEA 513
                       490       500       510       520       530       540
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2506117  657 RVQRLLYEspEWASRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLMERGGCYRSMVEA 719
Cdd:COG1132 514 LIQEALER--LMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLARGGLYARLYRL 574
ABC_6TM_TAP1 cd18589
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ...
177-455 1.97e-136

Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.


Pssm-ID: 350033 [Multi-domain]  Cd Length: 289  Bit Score: 403.39  E-value: 1.97e-136
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  177 GEMAIPFFTGRITDWILQDKTAPSFARNMWLMCILTIASTVLEFAGDGIYNITMGHMHSRVHGEVFRAVLHQETGFFLKN 256
Cdd:cd18589  11 GEMAIPYYTGRMTDWIMNKDAPEAFTAAITVMSLLTIASAVSEFVCDLIYNITMSRIHSRLQGLVFAAVLRQEIAFFDSN 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  257 PTGSITSRVTEDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQSLAVKVQES 336
Cdd:cd18589  91 QTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQQSLAVQVQKS 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  337 LAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKEALAYVTEVWTMSVSGMLLKVGILYLGGQLVVRGAV 416
Cdd:cd18589 171 LARANQVAVETFSAMKTVRSFANEEGEAQRYRQRLQKTYRLNKKEAAAYAVSMWTSSFSGLALKVGILYYGGQLVTAGTV 250
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 2506117  417 SSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKI 455
Cdd:cd18589 251 SSGDLVTFVLYELQFTSAVEVLLSYYPSVMKAVGSSEKI 289
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
469-697 4.00e-122

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: 364.10  E-value: 4.00e-122
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  469 GSLAPLNMKGLVKFQDVSFAYPNHPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQ 548
Cdd:cd03248   1 GSLAPDHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  549 YDHHYLHTQVAAVGQEPLLFGRSFRENIAYGLTRTPtMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAV 628
Cdd:cd03248  81 YEHKYLHSKVSLVGQEPVLFARSLQDNIAYGLQSCS-FECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRV 159
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2506117  629 ALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEwaSRTVLLITQQLSLAERAHHILFLKEGSV 697
Cdd:cd03248 160 AIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPE--RRTVLVIAHRLSTVERADQILVLDGGRI 226
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
179-718 9.98e-113

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: 356.45  E-value: 9.98e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  179 MAIPFFTGRITDWILQDKTAPSfarnMWLMCILTIASTVLEFAGDGIYNITMGHMHSRV----HGEVFRAVLHQETGFFL 254
Cdd:COG2274 173 LATPLFTQVVIDRVLPNQDLST----LWVLAIGLLLALLFEGLLRLLRSYLLLRLGQRIdlrlSSRFFRHLLRLPLSFFE 248
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  255 KNPTGSITSRVTeDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQSLAVKVQ 334
Cdd:COG2274 249 SRSVGDLASRFR-DVESIREFLTGSLLTALLDLLFVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREES 327
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  335 ESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKK-EALAYVTEVWTMSVSGMLLkVGILYLGGQLVVR 413
Cdd:COG2274 328 EASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKlRRLSNLLSTLSGLLQQLAT-VALLWLGAYLVID 406
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  414 GAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKIFEYLDRTP-CSPLSGSLAPLNMKGLVKFQDVSFAYPNH 492
Cdd:COG2274 407 GQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDILDLPPeREEGRSKLSLPRLKGDIELENVSFRYPGD 486
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  493 pNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQVAAVGQEPLLFGRSF 572
Cdd:COG2274 487 -SPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTI 565
                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  573 RENIAYGLTrTPTMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDATSALDA 652
Cdd:COG2274 566 RENITLGDP-DATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDA 644
                       490       500       510       520       530       540
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2506117  653 GNQLRVQRLLYEspEWASRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLMERGGCYRSMVE 718
Cdd:COG2274 645 ETEAIILENLRR--LLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQ 708
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
480-719 4.96e-96

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: 297.14  E-value: 4.96e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  480 VKFQDVSFAYPNHPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQVA 559
Cdd:cd03249   1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  560 AVGQEPLLFGRSFRENIAYGLTRtPTMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPR 639
Cdd:cd03249  81 LVSQEPVLFDGTIAENIRYGKPD-ATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPK 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  640 LLILDDATSALDAGNQLRVQRLLYESPEwaSRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLMERGGCYRSMVEA 719
Cdd:cd03249 160 ILLLDEATSALDAESEKLVQEALDRAMK--GRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKA 237
MsbA_rel TIGR02204
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ...
241-718 2.91e-94

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: 304.32  E-value: 2.91e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    241 VFRAVLHQETGFFLKNPTGSITSRVTEDT----SNVCESISDKLNLFLWYLGRglclLAFMIWGSFYLTVVTLLSLPLLF 316
Cdd:TIGR02204  97 VFAHLISLSPSFFDKNRSGEVVSRLTTDTtllqSVIGSSLSMALRNALMCIGG----LIMMFITSPKLTSLVLLAVPLVL 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    317 LLPRRLGKVYQSLAVKVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKK--EALAYVTE-VWTMS 393
Cdd:TIGR02204 173 LPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVEKAYEAARQriRTRALLTAiVIVLV 252
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    394 VSGMllkVGILYLGGQLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKIFEYLDRTP--CSPLSGSL 471
Cdd:TIGR02204 253 FGAI---VGVLWVGAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGAAERLIELLQAEPdiKAPAHPKT 329
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    472 APLNMKGLVKFQDVSFAYPNHPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDH 551
Cdd:TIGR02204 330 LPVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDP 409
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    552 HYLHTQVAAVGQEPLLFGRSFRENIAYGLTRTpTMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALA 631
Cdd:TIGR02204 410 AELRARMALVPQDPVLFAASVMENIRYGRPDA-TDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIA 488
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    632 RALIRKPRLLILDDATSALDAGNQLRVQRLLYESpeWASRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLMERGG 711
Cdd:TIGR02204 489 RAILKDAPILLLDEATSALDAESEQLVQQALETL--MKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGG 566

                  ....*..
gi 2506117    712 CYRSMVE 718
Cdd:TIGR02204 567 LYARLAR 573
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
239-713 2.77e-90

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: 293.55  E-value: 2.77e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    239 GEVFRAVLHQETGFFLKNPTGSITSRVTEDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTVVTLLSLPLLFLL 318
Cdd:TIGR02203  91 VRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLTLIVVVMLPVLSIL 170
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    319 PRRLGKVYQSLAVKVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKF-----RQKLEEMKPLNKKEALAYVTEVWTMS 393
Cdd:TIGR02203 171 MRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFdavsnRNRRLAMKMTSAGSISSPITQLIASL 250
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    394 VSGMLLkvgilYLGGQLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKIFEYLDRTPcSPLSGSLAP 473
Cdd:TIGR02203 251 ALAVVL-----FIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPP-EKDTGTRAI 324
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    474 LNMKGLVKFQDVSFAYPNHpNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHY 553
Cdd:TIGR02203 325 ERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLAS 403
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    554 LHTQVAAVGQEPLLFGRSFRENIAYGLTRTPTMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARA 633
Cdd:TIGR02203 404 LRRQVALVSQDVVLFNDTIANNIAYGRTEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARA 483
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    634 LIRKPRLLILDDATSALDAGNQLRVQRLLYESPEwaSRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLMERGGCY 713
Cdd:TIGR02203 484 LLKDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNGLY 561
ABC_6TM_TAP cd18572
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ...
177-455 8.35e-81

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: 259.01  E-value: 8.35e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  177 GEMAIPFFTGRITDWILQDKTAPSFARNMWLMCILTIASTVLEFAGDGIYNITMGHMHSRVHGEVFRAVLHQETGFFLKN 256
Cdd:cd18572  11 SELAIPHYTGAVIDAVVADGSREAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDAT 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  257 PTGSITSRVTEDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQSLAVKVQES 336
Cdd:cd18572  91 KTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRYYRKLSKEIQDA 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  337 LAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKEALAYVTEVWTMSVSGMLLKVGILYLGGQLVVRGAV 416
Cdd:cd18572 171 LAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFYGGHLVLSGRM 250
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 2506117  417 SSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKI 455
Cdd:cd18572 251 SAGQLVTFMLYQQQLGEAFQSLGDVFSSLMQAVGAAEKV 289
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
345-711 1.22e-78

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: 262.39  E-value: 1.22e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  345 LEALSAMPTVRSFANEEGEAQKFRQKLEE-----MKPLnkKEAL--AYVTEVWTM-SVSGMLLKVGILYLGGQLVVRGAV 416
Cdd:COG4988 201 LDRLRGLTTLKLFGRAKAEAERIAEASEDfrkrtMKVL--RVAFlsSAVLEFFASlSIALVAVYIGFRLLGGSLTLFAAL 278
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  417 ssgnlvsFVLYqLqftrAVEVLLSI-------YPSMQkSVGASEKIFEYLDRTPCSPLSGSL-APLNMKGLVKFQDVSFA 488
Cdd:COG4988 279 -------FVLL-L----APEFFLPLrdlgsfyHARAN-GIAAAEKIFALLDAPEPAAPAGTApLPAAGPPSIELEDVSFS 345
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  489 YPNHPNVqvLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQVAAVGQEPLLF 568
Cdd:COG4988 346 YPGGRPA--LDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLF 423
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  569 GRSFRENIAYGlTRTPTMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDATS 648
Cdd:COG4988 424 AGTIRENLRLG-RPDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTA 502
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2506117  649 ALDAGNQLRVQRLLYESpeWASRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLMERGG 711
Cdd:COG4988 503 HLDAETEAEILQALRRL--AKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
ABC_6TM_ABCB9_like cd18784
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ...
177-455 1.35e-76

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


Pssm-ID: 350057 [Multi-domain]  Cd Length: 289  Bit Score: 247.99  E-value: 1.35e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  177 GEMAIPFFTGRITDWILQDKTAPSFARNMWLMCILTIASTVleFAG--DGIYNITMGHMHSRVHGEVFRAVLHQETGFFL 254
Cdd:cd18784  11 GEIFIPYYTGQVIDGIVIEKSQDKFSRAIIIMGLLAIASSV--AAGirGGLFTLAMARLNIRIRNLLFRSIVSQEIGFFD 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  255 KNPTGSITSRVTEDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQSLAVKVQ 334
Cdd:cd18784  89 TVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYYKKLSKAVQ 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  335 ESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKEALAYVTEVWTMSVSGMLLKVGILYLGGQLVVRG 414
Cdd:cd18784 169 DSLAKANEVAEETISSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEALAYGGYVWSNELTELALTVSTLYYGGHLVITG 248
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 2506117  415 AVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKI 455
Cdd:cd18784 249 QISGGNLISFILYQLELGSCLESVGSVYTGLMQAVGAAEKV 289
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
353-716 6.70e-76

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: 256.29  E-value: 6.70e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  353 TVRSFANEEGEAQKFRQKLEEmkplnkKEALAyvTEVWTmsvSGMLLKVG-----------ILYLGGQLVVRGAVSSGNL 421
Cdd:COG5265 230 TVKYFGNEAREARRYDEALAR------YERAA--VKSQT---SLALLNFGqaliialgltaMMLMAAQGVVAGTMTVGDF 298
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  422 VSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKIFEYLDRTPCSPLSGSLAPLNMK-GLVKFQDVSFAYpnHPNVQVLQG 500
Cdd:COG5265 299 VLVNAYLIQLYIPLNFLGFVYREIRQALADMERMFDLLDQPPEVADAPDAPPLVVGgGEVRFENVSFGY--DPERPILKG 376
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  501 LTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQVAAVGQEPLLFGRSFRENIAYGl 580
Cdd:COG5265 377 VSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYG- 455
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  581 tRtP--TMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRV 658
Cdd:COG5265 456 -R-PdaSEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAI 533
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 2506117  659 QRLLYESPEwaSRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLMERGGCYRSM 716
Cdd:COG5265 534 QAALREVAR--GRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQM 589
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
478-711 3.75e-75

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: 242.13  E-value: 3.75e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  478 GLVKFQDVSFAY-PNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHT 556
Cdd:cd03254   1 GEIEFENVNFSYdEKKP---VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRS 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  557 QVAAVGQEPLLFGRSFRENIAYGlTRTPTMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIR 636
Cdd:cd03254  78 MIGVVLQDTFLFSGTIMENIRLG-RPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLR 156
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2506117  637 KPRLLILDDATSALDAGNQLRVQRLLYESPEwaSRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLMERGG 711
Cdd:cd03254 157 DPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
480-716 1.47e-74

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: 240.60  E-value: 1.47e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  480 VKFQDVSFAYPNHPNvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQVA 559
Cdd:cd03251   1 VEFKNVTFRYPGDGP-PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  560 AVGQEPLLFGRSFRENIAYGlTRTPTMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPR 639
Cdd:cd03251  80 LVSQDVFLFNDTVAENIAYG-RPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPP 158
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2506117  640 LLILDDATSALDAGNQLRVQRLLYESPEwaSRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLMERGGCYRSM 716
Cdd:cd03251 159 ILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
type_I_sec_HlyB TIGR01846
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ...
203-716 1.67e-74

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


Pssm-ID: 273831 [Multi-domain]  Cd Length: 694  Bit Score: 254.67  E-value: 1.67e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    203 RNMWLMCILTIASTVL---EFAGDGIYNITMGHMHSRVHGEV----FRAVLHQETGFFLKNPTGSITSRVTEdTSNVCES 275
Cdd:TIGR01846 173 RGLSTLSVLALAMLAVaifEPALGGLRTYLFAHLTSRIDVELgarlYRHLLGLPLGYFESRRVGDTVARVRE-LEQIRNF 251
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    276 ISDKLNLFLWYLGRGLCLLAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQSLAVKVQESLAKSTQVALEALSAMPTVR 355
Cdd:TIGR01846 252 LTGSALTVVLDLLFVVVFLAVMFFYSPTLTGVVIGSLVCYALLSVFVGPILRKRVEDKFERSAAATSFLVESVTGIETIK 331
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    356 SFANEEGEAQKFRQKLEemkplnkkealAYVTEVWTMSVSGMLLKVGI-----------LYLGGQLVVRGAVSSGNLVSF 424
Cdd:TIGR01846 332 ATATEPQFQNRWDRQLA-----------AYVAASFRVTNLGNIAGQAIeliqkltfailLWFGAHLVIGGALSPGQLVAF 400
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    425 VLYQLQFTRAVEVLLSIYPSMQKSVGASEKIFEYLDrTPCSPLSGSLAPL-NMKGLVKFQDVSFAY-PNHPnvQVLQGLT 502
Cdd:TIGR01846 401 NMLAGRVTQPVLRLAQLWQDFQQTGIALERLGDILN-SPTEPRSAGLAALpELRGAITFENIRFRYaPDSP--EVLSNLN 477
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    503 FTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQVAAVGQEPLLFGRSFRENIAYGLTR 582
Cdd:TIGR01846 478 LDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCNPG 557
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    583 TPtMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLL 662
Cdd:TIGR01846 558 AP-FEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNM 636
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2506117    663 YESPewASRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLMERGGCYRSM 716
Cdd:TIGR01846 637 REIC--RGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYARL 688
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
480-716 2.83e-74

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: 239.82  E-value: 2.83e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  480 VKFQDVSFAYpnHPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQVA 559
Cdd:cd03253   1 IEFENVTFAY--DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  560 AVGQEPLLFGRSFRENIAYGlTRTPTMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPR 639
Cdd:cd03253  79 VVPQDTVLFNDTIGYNIRYG-RPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPP 157
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2506117  640 LLILDDATSALDAGNQLRVQRLLYESPewASRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLMERGGCYRSM 716
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDVS--KGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEM 232
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
332-718 3.14e-71

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: 242.75  E-value: 3.14e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  332 KVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKEA-LAYVTEVWTMSVSGMLLkVGILYLGGQL 410
Cdd:COG4987 186 RLAAARAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLArLSALAQALLQLAAGLAV-VAVLWLAAPL 264
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  411 VVRGAVSSGNLVSFVLyqlqFTRAV-EVLLSIYPSMQ---KSVGASEKIFEYLDRTPCSPLSGSLAPLNMKGLVKFQDVS 486
Cdd:COG4987 265 VAAGALSGPLLALLVL----AALALfEALAPLPAAAQhlgRVRAAARRLNELLDAPPAVTEPAEPAPAPGGPSLELEDVS 340
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  487 FAYPNHPNvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQVAAVGQEPL 566
Cdd:COG4987 341 FRYPGAGR-PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPH 419
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  567 LFGRSFRENIAygLTR-TPTMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDD 645
Cdd:COG4987 420 LFDTTLRENLR--LARpDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDE 497
                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2506117  646 ATSALDAGNQLRVQRLLYESpeWASRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLMERGGCYRSMVE 718
Cdd:COG4987 498 PTEGLDAATEQALLADLLEA--LAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRYRQLYQ 568
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
480-718 5.13e-70

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: 228.91  E-value: 5.13e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  480 VKFQDVSFAY-PNHPnvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQV 558
Cdd:cd03252   1 ITFEHVRFRYkPDGP--VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  559 AAVGQEPLLFGRSFRENIAygLTRT-PTMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRK 637
Cdd:cd03252  79 GVVLQENVLFNRSIRDNIA--LADPgMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHN 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  638 PRLLILDDATSALDAGNQLRVQRLLYESpeWASRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLMERGGCYRSMV 717
Cdd:cd03252 157 PRILIFDEATSALDYESEHAIMRNMHDI--CAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLY 234

                .
gi 2506117  718 E 718
Cdd:cd03252 235 Q 235
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
227-713 8.31e-70

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 239.15  E-value: 8.31e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   227 NITMgHMHSRVhgevFRAVLHQETGFFLKNPTGSITSRVTEDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTV 306
Cdd:PRK11176  95 KVVM-TMRRRL----FGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSL 169
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   307 VTLLSLPLLFLLPRRLGKVYQSLAVKVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKEALAYV 386
Cdd:PRK11176 170 ILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRQQGMKMVSASS 249
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   387 TEVWTMSVSGMLLKVGILYLGGQLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKIFEYLDRTPcSP 466
Cdd:PRK11176 250 ISDPIIQLIASLALAFVLYAASFPSVMDTLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFAILDLEQ-EK 328
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   467 LSGSLAPLNMKGLVKFQDVSFAYP--NHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGE 544
Cdd:PRK11176 329 DEGKRVIERAKGDIEFRNVTFTYPgkEVP---ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGH 405
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   545 PLVQYDHHYLHTQVAAVGQEPLLFGRSFRENIAYGLTRTPTMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQ 624
Cdd:PRK11176 406 DLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQ 485
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   625 RQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEwaSRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHL 704
Cdd:PRK11176 486 RQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHA 563

                 ....*....
gi 2506117   705 QLMERGGCY 713
Cdd:PRK11176 564 ELLAQNGVY 572
ABC_6TM_TAP_ABCB8_10_like cd18557
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ...
177-455 9.50e-68

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: 224.75  E-value: 9.50e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  177 GEMAIPFFTGRITDWILQDKTAPSFARNMWLMCILTIASTVLEFAGDGIYNITMGHMHSRVHGEVFRAVLHQETGFFLKN 256
Cdd:cd18557  11 AQLLLPYLIGRLIDTIIKGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLRQEIAFFDKH 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  257 PTGSITSRVTEDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQSLAVKVQES 336
Cdd:cd18557  91 KTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIRKLSKEVQDA 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  337 LAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKEALAYVTEVWTMSVSGMLLKVGILYLGGQLVVRGAV 416
Cdd:cd18557 171 LAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWYGGYLVLSGQL 250
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 2506117  417 SSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKI 455
Cdd:cd18557 251 TVGELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
480-695 4.62e-66

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: 215.71  E-value: 4.62e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  480 VKFQDVSFAYPNHPNvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQVA 559
Cdd:cd03228   1 IEFKNVSFSYPGRPK-PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  560 AVGQEPLLFGRSFRENIaygltrtptmeeitavamesgahdfisgfpqgydtevgetgnqLSGGQRQAVALARALIRKPR 639
Cdd:cd03228  80 YVPQDPFLFSGTIRENI-------------------------------------------LSGGQRQRIAIARALLRDPP 116
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 2506117  640 LLILDDATSALDAGNQLRVQRLLYESPEwaSRTVLLITQQLSLAERAHHILFLKEG 695
Cdd:cd03228 117 ILILDEATSALDPETEALILEALRALAK--GKTVIVIAHRLSTIRDADRIIVLDDG 170
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
344-711 6.06e-63

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 220.60  E-value: 6.06e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   344 ALEALSAMPTVRSFANEEGEAQKFRQKLEEMkplnkkeaLAYVTEV--WTMSVSGM------LLKVGILYLGGQLVVRGA 415
Cdd:PRK13657 198 VSDAIGNVSVVQSYNRIEAETQALRDIADNL--------LAAQMPVlsWWALASVLnraastITMLAILVLGAALVQKGQ 269
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   416 VSSGNLVSFV-LYQLQFTRaVEVLLSIYPSMQKSVGASEKIFEYLDRTPCSPLSGSLAPL-NMKGLVKFQDVSFAYPNHP 493
Cdd:PRK13657 270 LRVGEVVAFVgFATLLIGR-LDQVVAFINQVFMAAPKLEEFFEVEDAVPDVRDPPGAIDLgRVKGAVEFDDVSFSYDNSR 348
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   494 nvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQVAAVGQEPLLFGRSFR 573
Cdd:PRK13657 349 --QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIE 426
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   574 ENIAYGLTrTPTMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDATSALDAG 653
Cdd:PRK13657 427 DNIRVGRP-DATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVE 505
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 2506117   654 NQLRVQRLLYESPEwaSRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLMERGG 711
Cdd:PRK13657 506 TEAKVKAALDELMK--GRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGG 561
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
478-701 1.28e-58

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: 197.81  E-value: 1.28e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  478 GLVKFQDVSFAYPNHPNVqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQ 557
Cdd:cd03245   1 GRIEFRNVSFSYPNQEIP-ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  558 VAAVGQEPLLFGRSFRENIAYGLTRTpTMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRK 637
Cdd:cd03245  80 IGYVPQDVTLFYGTLRDNITLGAPLA-DDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLND 158
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2506117  638 PRLLILDDATSALDAGNQLRVQRLLYESPewASRTVLLITQQLSLAERAHHILFLKEGSVCEQG 701
Cdd:cd03245 159 PPILLLDEPTSAMDMNSEERLKERLRQLL--GDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
252-719 4.09e-58

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


Pssm-ID: 130261 [Multi-domain]  Cd Length: 708  Bit Score: 209.60  E-value: 4.09e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    252 FFLKNPTGSITSRVTeDTSNVCESI-SDKLNLFL--WYLGRGLCLLAFMIWGSFYLTVVTLLSLPLLFLLPRrlgKVYQS 328
Cdd:TIGR01193 246 FFSTRRTGEIVSRFT-DASSIIDALaSTILSLFLdmWILVIVGLFLVRQNMLLFLLSLLSIPVYAVIIILFK---RTFNK 321
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    329 LAVKVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMkpLNKkeALAYV-TEVWTM---SVSGMLLKVGIL 404
Cdd:TIGR01193 322 LNHDAMQANAVLNSSIIEDLNGIETIKSLTSEAERYSKIDSEFGDY--LNK--SFKYQkADQGQQaikAVTKLILNVVIL 397
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    405 YLGGQLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKIFE-YLDRTPCSPLSGSLAPLNMKGLVKFQ 483
Cdd:TIGR01193 398 WTGAYLVMRGKLTLGQLITFNALLSYFLTPLENIINLQPKLQAARVANNRLNEvYLVDSEFINKKKRTELNNLNGDIVIN 477
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    484 DVSFAYPNHPNVqvLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQVAAVGQ 563
Cdd:TIGR01193 478 DVSYSYGYGSNI--LSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQ 555
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    564 EPLLFGRSFRENIAYGLTRTPTMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPRLLIL 643
Cdd:TIGR01193 556 EPYIFSGSILENLLLGAKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLIL 635
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2506117    644 DDATSALDAgnqLRVQRLLYESPEWASRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLMERGGCYRSMVEA 719
Cdd:TIGR01193 636 DESTSNLDT---ITEKKIVNNLLNLQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLIHN 708
ABC_membrane pfam00664
ABC transporter transmembrane region; This family represents a unit of six transmembrane ...
177-435 4.00e-55

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: 190.16  E-value: 4.00e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    177 GEMAIPFFTGRITDWILQDKTAPSFARNMWLMC--ILTIASTVLEFAGDGIYNITMGHMHSRVHGEVFRAVLHQETGFFL 254
Cdd:pfam00664  14 ISPAFPLVLGRILDVLLPDGDPETQALNVYSLAllLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLFKKILRQPMSFFD 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    255 KNPTGSITSRVTEDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQSLAVKVQ 334
Cdd:pfam00664  94 TNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVFAKILRKLSRKEQ 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    335 ESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKEALAYVTEVWTMSVSGMLLKVGILYLGGQLVVRG 414
Cdd:pfam00664 174 KAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYALALWFGAYLVISG 253
                         250       260
                  ....*....|....*....|.
gi 2506117    415 AVSSGNLVSFVLYQLQFTRAV 435
Cdd:pfam00664 254 ELSVGDLVAFLSLFAQLFGPL 274
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
240-724 1.63e-54

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


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 197.25  E-value: 1.63e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   240 EVFRAVLHQETGFFLKNPTGSITSRVTEDTsnvcESISDklnLFLWYLG---RGLCLLAFMIWGSFYLTVVTLLSLPLLF 316
Cdd:PRK10790 103 DVMDAALRQPLSAFDTQPVGQLISRVTNDT----EVIRD---LYVTVVAtvlRSAALIGAMLVAMFSLDWRMALVAIMIF 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   317 LLPRRLGKVYQSLAV----KVQESLAKSTQVALEALSAMPTVrsfaneegeaQKFRQKLEEMKPLNKKEALAYVTEVWTM 392
Cdd:PRK10790 176 PAVLVVMVIYQRYSTpivrRVRAYLADINDGFNEVINGMSVI----------QQFRQQARFGERMGEASRSHYMARMQTL 245
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   393 SVSGMLLK-----------VGILYLGGqLVVRGAVSSGNLVSFVLYqlqFTRAVEVL--LSIYPSM-QKSVGASEKIFEY 458
Cdd:PRK10790 246 RLDGFLLRpllslfsalilCGLLMLFG-FSASGTIEVGVLYAFISY---LGRLNEPLieLTTQQSMlQQAVVAGERVFEL 321
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   459 LDRtPCSPLSGSLAPLNmKGLVKFQDVSFAYpnHPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGK 538
Cdd:PRK10790 322 MDG-PRQQYGNDDRPLQ-SGRIDIDNVSFAY--RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGE 397
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   539 VLLDGEPLVQYDHHYLHTQVAAVGQEPLLFGRSFRENIAYGltRTPTMEEITAVAMESGAHDFISGFPQGYDTEVGETGN 618
Cdd:PRK10790 398 IRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLG--RDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGN 475
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   619 QLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEwaSRTVLLITQQLSLAERAHHILFLKEGSVC 698
Cdd:PRK10790 476 NLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVRE--HTTLVVIAHRLSTIVEADTILVLHRGQAV 553
                        490       500       510
                 ....*....|....*....|....*....|..
gi 2506117   699 EQGTHLQLMERGGCYRSMV------EALAAPS 724
Cdd:PRK10790 554 EQGTHQQLLAAQGRYWQMYqlqlagEELAASV 585
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
397-697 3.49e-54

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: 195.74  E-value: 3.49e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  397 MLLKVGILYLGGQLVVRGAVSSGNLV--SFVLyqlqfTRA---VEVLLSIYPSMQKSVGASEKIFEYLDRTPCSPLSGSL 471
Cdd:COG4618 250 LLLQSAVLGLGAYLVIQGEITPGAMIaaSILM-----GRAlapIEQAIGGWKQFVSARQAYRRLNELLAAVPAEPERMPL 324
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  472 -APlnmKGLVKFQDVSFAYPNHPNVqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYD 550
Cdd:COG4618 325 pRP---KGRLSVENLTVVPPGSKRP-ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWD 400
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  551 HHYLHTQVAAVGQEPLLFGRSFRENIAygltR--TPTMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAV 628
Cdd:COG4618 401 REELGRHIGYLPQDVELFDGTIAENIA----RfgDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRI 476
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2506117  629 ALARALIRKPRLLILDDATSALD-AGNQLRVQRLLyespEWASR--TVLLITQQLSLAERAHHILFLKEGSV 697
Cdd:COG4618 477 GLARALYGDPRLVVLDEPNSNLDdEGEAALAAAIR----ALKARgaTVVVITHRPSLLAAVDKLLVLRDGRV 544
chvA TIGR01192
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ...
401-719 3.86e-53

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


Pssm-ID: 130260 [Multi-domain]  Cd Length: 585  Bit Score: 193.57  E-value: 3.86e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    401 VGILYLGGQLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKIFEYLDRTPCSPLSGSLAPL-NMKGL 479
Cdd:TIGR01192 255 MCILVIGTVLVIKGELSVGEVIAFIGFANLLIGRLDQMSGFITQIFEARAKLEDFFDLEDSVFQREEPADAPELpNVKGA 334
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    480 VKFQDVSFAYPNhpNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQVA 559
Cdd:TIGR01192 335 VEFRHITFEFAN--SSQGVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESLRKSIA 412
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    560 AVGQEPLLFGRSFRENIAYGLTrTPTMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPR 639
Cdd:TIGR01192 413 TVFQDAGLFNRSIRENIRLGRE-GATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIARAILKNAP 491
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    640 LLILDDATSALDAGNQLRVQRLLYESPEwaSRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLMERGGCYRSMVEA 719
Cdd:TIGR01192 492 ILVLDEATSALDVETEARVKNAIDALRK--NRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQKDGRFYKLLRR 569
ABC_6TM_TAP2 cd18590
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ...
177-455 2.21e-50

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


Pssm-ID: 350034 [Multi-domain]  Cd Length: 289  Bit Score: 177.53  E-value: 2.21e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  177 GEMAIPFFTGRITDWILQDKTAPSFARNMWLMCILTIASTVleFAG--DGIYNITMGHMHSRVHGEVFRAVLHQETGFFL 254
Cdd:cd18590  11 CETFIPYYTGRVIDILGGEYQHNAFTSAIGLMCLFSLGSSL--SAGlrGGLFMCTLSRLNLRLRHQLFSSLVQQDIGFFE 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  255 KNPTGSITSRVTEDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQSLAVKVQ 334
Cdd:cd18590  89 KTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVKTLGMLGFMLSLSWQLTLLTLIEMPLTAIAQKVYNTYHQKLSQAVQ 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  335 ESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKEALAYVTEVWTMSVSGMLLKVGILYLGGQLVVRG 414
Cdd:cd18590 169 DSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTVRAVYLLVRRVLQLGVQVLMLYCGRQLIQSG 248
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 2506117  415 AVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKI 455
Cdd:cd18590 249 HLTTGSLVSFILYQKNLGSYVRTLVYIYGDMLSNVGAAAKV 289
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
407-716 1.73e-49

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


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 182.60  E-value: 1.73e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   407 GGQLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKIFEYLDRTPCSpLSGSLAPLNMKGLVKFQDVS 486
Cdd:PRK10789 242 GSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRIRAMLAEAPVV-KDGSEPVPEGRGELDVNIRQ 320
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   487 FAYPNHpNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQVAAVGQEPL 566
Cdd:PRK10789 321 FTYPQT-DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPF 399
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   567 LFGRSFRENIAYGlTRTPTMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDA 646
Cdd:PRK10789 400 LFSDTVANNIALG-RPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDA 478
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2506117   647 TSALDAGNQlrvQRLLYESPEW-ASRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLMERGGCYRSM 716
Cdd:PRK10789 479 LSAVDGRTE---HQILHNLRQWgEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDM 546
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
449-692 9.85e-49

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: 179.79  E-value: 9.85e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    449 VGASEKIFEYLDRT--PCSPLSGSLAPLNMKglVKFQDVSFAYPNHPNVqvLQGLTFTLYPGKVTALVGPNGSGKSTVAA 526
Cdd:TIGR02857 291 VAAAEALFAVLDAAprPLAGKAPVTAAPASS--LEFSGVSVAYPGRRPA--LRPVSFTVPPGERVALVGPSGAGKSTLLN 366
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    527 LLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQVAAVGQEPLLFGRSFRENIAYGlTRTPTMEEITAVAMESGAHDFISGFP 606
Cdd:TIGR02857 367 LLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLA-RPDASDAEIREALERAGLDEFVAALP 445
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    607 QGYDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEwaSRTVLLITQQLSLAERA 686
Cdd:TIGR02857 446 QGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAALA 523

                  ....*.
gi 2506117    687 HHILFL 692
Cdd:TIGR02857 524 DRIVVL 529
type_I_sec_PrtD TIGR01842
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ...
397-702 2.82e-48

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: 178.70  E-value: 2.82e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    397 MLLKVGILYLGGQLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKIFEYLDRTPCSPLSGSLAplNM 476
Cdd:TIGR01842 236 IVLQSLVLGLGAYLAIDGEITPGMMIAGSILVGRALAPIDGAIGGWKQFSGARQAYKRLNELLANYPSRDPAMPLP--EP 313
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    477 KGLVKFQDVSFAYPNhPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHT 556
Cdd:TIGR01842 314 EGHLSVENVTIVPPG-GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGK 392
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    557 QVAAVGQEPLLFGRSFRENIAYgLTRTPTMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIR 636
Cdd:TIGR01842 393 HIGYLPQDVELFPGTVAENIAR-FGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYG 471
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2506117    637 KPRLLILDDATSALD-AGNQLRVQRLLyeSPEWASRTVLLITQQLSLAERAHHILFLKEGSVCEQGT 702
Cdd:TIGR01842 472 DPKLVVLDEPNSNLDeEGEQALANAIK--ALKARGITVVVITHRPSLLGCVDKILVLQDGRIARFGE 536
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
478-702 4.32e-46

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: 163.43  E-value: 4.32e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  478 GLVKFQDVSFAYPNHPNVqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQ 557
Cdd:cd03244   1 GDIEFKNVSLRYRPNLPP-VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSR 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  558 VAAVGQEPLLFGRSFRENIAygltrtP----TMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARA 633
Cdd:cd03244  80 ISIIPQDPVLFSGTIRSNLD------PfgeySDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARA 153
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2506117  634 LIRKPRLLILDDATSALDAGNQLRVQRLLYEspEWASRTVLLItqqlslaerAHH---------ILFLKEGSVCEQGT 702
Cdd:cd03244 154 LLRKSKILVLDEATASVDPETDALIQKTIRE--AFKDCTVLTI---------AHRldtiidsdrILVLDKGRVVEFDS 220
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
479-702 4.55e-45

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: 161.75  E-value: 4.55e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  479 LVKFQDVSFAYPNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQV 558
Cdd:COG1120   1 MLEAENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  559 AAVGQEPLL-FGRSFRENIAYGltRTPTM----------EEITAVAMES-GAHDFIsgfpqgyDTEVgetgNQLSGGQRQ 626
Cdd:COG1120  78 AYVPQEPPApFGLTVRELVALG--RYPHLglfgrpsaedREAVEEALERtGLEHLA-------DRPV----DELSGGERQ 144
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2506117  627 AVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGT 702
Cdd:COG1120 145 RVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARyADRLVLLKDGRIVAQGP 221
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
498-648 2.03e-44

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: 156.27  E-value: 2.03e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    498 LQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQVAAVGQEPLLFGR-SFRENI 576
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2506117    577 AYGLtrtpTMEEITAVAMESGAHDFISGFPQGY--DTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDATS 648
Cdd:pfam00005  81 RLGL----LLKGLSKREKDARAEEALEKLGLGDlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
480-702 6.31e-44

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: 157.88  E-value: 6.31e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  480 VKFQDVSFAYPNhpNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQVA 559
Cdd:COG1122   1 IELENLSFSYPG--GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  560 AVGQEPL--LFGRSFRENIAYGLTRT----PTMEEITAVAMES-GAHDFISGFPQgydtevgetgnQLSGGQRQAVALAR 632
Cdd:COG1122  79 LVFQNPDdqLFAPTVEEDVAFGPENLglprEEIRERVEEALELvGLEHLADRPPH-----------ELSGGQKQRVAIAG 147
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2506117  633 ALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGT 702
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNK-EGKTVIIVTHDLDLVAElADRVIVLDDGRIVADGT 217
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
442-716 4.61e-43

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 164.63  E-value: 4.61e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   442 YPSMQKSVGASEKIFEYLDrTPCSPLSGSLAPLNMKGLVKFQDVSFAYPNHPNVQVLQGLTFTLYPGKVTALVGPNGSGK 521
Cdd:PRK11174 311 YHAKAQAVGAAESLVTFLE-TPLAHPQQGEKELASNDPVTIEAEDLEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGK 389
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   522 ST-VAALLQNL-YQptgGKVLLDGEPLVQYDHHYLHTQVAAVGQEPLLFGRSFRENIAYGltrTPTM--EEITAVAMESG 597
Cdd:PRK11174 390 TSlLNALLGFLpYQ---GSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLG---NPDAsdEQLQQALENAW 463
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   598 AHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYEspEWASRTVLLIT 677
Cdd:PRK11174 464 VSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNA--ASRRQTTLMVT 541
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 2506117   678 QQLSLAERAHHILFLKEGSVCEQGTHLQLMERGGCYRSM 716
Cdd:PRK11174 542 HQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATL 580
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
362-720 8.40e-43

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 163.84  E-value: 8.40e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   362 GEAQKFRQKLE--EMKPLNKKEALAYVTEVWT---MSVSGMLLkVGILYLGGQLVvRGAVSSGNLVS-FVLYQLQftrAV 435
Cdd:PRK11160 217 GAEDRYRQQLEqtEQQWLAAQRRQANLTGLSQalmILANGLTV-VLMLWLAAGGV-GGNAQPGALIAlFVFAALA---AF 291
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   436 EVLLSIYPSMQ---KSVGASEKIFEYLDRTPCSPLSGSLAPLNMKGLVKFQDVSFAYPNHPNvQVLQGLTFTLYPGKVTA 512
Cdd:PRK11160 292 EALMPVAGAFQhlgQVIASARRINEITEQKPEVTFPTTSTAAADQVSLTLNNVSFTYPDQPQ-PVLKGLSLQIKAGEKVA 370
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   513 LVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQVAAVGQEPLLFGRSFRENIAYGLTrTPTMEEITAV 592
Cdd:PRK11160 371 LLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAP-NASDEALIEV 449
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   593 AMESGAHDFISGfPQGYDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPewASRT 672
Cdd:PRK11160 450 LQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHA--QNKT 526
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 2506117   673 VLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLMERGGCYRSMVEAL 720
Cdd:PRK11160 527 VLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQLKQRL 574
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
395-680 1.15e-42

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: 162.53  E-value: 1.15e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    395 SGMLLKVGILYLGGQLVVRGAVSSGN-----LVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKIFEYLD-----RTPC 464
Cdd:TIGR02868 242 ALTLLAAGLAVLGALWAGGPAVADGRlapvtLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAAERIVEVLDaagpvAEGS 321
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    465 SPLSGSLAPlnMKGLVKFQDVSFAYPNHPnvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGE 544
Cdd:TIGR02868 322 APAAGAVGL--GKPTLELRDLSAGYPGAP--PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGV 397
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    545 PLVQYDHHYLHTQVAAVGQEPLLFGRSFRENIAYGlTRTPTMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQ 624
Cdd:TIGR02868 398 PVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLA-RPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGE 476
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2506117    625 RQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEwaSRTVLLITQQL 680
Cdd:TIGR02868 477 RQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALS--GRTVVLITHHL 530
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
479-701 1.35e-41

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: 151.12  E-value: 1.35e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  479 LVKFQDVSFAYPNHPN-VQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHH---YL 554
Cdd:cd03257   1 LLEVKNLSVSFPTGGGsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRlrkIR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  555 HTQVAAVGQEPLL-------FGRSFRE--NIAYGLTRTPTMEEITAVAMESG--AHDFISGFPqgydtevgetgNQLSGG 623
Cdd:cd03257  81 RKEIQMVFQDPMSslnprmtIGEQIAEplRIHGKLSKKEARKEAVLLLLVGVglPEEVLNRYP-----------HELSGG 149
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2506117  624 QRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQG 701
Cdd:cd03257 150 QRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
481-695 4.51e-41

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 149.20  E-value: 4.51e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  481 KFQDVSFAYPNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQVAA 560
Cdd:COG4619   2 ELEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAY 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  561 VGQEPLLFGRSFRENIAYGLT---RTPTMEEITAvAMESgahdFisGFPQGY-DTEVGEtgnqLSGGQRQAVALARALIR 636
Cdd:COG4619  79 VPQEPALWGGTVRDNLPFPFQlreRKFDRERALE-LLER----L--GLPPDIlDKPVER----LSGGERQRLALIRALLL 147
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  637 KPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEG 695
Cdd:COG4619 148 QPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERvADRVLTLEAG 207
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
480-696 1.09e-40

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


Pssm-ID: 213217 [Multi-domain]  Cd Length: 204  Bit Score: 148.00  E-value: 1.09e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  480 VKFQDVSFAYP--NHPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTV-AALLQNLyQPTGGKVlldgeplvqydhhYLHT 556
Cdd:cd03250   1 ISVEDASFTWDsgEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLlSALLGEL-EKLSGSV-------------SVPG 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  557 QVAAVGQEPLLFGRSFRENIAYGLTRTPTMEE--ITAVAMESgahDfISGFPQGYDTEVGETGNQLSGGQRQAVALARAL 634
Cdd:cd03250  67 SIAYVSQEPWIQNGTIRENILFGKPFDEERYEkvIKACALEP---D-LEILPDGDLTEIGEKGINLSGGQKQRISLARAV 142
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2506117  635 IRKPRLLILDDATSALDAgnqlRVQRLLYES---PEWA-SRTVLLITQQLSLAERAHHILFLKEGS 696
Cdd:cd03250 143 YSDADIYLLDDPLSAVDA----HVGRHIFENcilGLLLnNKTRILVTHQLQLLPHADQIVVLDNGR 204
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
480-709 8.44e-40

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 146.36  E-value: 8.44e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  480 VKFQDVSFAYPNHpnvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQyDHHYLHTQVA 559
Cdd:COG1131   1 IEVRGLTKRYGDK---TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  560 AVGQEPLLFGR-SFRENI-----AYGLTRTPTMEEI----TAVAMESGAHDFISgfpqgydtevgetgnQLSGGQRQAVA 629
Cdd:COG1131  77 YVPQEPALYPDlTVRENLrffarLYGLPRKEARERIdellELFGLTDAADRKVG---------------TLSGGMKQRLG 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  630 LARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGTHLQLME 708
Cdd:COG1131 142 LALALLHDPELLILDEPTSGLDPEARRELWELLRELAA-EGKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELKA 220

                .
gi 2506117  709 R 709
Cdd:COG1131 221 R 221
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
475-718 8.46e-40

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 158.27  E-value: 8.46e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    475 NMKGLVKFQDVSFAYPNHPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLY------------QPTG------ 536
Cdd:PTZ00265 1161 DIKGKIEIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYdlkndhhivfknEHTNdmtneq 1240
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    537 ------------------------------------GKVLLDGEPLVQYDHHYLHTQVAAVGQEPLLFGRSFRENIAYGl 580
Cdd:PTZ00265 1241 dyqgdeeqnvgmknvnefsltkeggsgedstvfknsGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFG- 1319
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    581 TRTPTMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQR 660
Cdd:PTZ00265 1320 KEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEK 1399
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2506117    661 LLYESPEWASRTVLLITQQLSLAERAHHILFL----KEGS-VCEQGTHLQLME-RGGCYRSMVE 718
Cdd:PTZ00265 1400 TIVDIKDKADKTIITIAHRIASIKRSDKIVVFnnpdRTGSfVQAHGTHEELLSvQDGVYKKYVK 1463
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
479-702 1.51e-39

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: 146.10  E-value: 1.51e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  479 LVKFQDVSFAYPNHP-NVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQ 557
Cdd:COG1124   1 MLEVRNLSVSYGQGGrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  558 VAAVGQEPLL-------FGRSFREniAYGLTRTPTMEEITAVAMES-G-AHDFISGFPqgydtevgetgNQLSGGQRQAV 628
Cdd:COG1124  81 VQMVFQDPYAslhprhtVDRILAE--PLRIHGLPDREERIAELLEQvGlPPSFLDRYP-----------HQLSGGQRQRV 147
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2506117  629 ALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGT 702
Cdd:COG1124 148 AIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELT 222
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
480-685 2.53e-39

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: 144.54  E-value: 2.53e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  480 VKFQDVSFAYPN-HPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQydhhyLHTQV 558
Cdd:cd03293   1 LEVRNVSKTYGGgGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG-----PGPDR 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  559 AAVGQEPLLFG-RSFRENIAYGLT-RTPTMEEITAVAMES----GAHDFISGFPQgydtevgetgnQLSGGQRQAVALAR 632
Cdd:cd03293  76 GYVFQQDALLPwLTVLDNVALGLElQGVPKAEARERAEELlelvGLSGFENAYPH-----------QLSGGMRQRVALAR 144
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 2506117  633 ALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLS----LAER 685
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDeavfLADR 201
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
476-709 5.40e-39

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: 151.59  E-value: 5.40e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  476 MKGLVKFQDVSFAYPNHPnVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTG---GKVLLDGEPLVQYDHH 552
Cdd:COG1123   1 MTPLLEVRDLSVRYPGGD-VPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  553 YLHTQVAAVGQEPL--LFGRSFRENIAYGL-TRTPTMEEITAVAMES----GAHDFISGFPQgydtevgetgnQLSGGQR 625
Cdd:COG1123  80 LRGRRIGMVFQDPMtqLNPVTVGDQIAEALeNLGLSRAEARARVLELleavGLERRLDRYPH-----------QLSGGQR 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  626 QAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSL-AERAHHILFLKEGSVCEQGTHL 704
Cdd:COG1123 149 QRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVvAEIADRVVVMDDGRIVEDGPPE 228

                ....*
gi 2506117  705 QLMER 709
Cdd:COG1123 229 EILAA 233
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
450-702 1.53e-38

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: 150.05  E-value: 1.53e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  450 GASEKIFEYLDRTPCSPLSGSLAPLNMKG------LVKFQDVSFAYPNHPN--VQVLQGLTFTLYPGKVTALVGPNGSGK 521
Cdd:COG1123 225 GPPEEILAAPQALAAVPRLGAARGRAAPAaaaaepLLEVRNLSKRYPVRGKggVRAVDDVSLTLRRGETLGLVGESGSGK 304
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  522 STVAALLQNLYQPTGGKVLLDGEPLVQYDH---HYLHTQVAAVGQEPL--LFGR-SFRENIAYGLT--RTPTMEEITAVA 593
Cdd:COG1123 305 STLARLLLGLLRPTSGSILFDGKDLTKLSRrslRELRRRVQMVFQDPYssLNPRmTVGDIIAEPLRlhGLLSRAERRERV 384
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  594 MES----G-AHDFISGFPqgydtevgetgNQLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEW 668
Cdd:COG1123 385 AELlervGlPPDLADRYP-----------HELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRE 453
                       250       260       270
                ....*....|....*....|....*....|....*
gi 2506117  669 ASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGT 702
Cdd:COG1123 454 LGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGP 488
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
483-701 2.16e-38

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: 140.65  E-value: 2.16e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  483 QDVSFAYPNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQVAAVG 562
Cdd:cd03214   3 ENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVP 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  563 QepllfgrsfreniaygltrtptmeeitavAMES-GAHDFIsgfPQGYDTevgetgnqLSGGQRQAVALARALIRKPRLL 641
Cdd:cd03214  80 Q-----------------------------ALELlGLAHLA---DRPFNE--------LSGGERQRVLLARALAQEPPIL 119
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2506117  642 ILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQG 701
Cdd:cd03214 120 LLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARyADRVILLKDGRIVAQG 180
ABC_6TM_ABCB10_like cd18573
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ...
179-455 2.82e-38

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


Pssm-ID: 350017 [Multi-domain]  Cd Length: 294  Bit Score: 144.19  E-value: 2.82e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  179 MAIPFFTGRITDWILQDKT-APSFARNMW-----LMCILTIAS-------TVLEFAGDGIYNitmghmhsRVHGEVFRAV 245
Cdd:cd18573  13 MSVPFAIGKLIDVASKESGdIEIFGLSLKtfalaLLGVFVVGAaanfgrvYLLRIAGERIVA--------RLRKRLFKSI 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  246 LHQETGFFLKNPTGSITSRVTEDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKV 325
Cdd:cd18573  85 LRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRY 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  326 YQSLAVKVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKEALAYVTEVWTMSVSGMLLKVGILY 405
Cdd:cd18573 165 VRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLLSVLY 244
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 2506117  406 LGGQLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKI 455
Cdd:cd18573 245 YGGSLVASGELTVGDLTSFLMYAVYVGSSVSGLSSFYSELMKGLGASSRL 294
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
483-697 3.34e-38

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: 139.66  E-value: 3.34e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  483 QDVSFAYPNHPNVqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQVAAVG 562
Cdd:cd03246   4 ENVSFRYPGAEPP-VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLP 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  563 QEPLLFGRSFRENIaygltrtptmeeitavamesgahdfisgfpqgydtevgetgnqLSGGQRQAVALARALIRKPRLLI 642
Cdd:cd03246  83 QDDELFSGSIAENI-------------------------------------------LSGGQRQRLGLARALYGNPRILV 119
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 2506117  643 LDDATSALDAGNQLRVQRLLyESPEWASRTVLLITQQLSLAERAHHILFLKEGSV 697
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAI-AALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
479-711 5.03e-38

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


Pssm-ID: 443618 [Multi-domain]  Cd Length: 243  Bit Score: 141.92  E-value: 5.03e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  479 LVKFQDVSFAYPNhpnVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLhTQV 558
Cdd:COG4555   1 MIEVENLSKKYGK---VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREAR-RQI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  559 AAVGQEPLLFGR-SFRENIAYGLTRTPTMEEITAVAMESGAHDFisGFPQGYDTEVGEtgnqLSGGQRQAVALARALIRK 637
Cdd:COG4555  77 GVLPDERGLYDRlTVRENIRYFAELYGLFDEELKKRIEELIELL--GLEEFLDRRVGE----LSTGMKKKVALARALVHD 150
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2506117  638 PRLLILDDATSALDAGNQLRVQRLLYespEWAS--RTVLLITQQLSLAER-AHHILFLKEGSVCEQGTHLQLMERGG 711
Cdd:COG4555 151 PKVLLLDEPTNGLDVMARRLLREILR---ALKKegKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
240-692 1.22e-37

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 151.72  E-value: 1.22e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    240 EVFRAVLHQETGFFLKNPTGSITSRVTEDTSNVCESISDK-----------LNLFLWYLGRGlCLLAFMIWGSFYLTVVT 308
Cdd:PTZ00265  135 EFLKSVFYQDGQFHDNNPGSKLTSDLDFYLEQVNAGIGTKfitiftyasafLGLYIWSLFKN-ARLTLCITCVFPLIYIC 213
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    309 LLSLPLLFLLPRRLGKVYQSLAVKVQEslakstqvalEALSAMPTVRSFANEEGEAQKFrqKLEEmKPLNKKEALAYVTE 388
Cdd:PTZ00265  214 GVICNKKVKINKKTSLLYNNNTMSIIE----------EALVGIRTVVSYCGEKTILKKF--NLSE-KLYSKYILKANFME 280
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    389 VWTMS-VSGMLL---KVGILYlGGQLVVRGAVSS--------GNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKIF 456
Cdd:PTZ00265  281 SLHIGmINGFILasyAFGFWY-GTRIIISDLSNQqpnndfhgGSVISILLGVLISMFMLTIILPNITEYMKSLEATNSLY 359
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    457 EYLDRTPCSPLSGSLAPLNMKGLVKFQDVSFAYPNHPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTG 536
Cdd:PTZ00265  360 EIINRKPLVENNDDGKKLKDIKKIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTE 439
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    537 GKVLL-DGEPLVQYDHHYLHTQVAAVGQEPLLFGRSFRENIAYGLTRTPTME---------------------------- 587
Cdd:PTZ00265  440 GDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSLYSLKDLEalsnyynedgndsqenknkrnscrakca 519
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    588 ----------------------------EITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPR 639
Cdd:PTZ00265  520 gdlndmsnttdsneliemrknyqtikdsEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPK 599
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2506117    640 LLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAERAHHILFL 692
Cdd:PTZ00265  600 ILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHRLSTIRYANTIFVL 652
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
481-695 1.39e-37

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: 139.52  E-value: 1.39e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  481 KFQDVSFAYPNHpNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQVAA 560
Cdd:cd03225   1 ELKNLSFSYPDG-ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  561 VGQEP--LLFGRSFRENIAYGL----TRTPTMEEITAVAMEsgahdfisgfpqgydtEVGETG------NQLSGGQRQAV 628
Cdd:cd03225  80 VFQNPddQFFGPTVEEEVAFGLenlgLPEEEIEERVEEALE----------------LVGLEGlrdrspFTLSGGQKQRV 143
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2506117  629 ALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQLS-LAERAHHILFLKEG 695
Cdd:cd03225 144 AIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKA-EGKTIIIVTHDLDlLLELADRVIVLEDG 210
PLN03232 PLN03232
ABC transporter C family member; Provisional
232-719 2.31e-37

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 150.90  E-value: 2.31e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    232 HMHSRVHGEVFRAVLHQETGFFLKNPTGSITSRVTEDTSNVCESISDKLNLF---LWYLgrglcLLAFMIWGSfyLTVVT 308
Cdd:PLN03232  980 HAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFmnqLWQL-----LSTFALIGT--VSTIS 1052
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    309 LLSLPLLFLLPRRLGKVYQSLAVKVQ--ESLAKSTQVAL--EALSAMPTVRSFaneegeaqkfrQKLEEMKPLNKKEALA 384
Cdd:PLN03232 1053 LWAIMPLLILFYAAYLYYQSTSREVRrlDSVTRSPIYAQfgEALNGLSSIRAY-----------KAYDRMAKINGKSMDN 1121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    385 YVTEVWTMSVSGMLLKVGILYLGGQLV-------VRGAVSSGNLVSF-------VLYQLQFTRAVEVLLSIYPSMQKSVG 450
Cdd:PLN03232 1122 NIRFTLANTSSNRWLTIRLETLGGVMIwltatfaVLRNGNAENQAGFastmgllLSYTLNITTLLSGVLRQASKAENSLN 1201
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    451 ASEKIFEYLD------------RTPCS-PLSGSlaplnmkglVKFQDVSFAY-PNHPnvQVLQGLTFTLYPGKVTALVGP 516
Cdd:PLN03232 1202 SVERVGNYIDlpseataiiennRPVSGwPSRGS---------IKFEDVHLRYrPGLP--PVLHGLSFFVSPSEKVGVVGR 1270
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    517 NGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQVAAVGQEPLLFGRSFRENIaygltrTPTMEEITAVAMES 596
Cdd:PLN03232 1271 TGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNI------DPFSEHNDADLWEA 1344
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    597 --GAH--DFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYEspEWASRT 672
Cdd:PLN03232 1345 leRAHikDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIRE--EFKSCT 1422
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*...
gi 2506117    673 VLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLMER-GGCYRSMVEA 719
Cdd:PLN03232 1423 MLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRdTSAFFRMVHS 1470
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
476-677 3.14e-37

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


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 139.84  E-value: 3.14e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  476 MKGLVKFQDVSFAYPNHPN-VQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQydhhyL 554
Cdd:COG1116   4 AAPALELRGVSKRFPTGGGgVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG-----P 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  555 HTQVAAVGQEPLLFG-RSFRENIAYGL-TRTPTMEEITAVAMES----GAHDFISGFPqgydtevgetgNQLSGGQRQAV 628
Cdd:COG1116  79 GPDRGVVFQEPALLPwLTVLDNVALGLeLRGVPKAERRERARELlelvGLAGFEDAYP-----------HQLSGGMRQRV 147
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 2506117  629 ALARALIRKPRLLILDDATSALDAGNQLRVQRLLYEspEWASR--TVLLIT 677
Cdd:COG1116 148 AIARALANDPEVLLMDEPFGALDALTRERLQDELLR--LWQETgkTVLFVT 196
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
480-695 5.04e-37

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: 138.01  E-value: 5.04e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  480 VKFQDVSFAYP-NHPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDH----HYL 554
Cdd:cd03255   1 IELKNLSKTYGgGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEkelaAFR 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  555 HTQVAAVGQEP-LLFGRSFRENIAYGL----TRTPTMEE-----ITAVAMESGAHDFISgfpqgydtevgetgnQLSGGQ 624
Cdd:cd03255  81 RRHIGFVFQSFnLLPDLTALENVELPLllagVPKKERREraeelLERVGLGDRLNHYPS---------------ELSGGQ 145
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2506117  625 RQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAERAHHILFLKEG 695
Cdd:cd03255 146 QQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDG 216
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
481-695 7.72e-37

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


Pssm-ID: 213179 [Multi-domain]  Cd Length: 157  Bit Score: 135.45  E-value: 7.72e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  481 KFQDVSFAYPNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQVAA 560
Cdd:cd00267   1 EIENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  561 VGQepllfgrsfreniaygltrtptmeeitavamesgahdfisgfpqgydtevgetgnqLSGGQRQAVALARALIRKPRL 640
Cdd:cd00267  78 VPQ--------------------------------------------------------LSGGQRQRVALARALLLNPDL 101
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 2506117  641 LILDDATSALDAGNQLRVQRLLYESPEWAsRTVLLITQQLSLAERA-HHILFLKEG 695
Cdd:cd00267 102 LLLDEPTSGLDPASRERLLELLRELAEEG-RTVIIVTHDPELAELAaDRVIVLKDG 156
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
480-701 4.47e-36

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: 135.77  E-value: 4.47e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  480 VKFQDVSFAYPNHpnvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLY-----QPTGGKVLLDGEPL--VQYDHH 552
Cdd:cd03260   1 IELRDLNVYYGDK---HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIydLDVDVL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  553 YLHTQVAAVGQEPLLFGRSFRENIAYGLT-----RTPTMEEITAVAMESGahdfisgfpqGYDTEVGE--TGNQLSGGQR 625
Cdd:cd03260  78 ELRRRVGMVFQKPNPFPGSIYDNVAYGLRlhgikLKEELDERVEEALRKA----------ALWDEVKDrlHALGLSGGQQ 147
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2506117  626 QAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEwaSRTVLLITQQLSLAER-AHHILFLKEGSVCEQG 701
Cdd:cd03260 148 QRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKK--EYTIVIVTHNMQQAARvADRTAFLLNGRLVEFG 222
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
482-701 2.70e-35

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: 131.67  E-value: 2.70e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  482 FQDVSFAYPnHPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHyLHTQVAAV 561
Cdd:cd03247   3 INNVSFSYP-EQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-LSSLISVL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  562 GQEPLLFGRSFRENIaygltrtptmeeitavamesgahdfisgfpqgydtevgetGNQLSGGQRQAVALARALIRKPRLL 641
Cdd:cd03247  81 NQRPYLFDTTLRNNL----------------------------------------GRRFSGGERQRLALARILLQDAPIV 120
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  642 ILDDATSALDAGNQLRVQRLLYESPEwaSRTVLLITQQLSLAERAHHILFLKEGSVCEQG 701
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLK--DKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
236-716 5.71e-35

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: 143.16  E-value: 5.71e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117     236 RVHGEVFRAVLHQETGFFLKNPTGSITSRVTEDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTVVTLLSLPLL 315
Cdd:TIGR00957 1039 VLHQDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVIIPPLGLLY 1118
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117     316 FLLPRRLgkVYQSLAVKVQESLAKSTQVAL--EALSAMPTVRSFANEEGEAQKFRQKLEEmkplNKKEALAYVtevwtms 393
Cdd:TIGR00957 1119 FFVQRFY--VASSRQLKRLESVSRSPVYSHfnETLLGVSVIRAFEEQERFIHQSDLKVDE----NQKAYYPSI------- 1185
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117     394 VSGMLLKVGILYLGGQLVV---------RGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKIFEYLDRTPC 464
Cdd:TIGR00957 1186 VANRWLAVRLECVGNCIVLfaalfavisRHSLSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSETEKE 1265
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117     465 SP--LSGSLAPLNM--KGLVKFQDVSFAYpnHPNVQ-VLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKV 539
Cdd:TIGR00957 1266 APwqIQETAPPSGWppRGRVEFRNYCLRY--REDLDlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEI 1343
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117     540 LLDGEPLVQYDHHYLHTQVAAVGQEPLLFGRSFRENI----AYGltrtptmEEITAVAME-SGAHDFISGFPQGYDTEVG 614
Cdd:TIGR00957 1344 IIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLdpfsQYS-------DEEVWWALElAHLKTFVSALPDKLDHECA 1416
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117     615 ETGNQLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLyeSPEWASRTVLLITQQLSLAERAHHILFLKE 694
Cdd:TIGR00957 1417 EGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTI--RTQFEDCTVLTIAHRLNTIMDYTRVIVLDK 1494
                          490       500
                   ....*....|....*....|..
gi 2506117     695 GSVCEQGTHLQLMERGGCYRSM 716
Cdd:TIGR00957 1495 GEVAEFGAPSNLLQQRGIFYSM 1516
ABC_6TM_exporters cd07346
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ...
178-455 3.25e-34

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


Pssm-ID: 349983 [Multi-domain]  Cd Length: 292  Bit Score: 132.29  E-value: 3.25e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  178 EMAIPFFTGRITDWILQDKTAPSFARNMWLMCILTIASTVLEFAGDGIYNITMGHMHSRVHGEVFRAVLHQETGFFLKNP 257
Cdd:cd07346  15 GLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNR 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  258 TGSITSRVTEDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQSLAVKVQESL 337
Cdd:cd07346  95 TGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRRRIRKASREVRESL 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  338 AKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKealAYVTEVWTMSVSGMLLKVG---ILYLGGQLVVRG 414
Cdd:cd07346 175 AELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLR---AARLSALFSPLIGLLTALGtalVLLYGGYLVLQG 251
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 2506117  415 AVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKI 455
Cdd:cd07346 252 SLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
476-695 4.16e-34

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 130.16  E-value: 4.16e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  476 MKGLVKFQDVSFAYPNHPN-VQVLQGLTFTLYPGKVTALVGPNGSGKST---VAALLQnlyQPTGGKVLLDGEPLVQYDH 551
Cdd:COG1136   1 MSPLLELRNLTKSYGTGEGeVTALRGVSLSIEAGEFVAIVGPSGSGKSTllnILGGLD---RPTSGEVLIDGQDISSLSE 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  552 hylhTQVAA--------VGQEPLLFGR-SFRENIAY-----GLTRTPTMEEITAVAMESGAHDFISGFPqgydtevgetg 617
Cdd:COG1136  78 ----RELARlrrrhigfVFQFFNLLPElTALENVALplllaGVSRKERRERARELLERVGLGDRLDHRP----------- 142
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2506117  618 NQLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAERAHHILFLKEG 695
Cdd:COG1136 143 SQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVIRLRDG 220
ABC_6TM_AtABCB27_like cd18780
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ...
179-455 6.35e-34

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


Pssm-ID: 350053 [Multi-domain]  Cd Length: 295  Bit Score: 131.60  E-value: 6.35e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  179 MAIPFFTGRITDWILQDKTAPSFARN-------MWLMCILTIAST-------VLEFAGDGIYnitmghmhSRVHGEVFRA 244
Cdd:cd18780  13 LALPYFFGQVIDAVTNHSGSGGEEALralnqavLILLGVVLIGSIatflrswLFTLAGERVV--------ARLRKRLFSA 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  245 VLHQETGFFLKNPTGSITSRVTEDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTVVTLLSLPLLFLLPRRLGK 324
Cdd:cd18780  85 IIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAVIYGK 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  325 VYQSLAVKVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKEALAYVTEVWTMSVSGMLLKVGIL 404
Cdd:cd18780 165 YVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQLAIVLVL 244
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 2506117  405 YLGGQLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKI 455
Cdd:cd18780 245 WYGGRLVIDGELTTGLLTSFLLYTLTVAMSFAFLSSLYGDFMQAVGASVRV 295
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
475-699 2.35e-33

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 128.67  E-value: 2.35e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  475 NMKGLVKFQDVSFAYPNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKST-VAALLqNLYQPTGGKVLLDGEPLVQYDHHy 553
Cdd:COG1121   2 MMMPAIELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTlLKAIL-GLLPPTSGTVRLFGKPPRRARRR- 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  554 lhtqVAAVGQEpLLFGRSF----RENIAYGLT------RTPTMEEITAV--AMES-GAHDFIsgfpqgyDTEVGEtgnqL 620
Cdd:COG1121  77 ----IGYVPQR-AEVDWDFpitvRDVVLMGRYgrrglfRRPSRADREAVdeALERvGLEDLA-------DRPIGE----L 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  621 SGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYespEWAS--RTVLLITQQLSLAER-AHHILFLKEGSV 697
Cdd:COG1121 141 SGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLR---ELRRegKTILVVTHDLGAVREyFDRVLLLNRGLV 217

                ..
gi 2506117  698 CE 699
Cdd:COG1121 218 AH 219
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
480-695 5.09e-33

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: 125.38  E-value: 5.09e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  480 VKFQDVSFAYPNHpnvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHY--LHTQ 557
Cdd:cd03229   1 LELKNVSKRYGQK---TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRR 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  558 VAAVGQEPLLF-GRSFRENIAYGLtrtptmeeitavamesgahdfisgfpqgydtevgetgnqlSGGQRQAVALARALIR 636
Cdd:cd03229  78 IGMVFQDFALFpHLTVLENIALGL----------------------------------------SGGQQQRVALARALAM 117
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  637 KPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEG 695
Cdd:cd03229 118 DPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARlADRVVVLRDG 177
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
480-697 5.49e-33

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


Pssm-ID: 213197 [Multi-domain]  Cd Length: 173  Bit Score: 124.82  E-value: 5.49e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  480 VKFQDVSFAYPNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHtQVA 559
Cdd:cd03230   1 IEVRNLSKRYGKKT---ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKR-RIG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  560 AVGQEPLLFGR-SFRENIaygltrtptmeeitavamesgahdfisgfpqgydtevgetgnQLSGGQRQAVALARALIRKP 638
Cdd:cd03230  77 YLPEEPSLYENlTVRENL------------------------------------------KLSGGMKQRLALAQALLHDP 114
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  639 RLLILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQLSLAER-AHHILFLKEGSV 697
Cdd:cd03230 115 ELLILDEPTSGLDPESRREFWELLRELKK-EGKTILLSSHILEEAERlCDRVAILNNGRI 173
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
480-701 4.71e-32

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: 123.78  E-value: 4.71e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  480 VKFQDVSFAYPNhpnVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHylHTQVA 559
Cdd:cd03259   1 LELKGLSKTYGS---VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIG 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  560 AVGQEPLLF-GRSFRENIAYGLT-RTPTMEEITAVAMESGAHDFISGFPQGYDTEvgetgnqLSGGQRQAVALARALIRK 637
Cdd:cd03259  76 MVFQDYALFpHLTVAENIAFGLKlRGVPKAEIRARVRELLELVGLEGLLNRYPHE-------LSGGQQQRVALARALARE 148
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2506117  638 PRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQG 701
Cdd:cd03259 149 PSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALAlADRIAVMNEGRIVQVG 213
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
484-697 7.87e-32

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


Pssm-ID: 213193 [Multi-domain]  Cd Length: 205  Bit Score: 122.75  E-value: 7.87e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  484 DVSFAYpnHPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDhhyLHTQVAAVGQ 563
Cdd:cd03226   4 NISFSY--KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKE---RRKSIGYVMQ 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  564 EP--LLFGRSFRENIAYGLTRTPTMEEITAVAMES-GAHDFISGFPQgydtevgetgnQLSGGQRQAVALARALIRKPRL 640
Cdd:cd03226  79 DVdyQLFTDSVREELLLGLKELDAGNEQAETVLKDlDLYALKERHPL-----------SLSGGQKQRLAIAAALLSGKDL 147
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 2506117  641 LILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQLSLAER-AHHILFLKEGSV 697
Cdd:cd03226 148 LIFDEPTSGLDYKNMERVGELIRELAA-QGKAVIVITHDYEFLAKvCDRVLLLANGAI 204
ECF_ATPase_1 TIGR04520
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
480-702 2.03e-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: 123.69  E-value: 2.03e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    480 VKFQDVSFAYPNHpNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDG-EPLVQYDHHYLHTQV 558
Cdd:TIGR04520   1 IEVENVSFSYPES-EKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGlDTLDEENLWEIRKKV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    559 AAVGQEP--LLFGRSFRENIAYGL----TRTPTMEEI-----TAVAMEsgahDFISGFPQgydtevgetgnQLSGGQRQA 627
Cdd:TIGR04520  80 GMVFQNPdnQFVGATVEDDVAFGLenlgVPREEMRKRvdealKLVGME----DFRDREPH-----------LLSGGQKQR 144
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2506117    628 VALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAERAHHILFLKEGSVCEQGT 702
Cdd:TIGR04520 145 VAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVLADRVIVMNKGKIVAEGT 219
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
475-702 7.08e-31

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 122.02  E-value: 7.08e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   475 NMKGLVKFQDVSFAYPNHPNvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYL 554
Cdd:PRK13632   3 NKSVMIKVENVSFSYPNSEN-NALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   555 HTQVAAVGQEP--LLFGRSFRENIAYGL-----TRTPTMEEITAVAMESGAHDFISGFPQgydtevgetgnQLSGGQRQA 627
Cdd:PRK13632  82 RKKIGIIFQNPdnQFIGATVEDDIAFGLenkkvPPKKMKDIIDDLAKKVGMEDYLDKEPQ-----------NLSGGQKQR 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2506117   628 VALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAERAHHILFLKEGSVCEQGT 702
Cdd:PRK13632 151 VAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGK 225
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
476-702 2.29e-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: 119.70  E-value: 2.29e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  476 MKGLVKFQDVSFAYPNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLH 555
Cdd:COG1127   2 SEPMIEVRNLTKSFGDRV---VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELY 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  556 TQVAAVG---QEPLLFGrSF--RENIAYGLTRTPTM--EEITAVAME-------SGAHDFisgFPqgydtevgetgNQLS 621
Cdd:COG1127  79 ELRRRIGmlfQGGALFD-SLtvFENVAFPLREHTDLseAEIRELVLEklelvglPGAADK---MP-----------SELS 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  622 GGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQ 700
Cdd:COG1127 144 GGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAiADRVAVLADGKIIAE 223

                ..
gi 2506117  701 GT 702
Cdd:COG1127 224 GT 225
COG4559 COG4559
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
496-702 3.61e-30

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


Pssm-ID: 443620 [Multi-domain]  Cd Length: 258  Bit Score: 119.84  E-value: 3.61e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  496 QVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQVAAVGQE-PLLFGRSFRE 574
Cdd:COG4559  15 TLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVLPQHsSLAFPFTVEE 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  575 NIAYGLTRTPTM----EEITAVAME-SGAHDFISGFPQgydtevgetgnQLSGGQRQAVALARALI-------RKPRLLI 642
Cdd:COG4559  95 VVALGRAPHGSSaaqdRQIVREALAlVGLAHLAGRSYQ-----------TLSGGEQQRVQLARVLAqlwepvdGGPRWLF 163
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2506117  643 LDDATSALDAGNQLRVQRLLYespEWASR--TVLLITQQLSLAER-AHHILFLKEGSVCEQGT 702
Cdd:COG4559 164 LDEPTSALDLAHQHAVLRLAR---QLARRggGVVAVLHDLNLAAQyADRILLLHQGRLVAQGT 223
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
479-706 4.28e-30

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: 118.84  E-value: 4.28e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  479 LVKFQDVSFAYPNHPN-VQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQ 557
Cdd:cd03258   1 MIELKNVSKVFGDTGGkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  558 VAAVG----QEPLLFGRSFRENIAYGL--TRTPtMEEITAVAME----SGAHDFISGFPqgydtevgetgNQLSGGQRQA 627
Cdd:cd03258  81 RRRIGmifqHFNLLSSRTVFENVALPLeiAGVP-KAEIEERVLEllelVGLEDKADAYP-----------AQLSGGQKQR 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  628 VALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGTHLQL 706
Cdd:cd03258 149 VGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEV 228
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
475-710 6.39e-30

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 119.73  E-value: 6.39e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   475 NMKGLVKFQDVSFAYPNHPNvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYL 554
Cdd:PRK13635   1 MKEEIIRVEHISFRYPDAAT-YALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   555 HTQVAAVGQEP--LLFGRSFRENIAYGL-----TRTPTMEEITAVAMESGAHDFISGFPqgydtevgetgNQLSGGQRQA 627
Cdd:PRK13635  80 RRQVGMVFQNPdnQFVGATVQDDVAFGLenigvPREEMVERVDQALRQVGMEDFLNREP-----------HRLSGGQKQR 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   628 VALARALIRKPRLLILDDATSALD-AGNQ--LRVQRLLYESpewASRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHL 704
Cdd:PRK13635 149 VAIAGVLALQPDIIILDEATSMLDpRGRRevLETVRQLKEQ---KGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPE 225

                 ....*.
gi 2506117   705 QLMERG 710
Cdd:PRK13635 226 EIFKSG 231
PLN03130 PLN03130
ABC transporter C family member; Provisional
236-722 6.57e-30

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 127.55  E-value: 6.57e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    236 RVHGEVFRAVLHQETGFFLKNPTGSITSRVTEDTSNVCESISDKLNLFL---WYLGRGLCLLAFM----IWGSFYLTVVT 308
Cdd:PLN03130  987 RLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVAVFVNMFLgqiFQLLSTFVLIGIVstisLWAIMPLLVLF 1066
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    309 LLSLPLlfllprrlgkvYQSLA--VKVQESLAKSTQVAL--EALSAMPTVRSFaneegeaqkfrQKLEEMKPLNKK--EA 382
Cdd:PLN03130 1067 YGAYLY-----------YQSTAreVKRLDSITRSPVYAQfgEALNGLSTIRAY-----------KAYDRMAEINGRsmDN 1124
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    383 LAYVTEVwTMSvSGMLLKVGILYLGG-------QLVVRGAVSSGNLVSF-------VLYQLQFTRAVEVLLSIYPSMQKS 448
Cdd:PLN03130 1125 NIRFTLV-NMS-SNRWLAIRLETLGGlmiwltaSFAVMQNGRAENQAAFastmgllLSYALNITSLLTAVLRLASLAENS 1202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    449 VGASEKIFEYLD------------RTPCS-PLSGSlaplnmkglVKFQDVSFAY-PNHPnvQVLQGLTFTLYPGKVTALV 514
Cdd:PLN03130 1203 LNAVERVGTYIDlpseaplviennRPPPGwPSSGS---------IKFEDVVLRYrPELP--PVLHGLSFEISPSEKVGIV 1271
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    515 GPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQVAAVGQEPLLFGRSFRENIaygltrTPTMEEITAVAM 594
Cdd:PLN03130 1272 GRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNL------DPFNEHNDADLW 1345
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    595 ES--GAH--DFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYEspEWAS 670
Cdd:PLN03130 1346 ESleRAHlkDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIRE--EFKS 1423
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2506117    671 RTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQL-MERGGCYRSMVEALAA 722
Cdd:PLN03130 1424 CTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLlSNEGSAFSKMVQSTGA 1476
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
480-702 1.13e-29

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: 117.60  E-value: 1.13e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  480 VKFQDVSFAYPNHpnvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEP---LVQYDHHYLHT 556
Cdd:cd03261   1 IELRGLTKSFGGR---TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDisgLSEAELYRLRR 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  557 QVAAVGQEPLLFGR-SFRENIAYGLTRTPTM--EEITAVAME-------SGAHDFisgFPqgydtevgetgNQLSGGQRQ 626
Cdd:cd03261  78 RMGMLFQSGALFDSlTVFENVAFPLREHTRLseEEIREIVLEkleavglRGAEDL---YP-----------AELSGGMKK 143
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2506117  627 AVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGT 702
Cdd:cd03261 144 RVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGT 220
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
479-702 1.52e-29

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


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 117.40  E-value: 1.52e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  479 LVKFQDVSFAYPNHpnvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHH--YLHT 556
Cdd:COG1126   1 MIEIENLHKSFGDL---EVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDinKLRR 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  557 QVAAVGQEPLLFG-RSFRENIAYGLTRTPTM--EEITAVAMES----GAHDFISGFPqgydtevgetgNQLSGGQRQAVA 629
Cdd:COG1126  78 KVGMVFQQFNLFPhLTVLENVTLAPIKVKKMskAEAEERAMELlervGLADKADAYP-----------AQLSGGQQQRVA 146
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2506117  630 LARALIRKPRLLILDDATSALD---AGNQLRVQRLLYESpewaSRTVLLITQQLSLAER-AHHILFLKEGSVCEQGT 702
Cdd:COG1126 147 IARALAMEPKVMLFDEPTSALDpelVGEVLDVMRDLAKE----GMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGP 219
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
476-702 3.10e-29

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 119.43  E-value: 3.10e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  476 MKGLVKFQDVSFAYPNhpnVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLvqydhhylh 555
Cdd:COG3842   2 AMPALELENVSKRYGD---VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV--------- 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  556 TQVAA----VG---QEPLLFG-RSFRENIAYGLT-RTPTMEEITA--------VAMESGAHDFISgfpqgydtevgetgn 618
Cdd:COG3842  70 TGLPPekrnVGmvfQDYALFPhLTVAENVAFGLRmRGVPKAEIRArvaellelVGLEGLADRYPH--------------- 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  619 QLSGGQRQAVALARALIRKPRLLILDDATSALDAgnQLRVQ------RLLYESPewasRTVLLIT--QQ--LSLAERahh 688
Cdd:COG3842 135 QLSGGQQQRVALARALAPEPRVLLLDEPLSALDA--KLREEmreelrRLQRELG----ITFIYVThdQEeaLALADR--- 205
                       250
                ....*....|....
gi 2506117  689 ILFLKEGSVCEQGT 702
Cdd:COG3842 206 IAVMNDGRIEQVGT 219
ABC_6TM_bac_exporter_ABCB8_10_like cd18576
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ...
179-455 3.63e-29

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


Pssm-ID: 350020 [Multi-domain]  Cd Length: 289  Bit Score: 117.58  E-value: 3.63e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  179 MAIPFFTGRITDWILQDKTAPSFARNMWLMCILTIASTVLEFAGDGIYNITMGHMHSRVHGEVFRAVLHQETGFFLKNPT 258
Cdd:cd18576  13 LVFPLLAGQLIDAALGGGDTASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRV 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  259 GSITSRVTEDTSNVCESISDKLNLFLwylgRGLCLL----AFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQSLAVKVQ 334
Cdd:cd18576  93 GELTSRLSNDVTQIQDTLTTTLAEFL----RQILTLiggvVLLFFISWKLTLLMLATVPVVVLVAVLFGRRIRKLSKKVQ 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  335 ESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKEALAYVTEVWTMSVSGMLLKVGILYLGGQLVVRG 414
Cdd:cd18576 169 DELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAIVAVLWYGGRLVLAG 248
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 2506117  415 AVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKI 455
Cdd:cd18576 249 ELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKALGASERV 289
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
474-652 4.04e-29

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 122.05  E-value: 4.04e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  474 LNMKGLVKfqdvSFaypnhPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLvqydhHY 553
Cdd:COG1129   5 LEMRGISK----SF-----GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPV-----RF 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  554 LHTQ------VAAVGQEPLLF-GRSFRENIA-------YGLTRTPTMEEITAVAMES-GAHdfISgfPqgyDTEVGEtgn 618
Cdd:COG1129  71 RSPRdaqaagIAIIHQELNLVpNLSVAENIFlgreprrGGLIDWRAMRRRARELLARlGLD--ID--P---DTPVGD--- 140
                       170       180       190
                ....*....|....*....|....*....|....
gi 2506117  619 qLSGGQRQAVALARALIRKPRLLILDDATSALDA 652
Cdd:COG1129 141 -LSVAQQQLVEIARALSRDARVLILDEPTASLTE 173
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
483-702 4.52e-29

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


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 119.10  E-value: 4.52e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  483 QDVSFAYPNhpnVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEpLVQYDHHYLHTQVAAVG 562
Cdd:COG1118   6 RNISKRFGS---FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGR-DLFTNLPPRERRVGFVF 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  563 QEPLLFgR--SFRENIAYGLT-RTPTMEEITAVAME----SGAHDFISGFPqgydtevgetgNQLSGGQRQAVALARALI 635
Cdd:COG1118  82 QHYALF-PhmTVAENIAFGLRvRPPSKAEIRARVEEllelVQLEGLADRYP-----------SQLSGGQRQRVALARALA 149
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2506117  636 RKPRLLILDDATSALDAgnQLRVQ------RLLYESPewasRTVLLITQQLSLA-ERAHHILFLKEGSVCEQGT 702
Cdd:COG1118 150 VEPEVLLLDEPFGALDA--KVRKElrrwlrRLHDELG----GTTVFVTHDQEEAlELADRVVVMNQGRIEQVGT 217
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
481-698 5.17e-29

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: 114.94  E-value: 5.17e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  481 KFQDVSFAYPNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHhylhtQVAA 560
Cdd:cd03235   1 EVEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERK-----RIGY 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  561 VGQEpLLFGRSF----RENIAYGLTRTPTM-------------EEITAVAMESGAHDFISgfpqgydtevgetgnQLSGG 623
Cdd:cd03235  73 VPQR-RSIDRDFpisvRDVVLMGLYGHKGLfrrlskadkakvdEALERVGLSELADRQIG---------------ELSGG 136
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2506117  624 QRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLyesPEWAS--RTVLLITQQLSLAER-AHHILFLKEGSVC 698
Cdd:cd03235 137 QQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELL---RELRRegMTILVVTHDLGLVLEyFDRVLLLNRTVVA 211
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
479-689 5.96e-29

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: 114.50  E-value: 5.96e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  479 LVKFQDVSFAYPNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTvaaLLQ---NLYQPTGGKVLLDGEPLVQYDHHYlH 555
Cdd:COG4133   2 MLEAENLSCRRGERL---LFSGLSFTLAAGEALALTGPNGSGKTT---LLRilaGLLPPSAGEVLWNGEPIRDAREDY-R 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  556 TQVAAVGQEPLLFGR-SFRENIA-----YGLTRTPT--MEEITAVAMESGAHDFISgfpqgydtevgetgnQLSGGQRQA 627
Cdd:COG4133  75 RRLAYLGHADGLKPElTVRENLRfwaalYGLRADREaiDEALEAVGLAGLADLPVR---------------QLSAGQKRR 139
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2506117  628 VALARALIRKPRLLILDDATSALDAGNQLRVQRLLyesPEWASR--TVLLITQQLSLAERAHHI 689
Cdd:COG4133 140 VALARLLLSPAPLWLLDEPFTALDAAGVALLAELI---AAHLARggAVLLTTHQPLELAAARVL 200
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
480-699 6.15e-29

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 115.15  E-value: 6.15e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  480 VKFQDVSFAYPNhpNVQVLQGLTFTLYPGKVTALVGPNGSGKSTvaaLLQNLY---QPTGGKVLLDGEPLVQYDHH---Y 553
Cdd:COG2884   2 IRFENVSKRYPG--GREALSDVSLEIEKGEFVFLTGPSGAGKST---LLKLLYgeeRPTSGQVLVNGQDLSRLKRReipY 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  554 LHTQVAAVGQE-PLLFGRSFRENIAY-----GLTRTPTMEEITAVAMESGAHDFISGFPqgydtevgetgNQLSGGQRQA 627
Cdd:COG2884  77 LRRRIGVVFQDfRLLPDRTVYENVALplrvtGKSRKEIRRRVREVLDLVGLSDKAKALP-----------HELSGGEQQR 145
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2506117  628 VALARALIRKPRLLILDDATSALDAGNQLRVQRLLYEspewASR---TVLLITQQLSLAERAHH-ILFLKEGSVCE 699
Cdd:COG2884 146 VAIARALVNRPELLLADEPTGNLDPETSWEIMELLEE----INRrgtTVLIATHDLELVDRMPKrVLELEDGRLVR 217
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
480-695 1.62e-28

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: 113.78  E-value: 1.62e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  480 VKFQDVSFAYPNHpnvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQ--YDHHYLHTQ 557
Cdd:cd03262   1 IEIKNLHKSFGDF---HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDdkKNINELRQK 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  558 VAAVGQEPLLFG-RSFRENIAYGLTRTPTM--EEITAVAMES----GAHDFISGFPqgydtevgetgNQLSGGQRQAVAL 630
Cdd:cd03262  78 VGMVFQQFNLFPhLTVLENITLAPIKVKGMskAEAEERALELlekvGLADKADAYP-----------AQLSGGQQQRVAI 146
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2506117  631 ARALIRKPRLLILDDATSALD---AGNQLRVQRLLYESpewaSRTVLLITQQLSLA-ERAHHILFLKEG 695
Cdd:cd03262 147 ARALAMNPKVMLFDEPTSALDpelVGEVLDVMKDLAEE----GMTMVVVTHEMGFArEVADRVIFMDDG 211
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
480-707 2.96e-28

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 114.34  E-value: 2.96e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   480 VKFQDVSFAYPNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQVA 559
Cdd:PRK11231   3 LRTENLTVGYGTKR---ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   560 AVGQEPLL-FGRSFRENIAYGltRTPTM----------EEITAVAMEsgahdfisgfpqgyDTEVGETGNQ----LSGGQ 624
Cdd:PRK11231  80 LLPQHHLTpEGITVRELVAYG--RSPWLslwgrlsaedNARVNQAME--------------QTRINHLADRrltdLSGGQ 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   625 RQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGTH 703
Cdd:PRK11231 144 RQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNT-QGKTVVTVLHDLNQASRyCDHLVVLANGHVMAQGTP 222

                 ....
gi 2506117   704 LQLM 707
Cdd:PRK11231 223 EEVM 226
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
496-702 1.93e-27

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 111.79  E-value: 1.93e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   496 QVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQVAAVGQEPLL-FGRSFRE 574
Cdd:PRK13548  16 TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFTVEE 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   575 NIAYGLT----RTPTMEEITAVAMESgahdfisgfpqgydTEVGETGN----QLSGGQRQAVALARALIR------KPRL 640
Cdd:PRK13548  96 VVAMGRAphglSRAEDDALVAAALAQ--------------VDLAHLAGrdypQLSGGEQQRVQLARVLAQlwepdgPPRW 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2506117   641 LILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGT 702
Cdd:PRK13548 162 LLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARyADRIVLLHQGRLVADGT 224
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
480-707 2.52e-27

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: 111.24  E-value: 2.52e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  480 VKFQDVSFAYPNHPnvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQVA 559
Cdd:cd03295   1 IEFENVTKRYGGGK--KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  560 AVGQEPLLF-GRSFRENIAYGLT---------RTPTMEEITAVAMESGahdfisGFPQGYDtevgetgNQLSGGQRQAVA 629
Cdd:cd03295  79 YVIQQIGLFpHMTVEENIALVPKllkwpkekiRERADELLALVGLDPA------EFADRYP-------HELSGGQQQRVG 145
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2506117  630 LARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGTHLQLM 707
Cdd:cd03295 146 VARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRlADRIAIMKNGEIVQVGTPDEIL 224
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
478-702 3.22e-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: 109.81  E-value: 3.22e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  478 GLVKFQDVSFAY-PNHPnvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHT 556
Cdd:cd03369   5 GEIEVENLSVRYaPDLP--PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  557 QVAAVGQEPLLFGRSFRENI-AYGLTrtpTMEEITAVamesgahdfisgfpqgydTEVGETGNQLSGGQRQAVALARALI 635
Cdd:cd03369  83 SLTIIPQDPTLFSGTIRSNLdPFDEY---SDEEIYGA------------------LRVSEGGLNLSQGQRQLLCLARALL 141
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2506117  636 RKPRLLILDDATSALDAGNQLRVQRLLYEspEWASRTVLLITQQLSLAERAHHILFLKEGSVCEQGT 702
Cdd:cd03369 142 KRPRVLVLDEATASIDYATDALIQKTIRE--EFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
cbiO PRK13640
energy-coupling factor transporter ATPase;
480-709 5.04e-27

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 111.43  E-value: 5.04e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   480 VKFQDVSFAYPNHPnVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQP---TGGKVLLDGEPLVQYDHHYLHT 556
Cdd:PRK13640   6 VEFKHVSFTYPDSK-KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWDIRE 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   557 QVAAVGQEP--LLFGRSFRENIAYGLTRT----PTMEEITA-VAMESGAHDFISGFPQgydtevgetgnQLSGGQRQAVA 629
Cdd:PRK13640  85 KVGIVFQNPdnQFVGATVGDDVAFGLENRavprPEMIKIVRdVLADVGMLDYIDSEPA-----------NLSGGQKQRVA 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   630 LARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLMER 709
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSK 233
ABC_6TM_Pgp_ABCB1_D1_like cd18577
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ...
179-455 1.31e-26

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: 110.64  E-value: 1.31e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  179 MAIPFFT---GRITD----WILQDKTAPSF----ARNMWLMCILTIASTVLEFAGDGIYNITMGHMHSRVHGEVFRAVLH 247
Cdd:cd18577  13 AALPLMTivfGDLFDaftdFGSGESSPDEFlddvNKYALYFVYLGIGSFVLSYIQTACWTITGERQARRIRKRYLKALLR 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  248 QETGFFLKNPTGSITSRVTEDTSNVCESISDKLNLFLWYLGRGLCLLAFmiwgSFY----LTVVTLLSLPLLFLLPRRLG 323
Cdd:cd18577  93 QDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFII----AFIyswkLTLVLLATLPLIAIVGGIMG 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  324 KVYQSLAVKVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKEALAYVTEVWTMSVSGMLLKVGI 403
Cdd:cd18577 169 KLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLFFIIFAMYALA 248
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 2506117  404 LYLGGQLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKI 455
Cdd:cd18577 249 FWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
485-709 1.94e-26

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: 110.53  E-value: 1.94e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  485 VSFAYPNHPnVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQP---TGGKVLLDGEPLVQYDH----HYLHTQ 557
Cdd:COG0444   9 VYFPTRRGV-VKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEkelrKIRGRE 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  558 VAAVGQEPL-----LF--GRSFRENIAY--GLTRtptmEEITAVAME-------SGAHDFISGFPqgydtevgetgNQLS 621
Cdd:COG0444  88 IQMIFQDPMtslnpVMtvGDQIAEPLRIhgGLSK----AEARERAIEllervglPDPERRLDRYP-----------HELS 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  622 GGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSL-AERAHHILFLKEGSVCEQ 700
Cdd:COG0444 153 GGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVvAEIADRVAVMYAGRIVEE 232

                ....*....
gi 2506117  701 GTHLQLMER 709
Cdd:COG0444 233 GPVEELFEN 241
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
495-708 2.03e-26

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: 107.91  E-value: 2.03e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  495 VQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLvqyDHHYLHTQVAA----VGQEPLLFGR 570
Cdd:cd03224  13 SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDI---TGLPPHERARAgigyVPEGRRIFPE 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  571 -SFRENI---AYGLTR---TPTMEEITAVamesgahdfisgFP---QGYDTEVGetgnQLSGGQRQAVALARALIRKPRL 640
Cdd:cd03224  90 lTVEENLllgAYARRRakrKARLERVYEL------------FPrlkERRKQLAG----TLSGGEQQMLAIARALMSRPKL 153
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2506117  641 LILDDATSAL---------DAGNQLRVQRLlyespewasrTVLLITQQLSLA-ERAHHILFLKEGSVCEQGTHLQLME 708
Cdd:cd03224 154 LLLDEPSEGLapkiveeifEAIRELRDEGV----------TILLVEQNARFAlEIADRAYVLERGRVVLEGTAAELLA 221
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
480-702 2.73e-26

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: 108.20  E-value: 2.73e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  480 VKFQDVSFAYPNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQydHHYLHTQVA 559
Cdd:cd03296   3 IEVRNVSKRFGDFV---ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATD--VPVQERNVG 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  560 AVGQEPLLFGR-SFRENIAYGLTRTPTMEEITAVAMESGAHDFI-----SGFPQGYDtevgetgNQLSGGQRQAVALARA 633
Cdd:cd03296  78 FVFQHYALFRHmTVFDNVAFGLRVKPRSERPPEAEIRAKVHELLklvqlDWLADRYP-------AQLSGGQRQRVALARA 150
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  634 LIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLA-ERAHHILFLKEGSVCEQGT 702
Cdd:cd03296 151 LAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEAlEVADRVVVMNKGRIEQVGT 220
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
502-708 3.47e-26

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: 108.50  E-value: 3.47e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  502 TFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYL----HTQVAAVGQEPLLF-GRSFRENI 576
Cdd:cd03294  44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLpHRTVLENV 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  577 AYGL-TRTPTMEEITAVAMES----GAHDFISGFPqgydtevgetgNQLSGGQRQAVALARALIRKPRLLILDDATSALD 651
Cdd:cd03294 124 AFGLeVQGVPRAEREERAAEAlelvGLEGWEHKYP-----------DELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 2506117  652 AGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGTHLQLME 708
Cdd:cd03294 193 PLIRREMQDELLRLQAELQKTIVFITHDLDEALRlGDRIAIMKDGRLVQVGTPEEILT 250
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
481-697 5.06e-26

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: 107.27  E-value: 5.06e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  481 KFQDVSFAYPNhpNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHT---Q 557
Cdd:cd03256   2 EVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQlrrQ 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  558 VAAVGQEPLLFGR-SFRENIAYG-LTRTPTM---------EEI-------TAVAMESGAHDFISgfpqgydtevgetgnQ 619
Cdd:cd03256  80 IGMIFQQFNLIERlSVLENVLSGrLGRRSTWrslfglfpkEEKqralaalERVGLLDKAYQRAD---------------Q 144
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2506117  620 LSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSV 697
Cdd:cd03256 145 LSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREyADRIVGLKDGRI 223
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
480-709 8.16e-26

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: 106.55  E-value: 8.16e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  480 VKFQDVSFAYPNhpnVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHylHTQVA 559
Cdd:cd03300   1 IELENVSKFYGG---FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVN 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  560 AVGQEPLLFGR-SFRENIAYGLTRTPT---------MEEITAVAMESGAHDFISgfpqgydtevgetgnQLSGGQRQAVA 629
Cdd:cd03300  76 TVFQNYALFPHlTVFENIAFGLRLKKLpkaeikervAEALDLVQLEGYANRKPS---------------QLSGGQQQRVA 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  630 LARALIRKPRLLILDDATSALDAgnQLRvQRLLYESPEWASR---TVLLIT--QQ--LSLAERahhILFLKEGSVCEQGT 702
Cdd:cd03300 141 IARALVNEPKVLLLDEPLGALDL--KLR-KDMQLELKRLQKElgiTFVFVThdQEeaLTMSDR---IAVMNKGKIQQIGT 214

                ....*..
gi 2506117  703 HLQLMER 709
Cdd:cd03300 215 PEEIYEE 221
cbiO PRK13642
energy-coupling factor transporter ATPase;
476-706 1.43e-25

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 107.10  E-value: 1.43e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   476 MKGLVKFQDVSFAYPNHPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLH 555
Cdd:PRK13642   1 MNKILEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   556 TQVAAVGQEP--LLFGRSFRENIAYGLT-----RTPTMEEITAVAMESGAHDFISGFPQgydtevgetgnQLSGGQRQAV 628
Cdd:PRK13642  81 RKIGMVFQNPdnQFVGATVEDDVAFGMEnqgipREEMIKRVDEALLAVNMLDFKTREPA-----------RLSGGQKQRV 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2506117   629 ALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQL 706
Cdd:PRK13642 150 AVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSEL 227
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
507-701 1.50e-25

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: 105.07  E-value: 1.50e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  507 PGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHH-YLHTQVAAVG---QEPLLFGR-SFRENIAYGLT 581
Cdd:cd03297  22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKiNLPPQQRKIGlvfQQYALFPHlNVRENLAFGLK 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  582 RTPTMEEITAVAMESGAHDfISGFPQGYDtevgetgNQLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRL 661
Cdd:cd03297 102 RKRNREDRISVDELLDLLG-LDHLLNRYP-------AQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPE 173
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 2506117  662 LYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQG 701
Cdd:cd03297 174 LKQIKKNLNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
479-702 1.63e-25

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 106.76  E-value: 1.63e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   479 LVKFQDVSFAYpNHPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQV 558
Cdd:PRK13648   7 IIVFKNVSFQY-QSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHI 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   559 AAVGQEP--LLFGRSFRENIAYGLTR----TPTMEEITAVAMES-GAHDFISGFPQGydtevgetgnqLSGGQRQAVALA 631
Cdd:PRK13648  86 GIVFQNPdnQFVGSIVKYDVAFGLENhavpYDEMHRRVSEALKQvDMLERADYEPNA-----------LSGGQKQRVAIA 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2506117   632 RALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAERAHHILFLKEGSVCEQGT 702
Cdd:PRK13648 155 GVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGT 225
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
483-708 2.29e-25

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 106.03  E-value: 2.29e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   483 QDVSFAYPNHpnvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQVAAVG 562
Cdd:PRK10575  15 RNVSFRVPGR---TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLP 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   563 QE-PLLFGRSFRENIAYG-------------LTRTPTMEEITAVAMESGAHDFIsgfpqgydtevgetgNQLSGGQRQAV 628
Cdd:PRK10575  92 QQlPAAEGMTVRELVAIGrypwhgalgrfgaADREKVEEAISLVGLKPLAHRLV---------------DSLSGGERQRA 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   629 ALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGTHLQLM 707
Cdd:PRK10575 157 WIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARyCDYLVALRGGEMIAQGTPAELM 236

                 .
gi 2506117   708 E 708
Cdd:PRK10575 237 R 237
ABC_6TM_MsbA_like cd18552
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ...
180-455 4.58e-25

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


Pssm-ID: 349996 [Multi-domain]  Cd Length: 292  Bit Score: 105.97  E-value: 4.58e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  180 AIPFFTGRITDWILQDKTApsfaRNMWLMCILTIASTVLEFAGDGIYNITMGHMHSRV----HGEVFRAVLHQETGFFLK 255
Cdd:cd18552  17 ALAWLLKPLLDDIFVEKDL----EALLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVvrdlRNDLFDKLLRLPLSFFDR 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  256 NPTGSITSRVTEDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQSLAVKVQE 335
Cdd:cd18552  93 NSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPIRRIGKRLRKISRRSQE 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  336 SLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEE-----MKPLNKKEALAYVTEVwtMSVSGMllkVGILYLGGQL 410
Cdd:cd18552 173 SMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERlrrlsMKIARARALSSPLMEL--LGAIAI---ALVLWYGGYQ 247
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 2506117  411 VVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKI 455
Cdd:cd18552 248 VISGELTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAAAERI 292
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
495-709 4.77e-25

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


Pssm-ID: 443332 [Multi-domain]  Cd Length: 533  Bit Score: 109.77  E-value: 4.77e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  495 VQVLQGLTFTLYPGKVTALVGPNGSGKSTVA-ALLQnLyQPTGGKVLLDGEPLVQYDHHYL-----HTQVaaVGQEPllF 568
Cdd:COG4172 299 VKAVDGVSLTLRRGETLGLVGESGSGKSTLGlALLR-L-IPSEGEIRFDGQDLDGLSRRALrplrrRMQV--VFQDP--F 372
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  569 G-----RSFRENIAYGLT------RTPTMEEITAVAMEsgahdfisgfpqgydtEVG---ETGN----QLSGGQRQAVAL 630
Cdd:COG4172 373 GslsprMTVGQIIAEGLRvhgpglSAAERRARVAEALE----------------EVGldpAARHryphEFSGGQRQRIAI 436
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  631 ARALIRKPRLLILDDATSALDAGNQLRVQRLL----------YespewasrtvLLITQQLSLAER-AHHILFLKEGSVCE 699
Cdd:COG4172 437 ARALILEPKLLVLDEPTSALDVSVQAQILDLLrdlqrehglaY----------LFISHDLAVVRAlAHRVMVMKDGKVVE 506
                       250
                ....*....|
gi 2506117  700 QGTHLQLMER 709
Cdd:COG4172 507 QGPTEQVFDA 516
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
484-702 7.52e-25

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 104.77  E-value: 7.52e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   484 DVSFAYPNhpNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLvQYDHHYL---HTQVAA 560
Cdd:PRK13639   6 DLKYSYPD--GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLlevRKTVGI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   561 VGQEP--LLFGRSFRENIAYG-LTRTPTMEEITAVAMESGAHDFISGFPQgydtevgETGNQLSGGQRQAVALARALIRK 637
Cdd:PRK13639  83 VFQNPddQLFAPTVEEDVAFGpLNLGLSKEEVEKRVKEALKAVGMEGFEN-------KPPHHLSGGQKKRVAIAGILAMK 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2506117   638 PRLLILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGT 702
Cdd:PRK13639 156 PEIIVLDEPTSGLDPMGASQIMKLLYDLNK-EGITIIISTHDVDLVPVyADKVYVMSDGKIIKEGT 220
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
495-695 8.62e-25

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: 103.28  E-value: 8.62e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  495 VQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHylhtQVAA-----VG----QEP 565
Cdd:COG4181  25 LTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDED----ARARlrarhVGfvfqSFQ 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  566 LLFGRSFRENIAYGL-------TRTPTMEEITAVAMESGAHDFisgfPqgydtevgetgNQLSGGQRQAVALARALIRKP 638
Cdd:COG4181 101 LLPTLTALENVMLPLelagrrdARARARALLERVGLGHRLDHY----P-----------AQLSGGEQQRVALARAFATEP 165
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 2506117  639 RLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAERAHHILFLKEG 695
Cdd:COG4181 166 AILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAARCDRVLRLRAG 222
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
474-697 1.41e-24

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: 100.58  E-value: 1.41e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  474 LNMKGLVKfqdvSFaypnhPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVqydhhy 553
Cdd:cd03216   1 LELRGITK----RF-----GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVS------ 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  554 lhtqvaavgqepllfGRSFRENIAYGltrtptmeeITAVamesgaHdfisgfpqgydtevgetgnQLSGGQRQAVALARA 633
Cdd:cd03216  66 ---------------FASPRDARRAG---------IAMV------Y-------------------QLSVGERQMVEIARA 96
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2506117  634 LIRKPRLLILDDATSALD---AGNQLRVQRLLYESpewaSRTVLLITQQLS-LAERAHHILFLKEGSV 697
Cdd:cd03216  97 LARNARLLILDEPTAALTpaeVERLFKVIRRLRAQ----GVAVIFISHRLDeVFEIADRVTVLRDGRV 160
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
480-706 1.51e-24

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: 102.20  E-value: 1.51e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  480 VKFQDVSFAYPNHPNVqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGeplvqydhHYLHTQVA 559
Cdd:cd03263   1 LQIRNLTKTYKKGTKP-AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYING--------YSIRTDRK 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  560 AVGQE--------PLLFGRSFRENIAY-----GLTRTPTMEEITAVAMESGAHDFIsgfpqgyDTEVGetgnQLSGGQRQ 626
Cdd:cd03263  72 AARQSlgycpqfdALFDELTVREHLRFyarlkGLPKSEIKEEVELLLRVLGLTDKA-------NKRAR----TLSGGMKR 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  627 AVALARALIRKPRLLILDDATSALDAgnqlRVQRLLYESPEWA--SRTVLLITQQLSLAER-AHHILFLKEGSVCEQGTH 703
Cdd:cd03263 141 KLSLAIALIGGPSVLLLDEPTSGLDP----ASRRAIWDLILEVrkGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSP 216

                ...
gi 2506117  704 LQL 706
Cdd:cd03263 217 QEL 219
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
495-701 2.20e-24

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


Pssm-ID: 213236 [Multi-domain]  Cd Length: 210  Bit Score: 101.59  E-value: 2.20e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  495 VQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHH-----------YLHTQVaavgQ 563
Cdd:cd03269  13 VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNrigylpeerglYPKMKV----I 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  564 EPLLFGRSFReniayGLTRTPTMEEITavamesgahDFISGFpqgydtEVGETGN----QLSGGQRQAVALARALIRKPR 639
Cdd:cd03269  89 DQLVYLAQLK-----GLKKEEARRRID---------EWLERL------ELSEYANkrveELSKGNQQKVQFIAAVIHDPE 148
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2506117  640 LLILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQLSLAER-AHHILFLKEGSVCEQG 701
Cdd:cd03269 149 LLILDEPFSGLDPVNVELLKDVIRELAR-AGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
481-702 2.73e-24

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 102.14  E-value: 2.73e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  481 KFQDVSFAYPNHPnvqvlqgLTFTLY--PGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHylhtQ- 557
Cdd:COG3840   3 RLDDLTYRYGDFP-------LRFDLTiaAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPA----Er 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  558 -VAAVGQEPLLFGR-SFRENIAYGLTrtPTM-------EEITAVAMESGAHDFISGFPQgydtevgetgnQLSGGQRQAV 628
Cdd:COG3840  72 pVSMLFQENNLFPHlTVAQNIGLGLR--PGLkltaeqrAQVEQALERVGLAGLLDRLPG-----------QLSGGQRQRV 138
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2506117  629 ALARALIRKPRLLILDDATSALDAGnqLRvQRLLYESPEWASR---TVLLITQQLSLAER-AHHILFLKEGSVCEQGT 702
Cdd:COG3840 139 ALARCLVRKRPILLLDEPFSALDPA--LR-QEMLDLVDELCRErglTVLMVTHDPEDAARiADRVLLVADGRIAADGP 213
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
479-699 4.05e-24

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 102.46  E-value: 4.05e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   479 LVKFQDVSFAYPN------HPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYD-- 550
Cdd:PRK10419   3 LLNVSGLSHHYAHgglsgkHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNra 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   551 -HHYLHTQVAAVGQEPL-------LFGRSFRENIAYGLTRTPTMEEITAVAMESG---AHDFISGFPQgydtevgetgnQ 619
Cdd:PRK10419  83 qRKAFRRDIQMVFQDSIsavnprkTVREIIREPLRHLLSLDKAERLARASEMLRAvdlDDSVLDKRPP-----------Q 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   620 LSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVC 698
Cdd:PRK10419 152 LSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERfCQRVMVMDNGQIV 231

                 .
gi 2506117   699 E 699
Cdd:PRK10419 232 E 232
ABCC_SUR2 cd03288
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...
459-719 5.61e-24

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: 101.91  E-value: 5.61e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  459 LDRTPCSPLSGslaplnMKGLVKFQDVSFAYPNHPNvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGK 538
Cdd:cd03288   5 ISGSSNSGLVG------LGGEIKIHDLCVRYENNLK-PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGK 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  539 VLLDGEPLVQYDHHYLHTQVAAVGQEPLLFGRSFRENIAYGLTRT-PTMEEITAVAMesgAHDFISGFPQGYDTEVGETG 617
Cdd:cd03288  78 IVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLDPECKCTdDRLWEALEIAQ---LKNMVKSLPGGLDAVVTEGG 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  618 NQLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESpeWASRTVLLITQQLSLAERAHHILFLKEGSV 697
Cdd:cd03288 155 ENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTA--FADRTVVTIAHRVSTILDADLVLVLSRGIL 232
                       250       260
                ....*....|....*....|...
gi 2506117  698 CEQGTHLQLM-ERGGCYRSMVEA 719
Cdd:cd03288 233 VECDTPENLLaQEDGVFASLVRT 255
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
479-709 8.99e-24

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 100.94  E-value: 8.99e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   479 LVKFQDVSFAYPNHpnvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDG----EPLVqyDHHYL 554
Cdd:PRK09493   1 MIEFKNVSKHFGPT---QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGlkvnDPKV--DERLI 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   555 HTQVAAVGQEPLLFGR-SFRENIAYGLTRT----------PTMEEITAVAMESGAHDFISgfpqgydtevgetgnQLSGG 623
Cdd:PRK09493  76 RQEAGMVFQQFYLFPHlTALENVMFGPLRVrgaskeeaekQARELLAKVGLAERAHHYPS---------------ELSGG 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   624 QRQAVALARALIRKPRLLILDDATSALDA---GNQLRVQRLLYESpewaSRTVLLITQQLSLAER-AHHILFLKEGSVCE 699
Cdd:PRK09493 141 QQQRVAIARALAVKPKLMLFDEPTSALDPelrHEVLKVMQDLAEE----GMTMVIVTHEIGFAEKvASRLIFIDKGRIAE 216
                        250
                 ....*....|
gi 2506117   700 QGTHLQLMER 709
Cdd:PRK09493 217 DGDPQVLIKN 226
PLN03130 PLN03130
ABC transporter C family member; Provisional
346-718 1.93e-23

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 106.75  E-value: 1.93e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    346 EALSAMPTVRSFANEegeaQKFRQKL-----EEMKPLNKKEALAYVTEVWTMSVSGM--LLKVGIL-YLGGQLVVRGAVS 417
Cdd:PLN03130  484 EVLAAMDTVKCYAWE----NSFQSKVqtvrdDELSWFRKAQLLSAFNSFILNSIPVLvtVVSFGVFtLLGGDLTPARAFT 559
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    418 SGNLVS---FVLYQLQ--FTRAVEVLLSIyPSMQKSVGASEKIFeyldrTPCSPLSGSLAPLNMKglvkfqDVSFAYPNH 492
Cdd:PLN03130  560 SLSLFAvlrFPLFMLPnlITQAVNANVSL-KRLEELLLAEERVL-----LPNPPLEPGLPAISIK------NGYFSWDSK 627
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    493 PNVQVLQGLTFTLYPGKVTALVGPNGSGK-STVAALLQNLYQPTGGKVLLDGeplvqydhhylhtQVAAVGQEPLLFGRS 571
Cdd:PLN03130  628 AERPTLSNINLDVPVGSLVAIVGSTGEGKtSLISAMLGELPPRSDASVVIRG-------------TVAYVPQVSWIFNAT 694
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    572 FRENIAYGLTRTPTMEEiTAVAMESGAHDfISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDATSALD 651
Cdd:PLN03130  695 VRDNILFGSPFDPERYE-RAIDVTALQHD-LDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    652 AgnqlRVQRLLYES---PEWASRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLMERGGCYRSMVE 718
Cdd:PLN03130  773 A----HVGRQVFDKcikDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKLME 838
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
480-697 3.08e-23

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: 98.63  E-value: 3.08e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  480 VKFQDVSFAYPNhpNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHH---YLHT 556
Cdd:cd03292   1 IEFINVTKTYPN--GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRaipYLRR 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  557 QVAAVGQE-PLLFGRSFRENIAYGL---------TRTPTMEEITAVAMESGAHDFisgfpqgydtevgetGNQLSGGQRQ 626
Cdd:cd03292  79 KIGVVFQDfRLLPDRNVYENVAFALevtgvppreIRKRVPAALELVGLSHKHRAL---------------PAELSGGEQQ 143
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2506117  627 AVALARALIRKPRLLILDDATSALDAGNQLRVQRLLyESPEWASRTVLLITQQLSLAER-AHHILFLKEGSV 697
Cdd:cd03292 144 RVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLL-KKINKAGTTVVVATHAKELVDTtRHRVIALERGKL 214
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
495-651 3.28e-23

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


Pssm-ID: 443658 [Multi-domain]  Cd Length: 329  Bit Score: 101.35  E-value: 3.28e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  495 VQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYL-----HTQV------AA--- 560
Cdd:COG4608  31 VKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELrplrrRMQMvfqdpyASlnp 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  561 ---VGQ---EPLLfgrsfreniAYGLTRTPTMEEITAVAMES-G-AHDFISGFPqgydtevgetgNQLSGGQRQAVALAR 632
Cdd:COG4608 111 rmtVGDiiaEPLR---------IHGLASKAERRERVAELLELvGlRPEHADRYP-----------HEFSGGQRQRIGIAR 170
                       170
                ....*....|....*....
gi 2506117  633 ALIRKPRLLILDDATSALD 651
Cdd:COG4608 171 ALALNPKLIVCDEPVSALD 189
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
484-701 3.59e-23

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: 98.03  E-value: 3.59e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  484 DVSFAYPNHpnvQVLQGLTFTLYPGkVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQyDHHYLHTQVAAVGQ 563
Cdd:cd03264   5 NLTKRYGKK---RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGYLPQ 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  564 EPLLFGR-SFRENIAY-----GLTRTPTMEEITAVAMESGAHDFisgfpqgYDTEVGetgnQLSGGQRQAVALARALIRK 637
Cdd:cd03264  80 EFGVYPNfTVREFLDYiawlkGIPSKEVKARVDEVLELVNLGDR-------AKKKIG----SLSGGMRRRVGIAQALVGD 148
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2506117  638 PRLLILDDATSALDAGNQLRVQRLLYESPEwaSRTVLLITQQLS-LAERAHHILFLKEGSVCEQG 701
Cdd:cd03264 149 PSILIVDEPTAGLDPEERIRFRNLLSELGE--DRIVILSTHIVEdVESLCNQVAVLNKGKLVFEG 211
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
479-702 3.86e-23

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 99.88  E-value: 3.86e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   479 LVKFQDVSFAYPNhpNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQV 558
Cdd:PRK13652   3 LIETRDLCYSYSG--SKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   559 AAVGQEP--LLFGRSFRENIAYGLTRTPTMEEITAVAMESGAHDFisgfpqGYDTEVGETGNQLSGGQRQAVALARALIR 636
Cdd:PRK13652  81 GLVFQNPddQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHML------GLEELRDRVPHHLSGGEKKRVAIAGVIAM 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2506117   637 KPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSL-AERAHHILFLKEGSVCEQGT 702
Cdd:PRK13652 155 EPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLvPEMADYIYVMDKGRIVAYGT 221
ABC_6TM_LmrA_like cd18551
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ...
180-455 4.02e-23

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: 100.20  E-value: 4.02e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  180 AIPFFTGRITDWILQDKtapSFARNMWLMCILTIASTVLEfagdGIYNITMGHMHSRVhgeVFRA-------VLHQETGF 252
Cdd:cd18551  17 AQPLLVKNLIDALSAGG---SSGGLLALLVALFLLQAVLS----ALSSYLLGRTGERV---VLDLrrrlwrrLLRLPVSF 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  253 FLKNPTGSITSRVTEDTSNVCESISDKL-NLFLwylgrGLCLL----AFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQ 327
Cdd:cd18551  87 FDRRRSGDLVSRVTNDTTLLRELITSGLpQLVT-----GVLTVvgavVLMFLLDWVLTLVTLAVVPLAFLIILPLGRRIR 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  328 SLAVKVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKEAL--AYVTEVWTMSVSGMLLkvGILY 405
Cdd:cd18551 162 KASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKieALIGPLMGLAVQLALL--VVLG 239
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 2506117  406 LGGQLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKI 455
Cdd:cd18551 240 VGGARVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGALERI 289
TauB COG4525
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
481-677 5.03e-23

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


Pssm-ID: 443596 [Multi-domain]  Cd Length: 262  Bit Score: 99.17  E-value: 5.03e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  481 KFQDVSFAYPNH-PNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPL--------VQYDH 551
Cdd:COG4525   5 TVRHVSVRYPGGgQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVtgpgadrgVVFQK 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  552 HylhtqvaavgqePLLFGRSFRENIAYGL--------TRTPTMEEITA-VAMESGAHDFISgfpqgydtevgetgnQLSG 622
Cdd:COG4525  85 D------------ALLPWLNVLDNVAFGLrlrgvpkaERRARAEELLAlVGLADFARRRIW---------------QLSG 137
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 2506117  623 GQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLIT 677
Cdd:COG4525 138 GMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLIT 192
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
480-702 7.47e-23

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 100.54  E-value: 7.47e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  480 VKFQDVSFAYP-NHPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQV 558
Cdd:COG1135   2 IELENLSKTFPtKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAAR 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  559 AAVG----QEPLLFGRSFRENIAY-----GLTRtptmEEITAVAME-------SGAHDFisgFPqgydtevgetgNQLSG 622
Cdd:COG1135  82 RKIGmifqHFNLLSSRTVAENVALpleiaGVPK----AEIRKRVAEllelvglSDKADA---YP-----------SQLSG 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  623 GQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYEspewASR----TVLLITQQLSLAER-AHHILFLKEGSV 697
Cdd:COG1135 144 GQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKD----INRelglTIVLITHEMDVVRRiCDRVAVLENGRI 219

                ....*
gi 2506117  698 CEQGT 702
Cdd:COG1135 220 VEQGP 224
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
480-701 8.99e-23

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


Pssm-ID: 213235 [Multi-domain]  Cd Length: 208  Bit Score: 96.90  E-value: 8.99e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  480 VKFQDVSFAYPNHpnvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVqyDHHYLHTQVA 559
Cdd:cd03268   1 LKTNDLTKTYGKK---RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQ--KNIEALRRIG 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  560 AVGQEPLLFG-RSFRENI-----AYGLTRTPTMEEITAVAMESGAHDFISGFpqgydtevgetgnqlSGGQRQAVALARA 633
Cdd:cd03268  76 ALIEAPGFYPnLTARENLrllarLLGIRKKRIDEVLDVVGLKDSAKKKVKGF---------------SLGMKQRLGIALA 140
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2506117  634 LIRKPRLLILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQLS-LAERAHHILFLKEGSVCEQG 701
Cdd:cd03268 141 LLGNPDLLILDEPTNGLDPDGIKELRELILSLRD-QGITVLISSHLLSeIQKVADRIGIINKGKLIEEG 208
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
480-701 1.16e-22

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: 96.79  E-value: 1.16e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  480 VKFQDVSFAY---PNHPNVQVLQGltftlypgKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEplvqyDHHYLHT 556
Cdd:cd03298   1 VRLDKIRFSYgeqPMHFDLTFAQG--------EITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGV-----DVTAAPP 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  557 Q---VAAVGQEPLLFGR-SFRENIAYGLTRTPTMEEITAVAMESGAHDFisgfpqGYDTEVGETGNQLSGGQRQAVALAR 632
Cdd:cd03298  68 AdrpVSMLFQENNLFAHlTVEQNVGLGLSPGLKLTAEDRQAIEVALARV------GLAGLEKRLPGELSGGERQRVALAR 141
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  633 ALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQG 701
Cdd:cd03298 142 VLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
477-659 1.27e-22

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 100.41  E-value: 1.27e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   477 KGLVKFQDVSFAYPNHpnvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPL--VQYDHHYL 554
Cdd:PRK09452  12 SPLVELRGISKSFDGK---EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIthVPAENRHV 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   555 HTqvaaVGQEPLLFGR-SFRENIAYGL--TRTPTmEEITAVAMESGA----HDFISGFPQgydtevgetgnQLSGGQRQA 627
Cdd:PRK09452  89 NT----VFQSYALFPHmTVFENVAFGLrmQKTPA-AEITPRVMEALRmvqlEEFAQRKPH-----------QLSGGQQQR 152
                        170       180       190
                 ....*....|....*....|....*....|..
gi 2506117   628 VALARALIRKPRLLILDDATSALDAgnQLRVQ 659
Cdd:PRK09452 153 VAIARAVVNKPKVLLLDESLSALDY--KLRKQ 182
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
497-702 1.33e-22

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 97.19  E-value: 1.33e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   497 VLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQ-----------------YDHHYLHTQVA 559
Cdd:PRK11629  24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKlssaakaelrnqklgfiYQFHHLLPDFT 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   560 AVGQ--EPLLFGRSFRENIaygltRTPTMEEITAVAMESGAHDFISgfpqgydtevgetgnQLSGGQRQAVALARALIRK 637
Cdd:PRK11629 104 ALENvaMPLLIGKKKPAEI-----NSRALEMLAAVGLEHRANHRPS---------------ELSGGERQRVAIARALVNN 163
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2506117   638 PRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAERAHHILFLKEGSVCEQGT 702
Cdd:PRK11629 164 PRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAELS 228
PLN03232 PLN03232
ABC transporter C family member; Provisional
255-718 1.48e-22

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 103.90  E-value: 1.48e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    255 KN-PTGSITSRVTEDtSNVCESISDKLNlFLWylGRGLCLLAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQSLAVKV 333
Cdd:PLN03232  393 KNfASGKVTNMITTD-ANALQQIAEQLH-GLW--SAPFRIIVSMVLLYQQLGVASLFGSLILFLLIPLQTLIVRKMRKLT 468
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    334 QESLA---KSTQVALEALSAMPTVRSFANE---EGEAQKFRQklEEMKPLNKKEALAYVTE--VWTMSVSGMLLKVGI-L 404
Cdd:PLN03232  469 KEGLQwtdKRVGIINEILASMDTVKCYAWEksfESRIQGIRN--EELSWFRKAQLLSAFNSfiLNSIPVVVTLVSFGVfV 546
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    405 YLGGQLVVRGAVSSGNLVSFVLYQLQFtraVEVLLSIYPSMQKSVGASEKIFEYLDR--TPCSPLSGSLAPLNMKglvkf 482
Cdd:PLN03232  547 LLGGDLTPARAFTSLSLFAVLRSPLNM---LPNLLSQVVNANVSLQRIEELLLSEERilAQNPPLQPGAPAISIK----- 618
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    483 qDVSFAYPNHPNVQVLQGLTFTLYPGKVTALVGPNGSGK-STVAALLQNLYQPTGGKVLLDGeplvqydhhylhtQVAAV 561
Cdd:PLN03232  619 -NGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKtSLISAMLGELSHAETSSVVIRG-------------SVAYV 684
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    562 GQEPLLFGRSFRENIAYGLTRTPTM--EEITAVAMEsgaHDfISGFPqGYD-TEVGETGNQLSGGQRQAVALARALIRKP 638
Cdd:PLN03232  685 PQVSWIFNATVRENILFGSDFESERywRAIDVTALQ---HD-LDLLP-GRDlTEIGERGVNISGGQKQRVSMARAVYSNS 759
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    639 RLLILDDATSALDAgnqlRVQRLLYES---PEWASRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLMERGGCYRS 715
Cdd:PLN03232  760 DIYIFDDPLSALDA----HVAHQVFDScmkDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKK 835

                  ...
gi 2506117    716 MVE 718
Cdd:PLN03232  836 LME 838
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
480-659 1.60e-22

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


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 99.76  E-value: 1.60e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  480 VKFQDVSFAYPNhpnVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEpLVQYdhhyLHTQ-- 557
Cdd:COG3839   4 LELENVSKSYGG---VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGR-DVTD----LPPKdr 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  558 -VAAVGQEPLLF-GRSFRENIAYGLT--RTPTmEEItavamesgahdfisgfpqgyDTEVGETG-------------NQL 620
Cdd:COG3839  76 nIAMVFQSYALYpHMTVYENIAFPLKlrKVPK-AEI--------------------DRRVREAAellgledlldrkpKQL 134
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 2506117  621 SGGQRQAVALARALIRKPRLLILDDATSALDAgnQLRVQ 659
Cdd:COG3839 135 SGGQRQRVALGRALVREPKVFLLDEPLSNLDA--KLRVE 171
cbiO PRK13650
energy-coupling factor transporter ATPase;
476-711 1.81e-22

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 97.88  E-value: 1.81e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   476 MKGLVKFQDVSFAYPNHPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLH 555
Cdd:PRK13650   1 MSNIIEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   556 TQVAAVGQEP--LLFGRSFRENIAYGLTRT----PTMEEITAVAME-SGAHDFISGFPQgydtevgetgnQLSGGQRQAV 628
Cdd:PRK13650  81 HKIGMVFQNPdnQFVGATVEDDVAFGLENKgiphEEMKERVNEALElVGMQDFKEREPA-----------RLSGGQKQRV 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   629 ALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLME 708
Cdd:PRK13650 150 AIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFS 229

                 ...
gi 2506117   709 RGG 711
Cdd:PRK13650 230 RGN 232
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
496-701 1.83e-22

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 97.13  E-value: 1.83e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   496 QVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKV-----LLDG-EPLVQYDH--HYLHTQVAAVGQEPLL 567
Cdd:PRK11264  17 TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgdiTIDTaRSLSQQKGliRQLRQHVGFVFQNFNL 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   568 F-GRSFRENIAYG--LTRTPTMEEITAVAMESGAHDFISGFPQGYDtevgetgNQLSGGQRQAVALARALIRKPRLLILD 644
Cdd:PRK11264  97 FpHRTVLENIIEGpvIVKGEPKEEATARARELLAKVGLAGKETSYP-------RRLSGGQQQRVAIARALAMRPEVILFD 169
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2506117   645 DATSALD---AGNQLRVQRLLYESpewaSRTVLLITQQLSLA-ERAHHILFLKEGSVCEQG 701
Cdd:PRK11264 170 EPTSALDpelVGEVLNTIRQLAQE----KRTMVIVTHEMSFArDVADRAIFMDQGRIVEQG 226
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
473-701 2.20e-22

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 100.30  E-value: 2.20e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   473 PLNMKGLvkfqDVSFAypnhpNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHH 552
Cdd:PRK09536   3 MIDVSDL----SVEFG-----DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSAR 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   553 YLHTQVAAVGQE-PLLFGRSFRENIAYG----LTRTPTMEEI--TAV--AMESGahdfisGFPQGYDTEVGEtgnqLSGG 623
Cdd:PRK09536  74 AASRRVASVPQDtSLSFEFDVRQVVEMGrtphRSRFDTWTETdrAAVerAMERT------GVAQFADRPVTS----LSGG 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   624 QRQAVALARALIRKPRLLILDDATSALDAGNQLR----VQRLLYEspewaSRTVLLITQQLSLAER-AHHILFLKEGSVC 698
Cdd:PRK09536 144 ERQRVLLARALAQATPVLLLDEPTASLDINHQVRtlelVRRLVDD-----GKTAVAAIHDLDLAARyCDELVLLADGRVR 218

                 ...
gi 2506117   699 EQG 701
Cdd:PRK09536 219 AAG 221
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
488-692 2.20e-22

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 95.38  E-value: 2.20e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   488 AYPNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVlldgeplvqydHHYLHTQVAAVGQ---E 564
Cdd:NF040873   1 GYGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV-----------RRAGGARVAYVPQrseV 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   565 PLLFGRSFRENIAYG------LTRTPTMEEITAV--AMES-GAHDFIsgfpqgyDTEVGEtgnqLSGGQRQAVALARALI 635
Cdd:NF040873  67 PDSLPLTVRDLVAMGrwarrgLWRRLTRDDRAAVddALERvGLADLA-------GRQLGE----LSGGQRQRALLAQGLA 135
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 2506117   636 RKPRLLILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQLSLAERAHHILFL 692
Cdd:NF040873 136 QEADLLLLDEPTTGLDAESRERIIALLAEEHA-RGATVVVVTHDLELVRRADPCVLL 191
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
497-663 2.21e-22

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 96.32  E-value: 2.21e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   497 VLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQVAAVGQEPLLFGRSFRENI 576
Cdd:PRK10247  22 ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTVYDNL 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   577 AYGLT---RTPTMEEITAVAMEsgahdFisGFPqgyDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDATSALDAG 653
Cdd:PRK10247 102 IFPWQirnQQPDPAIFLDDLER-----F--ALP---DTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDES 171
                        170
                 ....*....|
gi 2506117   654 NQLRVQRLLY 663
Cdd:PRK10247 172 NKHNVNEIIH 181
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
495-702 4.06e-22

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: 95.97  E-value: 4.06e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  495 VQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHylhtQVAAVG-----QEPLLFG 569
Cdd:cd03219  13 LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPH----EIARLGigrtfQIPRLFP 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  570 R-SFRENIAYGLTRT-----------PTMEEITAVAMEsgAHDFIsGFPQGYDTEVGEtgnqLSGGQRQAVALARALIRK 637
Cdd:cd03219  89 ElTVLENVMVAAQARtgsglllararREEREARERAEE--LLERV-GLADLADRPAGE----LSYGQQRRLEIARALATD 161
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2506117  638 PRLLILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGT 702
Cdd:cd03219 162 PKLLLLDEPAAGLNPEETEELAELIRELRE-RGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGT 226
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...
495-702 4.62e-22

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


Pssm-ID: 440180 [Multi-domain]  Cd Length: 257  Bit Score: 96.26  E-value: 4.62e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  495 VQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHylhtQVAAVG-----QEPLLFG 569
Cdd:COG0411  17 LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPH----RIARLGiartfQNPRLFP 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  570 R-SFRENIA------------YGLTRTP----TMEEITAVAMES----GAHDFIsgfpqgyDTEVGEtgnqLSGGQRQAV 628
Cdd:COG0411  93 ElTVLENVLvaaharlgrgllAALLRLPrarrEEREARERAEELlervGLADRA-------DEPAGN----LSYGQQRRL 161
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2506117  629 ALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGT 702
Cdd:COG0411 162 EIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGT 236
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
480-659 5.49e-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: 94.63  E-value: 5.49e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  480 VKFQDVSFAYPNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEplvqyDHHYL---HT 556
Cdd:cd03301   1 VELENVTKRFGNVT---ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGR-----DVTDLppkDR 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  557 QVAAVGQEPLLFGR-SFRENIAYGLTRTPTMEEITAVAMESGAHDFisgfpqGYDTEVGETGNQLSGGQRQAVALARALI 635
Cdd:cd03301  73 DIAMVFQNYALYPHmTVYDNIAFGLKLRKVPKDEIDERVREVAELL------QIEHLLDRKPKQLSGGQRQRVALGRAIV 146
                       170       180
                ....*....|....*....|....
gi 2506117  636 RKPRLLILDDATSALDAgnQLRVQ 659
Cdd:cd03301 147 REPKVFLMDEPLSNLDA--KLRVQ 168
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
496-697 8.74e-22

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 95.51  E-value: 8.74e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   496 QVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQY-DHHYLHTQVAAvgqepLLFGRSFRE 574
Cdd:PRK11247  26 TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEArEDTRLMFQDAR-----LLPWKKVID 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   575 NIAYGLT---RTPTMEEITAVAMESGAHDFISGfpqgydtevgetgnqLSGGQRQAVALARALIRKPRLLILDDATSALD 651
Cdd:PRK11247 101 NVGLGLKgqwRDAALQALAAVGLADRANEWPAA---------------LSGGQKQRVALARALIHRPGLLLLDEPLGALD 165
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 2506117   652 AGNQLRVQRLLyESpEWASR--TVLLITQQLS----LAERahhILFLKEGSV 697
Cdd:PRK11247 166 ALTRIEMQDLI-ES-LWQQHgfTVLLVTHDVSeavaMADR---VLLIEEGKI 212
ABC_6TM_bac_exporter_ABCB8_10_like cd18575
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ...
241-455 9.27e-22

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: 96.01  E-value: 9.27e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  241 VFRAVLHQETGFFLKNPTGSITSRVTEDTSNVCESISDKLNLFLwylgRGLCL----LAFMIWGSFYLTVVTLLSLPLLF 316
Cdd:cd18575  75 VFAHLLRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIAL----RNLLLliggLVMLFITSPKLTLLVLLVIPLVV 150
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  317 LLPRRLGKVYQSLAVKVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEmkplNKKEALAYVTEVWTMSVSG 396
Cdd:cd18575 151 LPIILFGRRVRRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEA----AFAAALRRIRARALLTALV 226
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2506117  397 MLLK----VGILYLGGQLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKI 455
Cdd:cd18575 227 IFLVfgaiVFVLWLGAHDVLAGRMSAGELSQFVFYAVLAAGSVGALSEVWGDLQRAAGAAERL 289
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
494-702 1.39e-21

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: 94.28  E-value: 1.39e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  494 NVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHylhtQVAAVG-----QEPLLF 568
Cdd:COG0410  15 GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPH----RIARLGigyvpEGRRIF 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  569 GR-SFRENI---AYGLTRTP----TMEEITAVamesgahdfisgFPqgydtEVGE----TGNQLSGGQRQAVALARALIR 636
Cdd:COG0410  91 PSlTVEENLllgAYARRDRAevraDLERVYEL------------FP-----RLKErrrqRAGTLSGGEQQMLAIGRALMS 153
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2506117  637 KPRLLILDDATSAL---------DAGNQLRVQRLlyespewasrTVLLITQQLSLA-ERAHHILFLKEGSVCEQGT 702
Cdd:COG0410 154 RPKLLLLDEPSLGLapliveeifEIIRRLNREGV----------TILLVEQNARFAlEIADRAYVLERGRIVLEGT 219
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
470-701 1.62e-21

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


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 94.72  E-value: 1.62e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  470 SLAPLNMKGLVKFQDVSFAYPNHpnvQVLQGLTFTLYPGKVTALVGPNGSGKSTvaaLLQNL--------YQPTGGKVLL 541
Cdd:COG1117   2 TAPASTLEPKIEVRNLNVYYGDK---QALKDINLDIPENKVTALIGPSGCGKST---LLRCLnrmndlipGARVEGEILL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  542 DGEPLvqYDHHY----LHTQVAAVGQEPLLFGRSFRENIAYGL-----TRTPTMEEI-----TAVAMesgahdfisgfpq 607
Cdd:COG1117  76 DGEDI--YDPDVdvveLRRRVGMVFQKPNPFPKSIYDNVAYGLrlhgiKSKSELDEIveeslRKAAL------------- 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  608 gYDtEV----GETGNQLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEwaSRTVLLIT---QQl 680
Cdd:COG1117 141 -WD-EVkdrlKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKK--DYTIVIVThnmQQ- 215
                       250       260
                ....*....|....*....|..
gi 2506117  681 slAER-AHHILFLKEGSVCEQG 701
Cdd:COG1117 216 --AARvSDYTAFFYLGELVEFG 235
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
474-702 3.04e-21

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 95.42  E-value: 3.04e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   474 LNMKGLVKFQDVS---FAYPNHpnVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYD 550
Cdd:PRK11308   6 LQAIDLKKHYPVKrglFKPERL--VKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKAD 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   551 HHY---LHTQVAAVGQ-----------------EPLLfgrsfrenIAYGLTRTPTMEEITAVAMESGAHdfisgfPQGYD 610
Cdd:PRK11308  84 PEAqklLRQKIQIVFQnpygslnprkkvgqileEPLL--------INTSLSAAERREKALAMMAKVGLR------PEHYD 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   611 tevgETGNQLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHI 689
Cdd:PRK11308 150 ----RYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHiADEV 225
                        250
                 ....*....|...
gi 2506117   690 LFLKEGSVCEQGT 702
Cdd:PRK11308 226 MVMYLGRCVEKGT 238
ABC_6TM_TmrB_like cd18541
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ...
179-427 3.56e-21

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: 94.40  E-value: 3.56e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  179 MAIPFFTGRITDWILQDK-TAPSFARNMWLMCILTIASTVLEFagdgIYNITMGHMHSRV----HGEVFRAVLHQETGFF 253
Cdd:cd18541  16 LLIPRIIGRAIDALTAGTlTASQLLRYALLILLLALLIGIFRF----LWRYLIFGASRRIeydlRNDLFAHLLTLSPSFY 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  254 LKNPTGSITSRVTEDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQSLAVKV 333
Cdd:cd18541  92 QKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLVYRLGKKIHKRFRKV 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  334 QESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEmkplNKKEALAYVTeVW-----TMSVSGMLLKVGILYLGG 408
Cdd:cd18541 172 QEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEE----YVEKNLRLAR-VDalffpLIGLLIGLSFLIVLWYGG 246
                       250
                ....*....|....*....
gi 2506117  409 QLVVRGAVSSGNLVSFVLY 427
Cdd:cd18541 247 RLVIRGTITLGDLVAFNSY 265
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
496-701 3.88e-21

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 97.85  E-value: 3.88e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   496 QVLQGLTFTLYPGKVTALVGPNGSGKSTVA-ALLQNLyqPTGGKVLLDGEPLVQYDHHYL---HTQVAAVGQEP--LLFG 569
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTTGlALLRLI--NSQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDPnsSLNP 377
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   570 R-SFRENIAYGLT-RTPTM-----EEITAVAMESGAHDFISgfPQGYDTEvgetgnqLSGGQRQAVALARALIRKPRLLI 642
Cdd:PRK15134 378 RlNVLQIIEEGLRvHQPTLsaaqrEQQVIAVMEEVGLDPET--RHRYPAE-------FSGGQRQRIAIARALILKPSLII 448
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2506117   643 LDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAeRA--HHILFLKEGSVCEQG 701
Cdd:PRK15134 449 LDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVV-RAlcHQVIVLRQGEVVEQG 508
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
503-709 5.48e-21

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: 95.17  E-value: 5.48e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  503 FTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDH-HYLHT---QVAAVGQEPLLFG-RSFRENIA 577
Cdd:COG4148  20 FTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARgIFLPPhrrRIGYVFQEARLFPhLSVRGNLL 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  578 YGLTRTPT------MEEITAVAmesGAHDFISGFPQgydtevgetgnQLSGGQRQAVALARALIRKPRLLILDDATSALD 651
Cdd:COG4148 100 YGRKRAPRaerrisFDEVVELL---GIGHLLDRRPA-----------TLSGGERQRVAIGRALLSSPRLLLMDEPLAALD 165
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2506117  652 AGnqlRVQRLL-Y-ES-PEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGTHLQLMER 709
Cdd:COG4148 166 LA---RKAEILpYlERlRDELDIPILYVSHSLDEVARlADHVVLLEQGRVVASGPLAEVLSR 224
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
498-725 6.76e-21

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: 98.48  E-value: 6.76e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117     498 LQGLTFTLYPGKVTALVGPNGSGKST-VAALLQNLyQPTGGKVLLDGeplvqydhhylhtQVAAVGQEPLLFGRSFRENI 576
Cdd:TIGR00957  654 LNGITFSIPEGALVAVVGQVGCGKSSlLSALLAEM-DKVEGHVHMKG-------------SVAYVPQQAWIQNDSLRENI 719
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117     577 AYGltrTPTMEEITAVAMESGA--HDfISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDATSALDAgn 654
Cdd:TIGR00957  720 LFG---KALNEKYYQQVLEACAllPD-LEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDA-- 793
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2506117     655 qlRVQRLLYES---PE--WASRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLMERGGCYRSMVEALAAPSD 725
Cdd:TIGR00957  794 --HVGKHIFEHvigPEgvLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFLRTYAPDEQ 867
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
497-702 6.90e-21

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: 92.40  E-value: 6.90e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  497 VLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQY--DHHylhtQVAAVGQEPLLFGR-SFR 573
Cdd:cd03299  14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLppEKR----DISYVPQNYALFPHmTVY 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  574 ENIAYGL-TRTPTMEEITAVAMEsgahdfISGFpQGYDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDATSALDA 652
Cdd:cd03299  90 KNIAYGLkKRKVDKKEIERKVLE------IAEM-LGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDV 162
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 2506117  653 GNQLRVQRLLYESPEWASRTVLLITQQL----SLAERahhILFLKEGSVCEQGT 702
Cdd:cd03299 163 RTKEKLREELKKIRKEFGVTVLHVTHDFeeawALADK---VAIMLNGKLIQVGK 213
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
467-712 7.13e-21

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 94.10  E-value: 7.13e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   467 LSGSLAPLNMKGLVKfqdvsfAYPNHpnvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPL 546
Cdd:PRK13537   1 GPMSVAPIDFRNVEK------RYGDK---LVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPV 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   547 VQYDHHyLHTQVAAVGQ----EP--------LLFGRSFRENIAYGLTRTPTMEEITavAMESGAhdfisgfpqgyDTEVG 614
Cdd:PRK13537  72 PSRARH-ARQRVGVVPQfdnlDPdftvrenlLVFGRYFGLSAAAARALVPPLLEFA--KLENKA-----------DAKVG 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   615 EtgnqLSGGQRQAVALARALIRKPRLLILDDATSALDAgnQLRvqRLLYE---SPEWASRTVLLITQQLSLAER-AHHIL 690
Cdd:PRK13537 138 E----LSGGMKRRLTLARALVNDPDVLVLDEPTTGLDP--QAR--HLMWErlrSLLARGKTILLTTHFMEEAERlCDRLC 209
                        250       260
                 ....*....|....*....|...
gi 2506117   691 FLKEGSVCEQGTHLQLMERG-GC 712
Cdd:PRK13537 210 VIEEGRKIAEGAPHALIESEiGC 232
PTZ00243 PTZ00243
ABC transporter; Provisional
462-720 7.34e-21

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 98.31  E-value: 7.34e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    462 TPCSPLSGslAPLNMK-GLVKFQDVSFAYPNHPNVqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVL 540
Cdd:PTZ00243 1292 EPASPTSA--APHPVQaGSLVFEGVQMRYREGLPL-VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIR 1368
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    541 LDGEPLVQYDHHYLHTQVAAVGQEPLLFGRSFRENIAYGLTRTPtmEEITAVAMESGAHDFISGFPQGYDTEVGETGNQL 620
Cdd:PTZ00243 1369 VNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVDPFLEASS--AEVWAALELVGLRERVASESEGIDSRVLEGGSNY 1446
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    621 SGGQRQAVALARALIRKPRLLIL-DDATSALDAGNQLRVQRLLYESpeWASRTVLLITQQLSLAERAHHILFLKEGSVCE 699
Cdd:PTZ00243 1447 SVGQRQLMCMARALLKKGSGFILmDEATANIDPALDRQIQATVMSA--FSAYTVITIAHRLHTVAQYDKIIVMDHGAVAE 1524
                         250       260
                  ....*....|....*....|..
gi 2506117    700 QGTHLQL-MERGGCYRSMVEAL 720
Cdd:PTZ00243 1525 MGSPRELvMNRQSIFHSMVEAL 1546
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
490-701 1.30e-20

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: 90.89  E-value: 1.30e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  490 PNHPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGeplvqYDhhyLHTQVAAVGQEPLLFG 569
Cdd:cd03266  13 DVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG-----FD---VVKEPAEARRRLGFVS 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  570 RSF--------RENIAY-----GLTRTPTMEEITAVAMESGAHDFIsgfpqgyDTEVGEtgnqLSGGQRQAVALARALIR 636
Cdd:cd03266  85 DSTglydrltaRENLEYfaglyGLKGDELTARLEELADRLGMEELL-------DRRVGG----FSTGMRQKVAIARALVH 153
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2506117  637 KPRLLILDDATSALD--AGNQLR-VQRLLYEspewASRTVLLITQQLSLAER-AHHILFLKEGSVCEQG 701
Cdd:cd03266 154 DPPVLLLDEPTTGLDvmATRALReFIRQLRA----LGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
477-702 1.63e-20

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


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 92.48  E-value: 1.63e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  477 KGLVKfqdvSFAypnhpNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLvQYDHhylht 556
Cdd:COG4152   5 KGLTK----RFG-----DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL-DPED----- 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  557 qVAAVG---QEPLLFGR-SFRENIAY-----GLTRtptmeeitAVAMESgAHDFISGFpqgydtEVGETGN----QLSGG 623
Cdd:COG4152  70 -RRRIGylpEERGLYPKmKVGEQLVYlarlkGLSK--------AEAKRR-ADEWLERL------GLGDRANkkveELSKG 133
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  624 QRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGT 702
Cdd:COG4152 134 NQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAA-KGTTVIFSSHQMELVEElCDRIVIINKGRKVLSGS 212
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
495-723 1.76e-20

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 91.77  E-value: 1.76e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   495 VQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQVAAVGQEP--------- 565
Cdd:PRK15112  26 VEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDPstslnprqr 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   566 --LLFGRSFRENIAygLTRTPTMEEITAVAMESG-AHDFISGFPqgydtevgetgNQLSGGQRQAVALARALIRKPRLLI 642
Cdd:PRK15112 106 isQILDFPLRLNTD--LEPEQREKQIIETLRQVGlLPDHASYYP-----------HMLAPGQKQRLGLARALILRPKVII 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   643 LDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGthlqlmerggcyrSMVEALA 721
Cdd:PRK15112 173 ADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERG-------------STADVLA 239

                 ..
gi 2506117   722 AP 723
Cdd:PRK15112 240 SP 241
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
479-695 2.26e-20

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 90.32  E-value: 2.26e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   479 LVKFQDVSFAYPNhpNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHH---YLH 555
Cdd:PRK10908   1 MIRFEHVSKAYLG--GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNRevpFLR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   556 TQVAAVGQE-PLLFGRSFRENIAYGLTRTPTMEE-----ITAVAMESGAHDFISGFPQgydtevgetgnQLSGGQRQAVA 629
Cdd:PRK10908  79 RQIGMIFQDhHLLMDRTVYDNVAIPLIIAGASGDdirrrVSAALDKVGLLDKAKNFPI-----------QLSGGEQQRVG 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2506117   630 LARALIRKPRLLILDDATSALDAGNQLRVQRlLYESPEWASRTVLLITQQLSL-AERAHHILFLKEG 695
Cdd:PRK10908 148 IARAVVNKPAVLLADEPTGNLDDALSEGILR-LFEEFNRVGVTVLMATHDIGLiSRRSYRMLTLSDG 213
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
475-650 2.27e-20

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 95.12  E-value: 2.27e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   475 NMKGLVKFQDVSFAYPNhpnVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLvqydHHYL 554
Cdd:PRK15439   7 TAPPLLCARSISKQYSG---VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPC----ARLT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   555 HTQVAAVG-----QEPLLF-GRSFRENIAYGLTRTP-TMEEITAVAMESGAHdfisgfpqgYDTEVgeTGNQLSGGQRQA 627
Cdd:PRK15439  80 PAKAHQLGiylvpQEPLLFpNLSVKENILFGLPKRQaSMQKMKQLLAALGCQ---------LDLDS--SAGSLEVADRQI 148
                        170       180
                 ....*....|....*....|...
gi 2506117   628 VALARALIRKPRLLILDDATSAL 650
Cdd:PRK15439 149 VEILRGLMRDSRILILDEPTASL 171
ABC_6TM_YknU_like cd18542
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ...
179-455 2.98e-20

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: 91.72  E-value: 2.98e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  179 MAIPFFTGRITDWILQDKtapsFARNMWLMCILTIASTVLEFAGDGIYNITMG----HMHSRVHGEVFRAVLHQETGFFL 254
Cdd:cd18542  16 LLIPLLIRRIIDSVIGGG----LRELLWLLALLILGVALLRGVFRYLQGYLAEkasqKVAYDLRNDLYDHLQRLSFSFHD 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  255 KNPTGSITSRVTEDTSNVCESISDKLNLFLwylgRGLCLLAF----MIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQSLA 330
Cdd:cd18542  92 KARTGDLMSRCTSDVDTIRRFLAFGLVELV----RAVLLFIGaliiMFSINWKLTLISLAIIPFIALFSYVFFKKVRPAF 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  331 VKVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKeaLAYVTEVW--TMSVSGMLLKVGILYLGG 408
Cdd:cd18542 168 EEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIK--LAKLLAKYwpLMDFLSGLQIVLVLWVGG 245
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 2506117  409 QLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKI 455
Cdd:cd18542 246 YLVINGEITLGELVAFISYLWMLIWPVRQLGRLINDMSRASASAERI 292
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
476-701 3.84e-20

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 90.95  E-value: 3.84e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   476 MKGLVKFQDVSFAYPNhpNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLH 555
Cdd:PRK13647   1 MDNIIEVEDLHFRYKD--GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   556 TQVAAVGQEP--LLFGRSFRENIAYG-----LTRTP----TMEEITAVAMESGAHdfisgfpqgydtevgETGNQLSGGQ 624
Cdd:PRK13647  79 SKVGLVFQDPddQVFSSTVWDDVAFGpvnmgLDKDEverrVEEALKAVRMWDFRD---------------KPPYHLSYGQ 143
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2506117   625 RQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQLSLA-ERAHHILFLKEGSVCEQG 701
Cdd:PRK13647 144 KKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHN-QGKTVIVATHDVDLAaEWADQVIVLKEGRVLAEG 220
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
494-701 5.03e-20

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 89.97  E-value: 5.03e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   494 NVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQ-----PTGGKVLLDGEPLVQYDHHYLHTQVAAVGQEP-LL 567
Cdd:PRK14247  15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPnPI 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   568 FGRSFRENIAYGL------TRTPTMEEITAVAMESGahdfisgfpQGYD---TEVGETGNQLSGGQRQAVALARALIRKP 638
Cdd:PRK14247  95 PNLSIFENVALGLklnrlvKSKKELQERVRWALEKA---------QLWDevkDRLDAPAGKLSGGQQQRLCIARALAFQP 165
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2506117   639 RLLILDDATSALDAGNQLRVQRLLYESPEwaSRTVLLITQQLSLAER-AHHILFLKEGSVCEQG 701
Cdd:PRK14247 166 EVLLADEPTANLDPENTAKIESLFLELKK--DMTIVLVTHFPQQAARiSDYVAFLYKGQIVEWG 227
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
481-659 5.17e-20

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


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 89.08  E-value: 5.17e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  481 KFQDVSFAYPNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTV-AALLQNLYQP--TGGKVLLDGEPLvqydhHYLHTQ 557
Cdd:COG4136   3 SLENLTITLGGRP---LLAPLSLTVAPGEILTLMGPSGSGKSTLlAAIAGTLSPAfsASGEVLLNGRRL-----TALPAE 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  558 VAAVG---QEPLLFGR-SFRENIAYGLTRTPTMEEITAVAM----ESGAHDFISGFPqgydtevgetgNQLSGGQRQAVA 629
Cdd:COG4136  75 QRRIGilfQDDLLFPHlSVGENLAFALPPTIGRAQRRARVEqaleEAGLAGFADRDP-----------ATLSGGQRARVA 143
                       170       180       190
                ....*....|....*....|....*....|
gi 2506117  630 LARALIRKPRLLILDDATSALDAGnqLRVQ 659
Cdd:COG4136 144 LLRALLAEPRALLLDEPFSKLDAA--LRAQ 171
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
482-677 5.37e-20

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 93.98  E-value: 5.37e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  482 FQDVSFAYPNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGeplvqydhhylHTQVAAV 561
Cdd:COG0488   1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-----------GLRIGYL 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  562 GQEPLLF-GRSFRENIAYGLTR------------------TPTMEEITAV----------AMESGAHDFIS--GFPQG-Y 609
Cdd:COG0488  67 PQEPPLDdDLTVLDTVLDGDAElraleaeleeleaklaepDEDLERLAELqeefealggwEAEARAEEILSglGFPEEdL 146
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2506117  610 DTEVGEtgnqLSGGQRQAVALARALIRKPRLLILDDATSALDAgnqlrvqrllyESPEW-----ASR--TVLLIT 677
Cdd:COG0488 147 DRPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDL-----------ESIEWleeflKNYpgTVLVVS 206
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
465-712 1.07e-19

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 91.05  E-value: 1.07e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   465 SPLSGSLAPLnmkgLVKFQDVSFAYPNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGE 544
Cdd:PRK13536  31 ASIPGSMSTV----AIDLAGVSKSYGDKA---VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGV 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   545 P--------------LVQYDHHYLHTQVaavgQEPLL-FGRSFRENIAYGLTRTPTMEEITavAMESGAhdfisgfpqgy 609
Cdd:PRK13536 104 PvpararlararigvVPQFDNLDLEFTV----RENLLvFGRYFGMSTREIEAVIPSLLEFA--RLESKA----------- 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   610 DTEVGEtgnqLSGGQRQAVALARALIRKPRLLILDDATSALDA-GNQLRVQRLlyESPEWASRTVLLITQQLSLAERAHH 688
Cdd:PRK13536 167 DARVSD----LSGGMKRRLTLARALINDPQLLILDEPTTGLDPhARHLIWERL--RSLLARGKTILLTTHFMEEAERLCD 240
                        250       260
                 ....*....|....*....|....*.
gi 2506117   689 ILFLKEG--SVCEQGTHLQLMERGGC 712
Cdd:PRK13536 241 RLCVLEAgrKIAEGRPHALIDEHIGC 266
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
501-677 1.08e-19

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 91.82  E-value: 1.08e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   501 LTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHylHTQVAAVGQEPLLFGR-SFRENIAYG 579
Cdd:PRK11607  38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPY--QRPINMMFQSYALFPHmTVEQNIAFG 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   580 LT--RTPTMEEITAVA-MESGAH--DFISGFPqgydtevgetgNQLSGGQRQAVALARALIRKPRLLILDDATSALDAGN 654
Cdd:PRK11607 116 LKqdKLPKAEIASRVNeMLGLVHmqEFAKRKP-----------HQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKL 184
                        170       180
                 ....*....|....*....|...
gi 2506117   655 QLRVQRLLYESPEWASRTVLLIT 677
Cdd:PRK11607 185 RDRMQLEVVDILERVGVTCVMVT 207
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
493-696 1.15e-19

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: 88.16  E-value: 1.15e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  493 PNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVL----LDGEPLVQYDHHYLHTQVAAVGQEPLLF 568
Cdd:cd03290  12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnkNESEPSFEATRSRNRYSVAYAAQKPWLL 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  569 GRSFRENIAYGltrTP-TMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDAT 647
Cdd:cd03290  92 NATVEENITFG---SPfNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPF 168
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 2506117  648 SALDA--GNQLrVQRLLYESPEWASRTVLLITQQLSLAERAHHILFLKEGS 696
Cdd:cd03290 169 SALDIhlSDHL-MQEGILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDGS 218
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
497-652 1.31e-19

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 90.93  E-value: 1.31e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   497 VLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLV-----QYDhhylhtqVAAVGQEPLLFGR- 570
Cdd:PRK11432  21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVThrsiqQRD-------ICMVFQSYALFPHm 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   571 SFRENIAYGLTrtptM-----EEITAVAMESGAHDFISGFPQGYDtevgetgNQLSGGQRQAVALARALIRKPRLLILDD 645
Cdd:PRK11432  94 SLGENVGYGLK----MlgvpkEERKQRVKEALELVDLAGFEDRYV-------DQISGGQQQRVALARALILKPKVLLFDE 162

                 ....*..
gi 2506117   646 ATSALDA 652
Cdd:PRK11432 163 PLSNLDA 169
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
480-685 1.43e-19

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 88.94  E-value: 1.43e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   480 VKFQDVSFAYPNHpnvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTG-----GKVLLDGEPLVQ--YDHH 552
Cdd:PRK14258   8 IKVNNLSFYYDTQ---KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYErrVNLN 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   553 YLHTQVAAVGQEPLLFGRSFRENIAYGLTRT---PTMEEITAVamESGAHDfiSGFPQGYDTEVGETGNQLSGGQRQAVA 629
Cdd:PRK14258  85 RLRRQVSMVHPKPNLFPMSVYDNVAYGVKIVgwrPKLEIDDIV--ESALKD--ADLWDEIKHKIHKSALDLSGGQQQRLC 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 2506117   630 LARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER 685
Cdd:PRK14258 161 IARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSR 216
ABC_6TM_exporter_like cd18563
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
178-455 1.54e-19

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


Pssm-ID: 350007 [Multi-domain]  Cd Length: 296  Bit Score: 89.88  E-value: 1.54e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  178 EMAIPFFTGRITDWILQDKTAPSFARNMWLMCILTIASTVLEFAGDGIYNITMGHMHSRVHG----EVFRAVLHQETGFF 253
Cdd:cd18563  15 GLVPPYLTKILIDDVLIQLGPGGNTSLLLLLVLGLAGAYVLSALLGILRGRLLARLGERITAdlrrDLYEHLQRLSLSFF 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  254 LKNPTGSITSRVTEDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQSLAVKV 333
Cdd:cd18563  95 DKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVVWGSYFFWKKIRRLFHRQ 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  334 QESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKealayVTEVWTM--SVSGMLLKVG---ILYLGG 408
Cdd:cd18563 175 WRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIR-----AEKLWATffPLLTFLTSLGtliVWYFGG 249
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 2506117  409 QLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKI 455
Cdd:cd18563 250 RQVLSGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRALTSAERI 296
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
496-701 2.59e-19

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: 86.45  E-value: 2.59e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  496 QVLQGLTFTLYPGKVTALVGPNGSGKSTVAALL--QNLYQPTGGKVLLDGEPLvqyDHHYLHTQVAAVGQEPLLFGR-SF 572
Cdd:cd03213  23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPL---DKRSFRKIIGYVPQDDILHPTlTV 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  573 RENIAYgltrtptmeeitAVAMESgahdfisgfpqgydtevgetgnqLSGGQRQAVALARALIRKPRLLILDDATSALDA 652
Cdd:cd03213 100 RETLMF------------AAKLRG-----------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDS 144
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 2506117  653 GNQLRVQRLLYESPEwASRTVLLITQQLS--LAERAHHILFLKEGSVCEQG 701
Cdd:cd03213 145 SSALQVMSLLRRLAD-TGRTIICSIHQPSseIFELFDKLLLLSQGRVIYFG 194
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
479-701 3.71e-19

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: 87.45  E-value: 3.71e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  479 LVKFQDVSFAYPNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTvaaLLQnlyqptggkvLLDGeplvqyDHHylhtqv 558
Cdd:COG1119   3 LLELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKST---LLS----------LITG------DLP------ 54
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  559 AAVGQEPLLFGRSF--------RENIAY-------GLTRTPTMEEITAvameSGAHDFIsGFPQGYDTE----------- 612
Cdd:COG1119  55 PTYGNDVRLFGERRggedvwelRKRIGLvspalqlRFPRDETVLDVVL----SGFFDSI-GLYREPTDEqrerarellel 129
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  613 ------VGETGNQLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLS-LAER 685
Cdd:COG1119 130 lglahlADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEeIPPG 209
                       250
                ....*....|....*.
gi 2506117  686 AHHILFLKEGSVCEQG 701
Cdd:COG1119 210 ITHVLLLKDGRVVAAG 225
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
500-704 8.29e-19

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


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 86.58  E-value: 8.29e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   500 GLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHylhtQVAAVG-----QEPLLFG----- 569
Cdd:PRK11300  23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGH----QIARMGvvrtfQHVRLFRemtvi 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   570 --------RSFRENIAYGLTRTPTMEEITAVAMESGAH--DFIsGFpqgydTEVG--ETGNqLSGGQRQAVALARALIRK 637
Cdd:PRK11300  99 enllvaqhQQLKTGLFSGLLKTPAFRRAESEALDRAATwlERV-GL-----LEHAnrQAGN-LAYGQQRRLEIARCMVTQ 171
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2506117   638 PRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLA-ERAHHILflkegsVCEQGTHL 704
Cdd:PRK11300 172 PEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVmGISDRIY------VVNQGTPL 233
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
485-702 1.02e-18

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: 90.13  E-value: 1.02e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  485 VSFAYPNHPnVQVLQGLTFTLYPGKVTALVGPNGSGKS-TVAALLQNLYQP---TGGKVLLDGEPLVQYDHHYLHT---- 556
Cdd:COG4172  14 VAFGQGGGT-VEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLPDPaahPSGSILFDGQDLLGLSERELRRirgn 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  557 QVAAVGQEPL-----LF--GRSFRENIA--YGLTRTPTMEEITAVAMESG---AHDFISGFPqgydtevgetgNQLSGGQ 624
Cdd:COG4172  93 RIAMIFQEPMtslnpLHtiGKQIAEVLRlhRGLSGAAARARALELLERVGipdPERRLDAYP-----------HQLSGGQ 161
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2506117  625 RQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGT 702
Cdd:COG4172 162 RQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRfADRVAVMRQGEIVEQGP 240
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
496-708 1.03e-18

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: 85.67  E-value: 1.03e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  496 QVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHylhtQVAAVG-----QEPLLFGR 570
Cdd:cd03218  14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMH----KRARLGigylpQEASIFRK 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  571 -SFRENIAYGLTRTPTMEEITAVAMESGAHDFisgfpqGYDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDATSA 649
Cdd:cd03218  90 lTVEENILAVLEIRGLSKKEREEKLEELLEEF------HITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAG 163
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2506117  650 LDAGNQLRVQRLLYESPEWAsrTVLLIT-----QQLSLAERAhHILFlkEGSVCEQGTHLQLME 708
Cdd:cd03218 164 VDPIAVQDIQKIIKILKDRG--IGVLITdhnvrETLSITDRA-YIIY--EGKVLAEGTPEEIAA 222
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
474-651 1.03e-18

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


Pssm-ID: 440718 [Multi-domain]  Cd Length: 264  Bit Score: 86.68  E-value: 1.03e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  474 LNMKGLVKfqdvSFaYPNHPN-VQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHH 552
Cdd:COG1101   2 LELKNLSK----TF-NPGTVNeKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEY 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  553 YLHTQVAAVGQEPLLfGRSFR----EN--IAY------GLTRTPTMEEITAVamesgaHDFISGFPQGY----DTEVGet 616
Cdd:COG1101  77 KRAKYIGRVFQDPMM-GTAPSmtieENlaLAYrrgkrrGLRRGLTKKRRELF------RELLATLGLGLenrlDTKVG-- 147
                       170       180       190
                ....*....|....*....|....*....|....*
gi 2506117  617 gnQLSGGQRQAVALARALIRKPRLLILDDATSALD 651
Cdd:COG1101 148 --LLSGGQRQALSLLMATLTKPKLLLLDEHTAALD 180
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
501-710 1.09e-18

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: 88.25  E-value: 1.09e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    501 LTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHH-YLHTQVAAVG---QEPLLFGR-SFREN 575
Cdd:TIGR02142  16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGiFLPPEKRRIGyvfQEARLFPHlSVRGN 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    576 IAYGLTRT------PTMEEITAVAmesgahdfisgfpqGYDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDATSA 649
Cdd:TIGR02142  96 LRYGMKRArpserrISFERVIELL--------------GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAA 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2506117    650 LDagNQLRVQRLLY-ESPEWASRT-VLLITQQLSLAER-AHHILFLKEGSVCEQGTHLQLMERG 710
Cdd:TIGR02142 162 LD--DPRKYEILPYlERLHAEFGIpILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWASP 223
cbiO PRK13644
energy-coupling factor transporter ATPase;
479-702 1.13e-18

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 86.58  E-value: 1.13e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   479 LVKFQDVSFAYPNhpNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDH-HYLHTQ 557
Cdd:PRK13644   1 MIRLENVSYSYPD--GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKlQGIRKL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   558 VAAVGQEP--LLFGRSFRENIAYG-----LTRTPTMEEITAVAMESGAHDFISGFPQgydtevgetgnQLSGGQRQAVAL 630
Cdd:PRK13644  79 VGIVFQNPetQFVGRTVEEDLAFGpenlcLPPIEIRKRVDRALAEIGLEKYRHRSPK-----------TLSGGQGQCVAL 147
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2506117   631 ARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQLSLAERAHHILFLKEGSVCEQGT 702
Cdd:PRK13644 148 AGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHE-KGKTIVYITHNLEELHDADRIIVMDRGKIVLEGE 218
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
497-702 1.26e-18

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 86.25  E-value: 1.26e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   497 VLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQ------PTGGKVLLDGEPLVQYDHHYLHTQVAAVGQEPLLFGR 570
Cdd:PRK14246  25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNPFPH 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   571 -SFRENIAYGLTRTPTME--EITAVAMESGAHdfISGFPQGYDtEVGETGNQLSGGQRQAVALARALIRKPRLLILDDAT 647
Cdd:PRK14246 105 lSIYDNIAYPLKSHGIKEkrEIKKIVEECLRK--VGLWKEVYD-RLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 2506117   648 SALDAGNQLRVQRLLYESPEwaSRTVLLITQQLSLAER-AHHILFLKEGSVCEQGT 702
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELKN--EIAIVIVSHNPQQVARvADYVAFLYNGELVEWGS 235
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
494-702 1.67e-18

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 87.83  E-value: 1.67e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   494 NVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEplvqyDHHYLHT---QVAAVGQEPLLFGR 570
Cdd:PRK10851  14 RTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGT-----DVSRLHArdrKVGFVFQHYALFRH 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   571 -SFRENIAYGLTRTPTMEEITAVAMESGAHDFI-----SGFPQGYDTevgetgnQLSGGQRQAVALARALIRKPRLLILD 644
Cdd:PRK10851  89 mTVFDNIAFGLTVLPRRERPNAAAIKAKVTQLLemvqlAHLADRYPA-------QLSGGQKQRVALARALAVEPQILLLD 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2506117   645 DATSALDAgnQLRVQ-----RLLYESPEWASrtVLLITQQLSLAERAHHILFLKEGSVCEQGT 702
Cdd:PRK10851 162 EPFGALDA--QVRKElrrwlRQLHEELKFTS--VFVTHDQEEAMEVADRVVVMSQGNIEQAGT 220
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
485-677 2.46e-18

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 85.14  E-value: 2.46e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   485 VSFAYPNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDhhylhTQVAAVGQ- 563
Cdd:PRK11248   7 LYADYGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG-----AERGVVFQn 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   564 EPLLFGRSFRENIAYGLT-RTPTMEEITAVAMESGAHDFISGFPQGYDTevgetgnQLSGGQRQAVALARALIRKPRLLI 642
Cdd:PRK11248  79 EGLLPWRNVQDNVAFGLQlAGVEKMQRLEIAHQMLKKVGLEGAEKRYIW-------QLSGGQRQRVGIARALAANPQLLL 151
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 2506117   643 LDDATSALDAGNQLRVQRLLYESPEWASRTVLLIT 677
Cdd:PRK11248 152 LDEPFGALDAFTREQMQTLLLKLWQETGKQVLLIT 186
cbiO PRK13643
energy-coupling factor transporter ATPase;
479-702 2.86e-18

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 85.94  E-value: 2.86e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   479 LVKFQDVSFAY-PNHPNV-QVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLdGEPLV-----QYDH 551
Cdd:PRK13643   1 MIKFEKVNYTYqPNSPFAsRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTV-GDIVVsstskQKEI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   552 HYLHTQVAAVGQEP--LLFGRSFRENIAYGltrtPTMEEITAVAMESGAHDFISGFpqGYDTEVGETGN-QLSGGQRQAV 628
Cdd:PRK13643  80 KPVRKKVGVVFQFPesQLFEETVLKDVAFG----PQNFGIPKEKAEKIAAEKLEMV--GLADEFWEKSPfELSGGQMRRV 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2506117   629 ALARALIRKPRLLILDDATSALDAGNQLRVQRlLYESPEWASRTVLLITQQL-SLAERAHHILFLKEGSVCEQGT 702
Cdd:PRK13643 154 AIAGILAMEPEVLVLDEPTAGLDPKARIEMMQ-LFESIHQSGQTVVLVTHLMdDVADYADYVYLLEKGHIISCGT 227
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
480-702 2.93e-18

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 86.78  E-value: 2.93e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   480 VKFQDVSFAYPNH-PNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHT-- 556
Cdd:PRK11153   2 IELKNISKVFPQGgRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKar 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   557 -QVAAVGQE-PLLFGRSFRENIAYGLT--RTPTmEEITAVAME-------SGAHDFisgFPQgydtevgetgnQLSGGQR 625
Cdd:PRK11153  82 rQIGMIFQHfNLLSSRTVFDNVALPLElaGTPK-AEIKARVTEllelvglSDKADR---YPA-----------QLSGGQK 146
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2506117   626 QAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGT 702
Cdd:PRK11153 147 QRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRiCDRVAVIDAGRLVEQGT 224
ABC_6TM_Pgp_ABCB1_D2_like cd18578
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ...
204-463 3.65e-18

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: 85.97  E-value: 3.65e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  204 NMW--LMCILTIASTVLEFAGDGIYNITMGHMHSRVHGEVFRAVLHQETGFF--LKNPTGSITSRVTEDTSNVCESISDK 279
Cdd:cd18578  52 NFWalMFLVLAIVAGIAYFLQGYLFGIAGERLTRRLRKLAFRAILRQDIAWFddPENSTGALTSRLSTDASDVRGLVGDR 131
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  280 LNLFL-----------------WYLGrgLCLLAFM--IWGSFYLtvvtllslpllfllprrLGKVYQSLAVKVQESLAKS 340
Cdd:cd18578 132 LGLILqaivtlvagliiafvygWKLA--LVGLATVplLLLAGYL-----------------RMRLLSGFEEKNKKAYEES 192
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  341 TQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKEALayvtevWTMSVSG------MLLKVGILYLGGQLVVRG 414
Cdd:cd18578 193 SKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRAL------ISGLGFGlsqsltFFAYALAFWYGGRLVANG 266
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 2506117  415 AVSSGN-LVSFVLyqLQFT-RAVEVLLSIYPSMQKSVGASEKIFEYLDRTP 463
Cdd:cd18578 267 EYTFEQfFIVFMA--LIFGaQSAGQAFSFAPDIAKAKAAAARIFRLLDRKP 315
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
476-702 4.89e-18

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


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 83.98  E-value: 4.89e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  476 MKGLVKFQDVSFAYP-------------------NHPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTvaaLLQ---NLYQ 533
Cdd:COG1134   1 MSSMIEVENVSKSYRlyhepsrslkelllrrrrtRREEFWALKDVSFEVERGESVGIIGRNGAGKST---LLKliaGILE 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  534 PTGGKVLLDGEplvqydhhylhtqVAAvgqePLLFGRSF------RENI-----AYGLTRtptmEEITAVAmesgahDFI 602
Cdd:COG1134  78 PTSGRVEVNGR-------------VSA----LLELGAGFhpeltgRENIylngrLLGLSR----KEIDEKF------DEI 130
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  603 SGFpqgydTEVGETGNQ----LSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQ 678
Cdd:COG1134 131 VEF-----AELGDFIDQpvktYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRE-SGRTVIFVSH 204
                       250       260
                ....*....|....*....|....*
gi 2506117  679 QLSLAER-AHHILFLKEGSVCEQGT 702
Cdd:COG1134 205 SMGAVRRlCDRAIWLEKGRLVMDGD 229
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
479-707 5.14e-18

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 83.86  E-value: 5.14e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   479 LVKFQDVSFAYPNHPnvqvlqgLTFTLY--PGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEplvqyDHHylHT 556
Cdd:PRK10771   1 MLKLTDITWLYHHLP-------MRFDLTveRGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQ-----DHT--TT 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   557 Q-----VAAVGQEPLLFGR-SFRENIAYGLTrtPTM-------EEITAVAMESGAHDFISGFPqgydtevgetgNQLSGG 623
Cdd:PRK10771  67 PpsrrpVSMLFQENNLFSHlTVAQNIGLGLN--PGLklnaaqrEKLHAIARQMGIEDLLARLP-----------GQLSGG 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   624 QRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGT 702
Cdd:PRK10771 134 QRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARiAPRSLVVADGRIAWDGP 213

                 ....*
gi 2506117   703 HLQLM 707
Cdd:PRK10771 214 TDELL 218
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
497-701 5.14e-18

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 84.65  E-value: 5.14e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   497 VLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQVAAVGQEPLLFGR-SFREN 575
Cdd:PRK10253  22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDiTVQEL 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   576 IAYGltRTPTM----------EEITAVAMESGAHDFISGfpQGYDTevgetgnqLSGGQRQAVALARALIRKPRLLILDD 645
Cdd:PRK10253 102 VARG--RYPHQplftrwrkedEEAVTKAMQATGITHLAD--QSVDT--------LSGGQRQRAWIAMVLAQETAIMLLDE 169
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 2506117   646 ATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQG 701
Cdd:PRK10253 170 PTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRyASHLIALREGKIVAQG 226
BtuD COG4138
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ...
494-707 7.81e-18

ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];


Pssm-ID: 443313 [Multi-domain]  Cd Length: 248  Bit Score: 83.74  E-value: 7.81e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  494 NVQV---LQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYqPTGGKVLLDGEPLVQYDHH-------YLHTQVAAVGQ 563
Cdd:COG4138   5 DVAVagrLGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAelarhraYLSQQQSPPFA 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  564 EPLLfgrsfrENIAYGLTRTPTMEEITAVaMESGAHDFisgfpqGYDTEVGETGNQLSGGQRQAVALARALIR------- 636
Cdd:COG4138  84 MPVF------QYLALHQPAGASSEAVEQL-LAQLAEAL------GLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinp 150
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2506117  637 KPRLLILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGTHLQLM 707
Cdd:COG4138 151 EGQLLLLDEPMNSLDVAQQAALDRLLRELCQ-QGITVVMSSHDLNHTLRhADRVWLLKQGKLVASGETAEVM 221
ABC_6TM_TmrA_like cd18544
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ...
178-455 9.03e-18

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


Pssm-ID: 349988 [Multi-domain]  Cd Length: 294  Bit Score: 84.36  E-value: 9.03e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  178 EMAIPFFTGRITDWILQDKTAPsfARNMWLMCILTIASTVLEFAGDGIYNITMGH-----MHS-RVhgEVFRAVLHQETG 251
Cdd:cd18544  15 ELLGPLLIKRAIDDYIVPGQGD--LQGLLLLALLYLGLLLLSFLLQYLQTYLLQKlgqriIYDlRR--DLFSHIQRLPLS 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  252 FFLKNPTGSITSRVTEDTsnvcESISDKLNLFLWYLGRGLCLL----AFMIWGSFYLTVVTLLS----LPLLFLLPRRLG 323
Cdd:cd18544  91 FFDRTPVGRLVTRVTNDT----EALNELFTSGLVTLIGDLLLLigilIAMFLLNWRLALISLLVlpllLLATYLFRKKSR 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  324 KVYQslavKVQESLAK-STQVAlEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKEALAYVTEVWTMSVSGMLLKVG 402
Cdd:cd18544 167 KAYR----EVREKLSRlNAFLQ-ESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELLSSLALAL 241
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 2506117  403 ILYLGGQLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKI 455
Cdd:cd18544 242 VLWYGGGQVLSGAVTLGVLYAFIQYIQRFFRPIRDLAEKFNILQSAMASAERI 294
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
498-685 1.06e-17

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: 82.90  E-value: 1.06e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    498 LQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLvqydhhylhtqvaavgQEP------------ 565
Cdd:TIGR01184   1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQI----------------TEPgpdrmvvfqnys 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    566 LLFGRSFRENIAYGLTRT-PTM----------EEITAVAMESGAHDFISgfpqgydtevgetgnQLSGGQRQAVALARAL 634
Cdd:TIGR01184  65 LLPWLTVRENIALAVDRVlPDLskserraiveEHIALVGLTEAADKRPG---------------QLSGGMKQRVAIARAL 129
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2506117    635 IRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLIT----QQLSLAER 685
Cdd:TIGR01184 130 SIRPKVLLLDEPFGALDALTRGNLQEELMQIWEEHRVTVLMVThdvdEALLLSDR 184
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
476-685 1.19e-17

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 83.29  E-value: 1.19e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   476 MKGLVKFQDVSFAYPNHpnvQVLQGLTFTLYPGKVTALVGPNGSGKSTvaaLLQNLYQ--------PTGGKVLLDGEPLV 547
Cdd:PRK14239   2 TEPILQVSDLSVYYNKK---KALNSVSLDFYPNEITALIGPSGSGKST---LLRSINRmndlnpevTITGSIVYNGHNIY 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   548 --QYDHHYLHTQVAAVGQEPLLFGRSFRENIAYGLTRTPTME-EITAVAMES---GAHDFISGFPQGYDTEVGetgnqLS 621
Cdd:PRK14239  76 spRTDTVDLRKEIGMVFQQPNPFPMSIYENVVYGLRLKGIKDkQVLDEAVEKslkGASIWDEVKDRLHDSALG-----LS 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2506117   622 GGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEwaSRTVLLITQQLSLAER 685
Cdd:PRK14239 151 GGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKD--DYTMLLVTRSMQQASR 212
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
484-711 1.37e-17

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 83.52  E-value: 1.37e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   484 DVSFAYPNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLvQYDHH---YLHTQVAA 560
Cdd:PRK13638   6 DLWFRYQDEP---VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL-DYSKRgllALRQQVAT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   561 VGQEP--LLFGRSFRENIAYGLTRTPTME-EITAVAMESGAHDFISGFPQgydtevgETGNQLSGGQRQAVALARALIRK 637
Cdd:PRK13638  82 VFQDPeqQIFYTDIDSDIAFSLRNLGVPEaEITRRVDEALTLVDAQHFRH-------QPIQCLSHGQKKRVAIAGALVLQ 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   638 PRLLILDDATSALDAGNQLR----VQRLLYEspewaSRTVLLITQQLSLA-ERAHHILFLKEGSVCEQG------THLQL 706
Cdd:PRK13638 155 ARYLLLDEPTAGLDPAGRTQmiaiIRRIVAQ-----GNHVIISSHDIDLIyEISDAVYVLRQGQILTHGapgevfACTEA 229

                 ....*
gi 2506117   707 MERGG 711
Cdd:PRK13638 230 MEQAG 234
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
479-706 1.48e-17

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 86.30  E-value: 1.48e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   479 LVKFQDVSFAYPNHPNV-QVLQGLTFTLYPGKVTALVGPNGSGKSTVA-ALLQNLYQP----TGGKVLLDGEPLVQYDHH 552
Cdd:PRK15134   5 LLAIENLSVAFRQQQTVrTVVNDVSLQIEAGETLALVGESGSGKSVTAlSILRLLPSPpvvyPSGDIRFHGESLLHASEQ 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   553 YLH----TQVAAVGQEPLL-------FGRSFRENIAY--GLTRTPTMEEITAVAMESG---AHDFISGFPqgydtevget 616
Cdd:PRK15134  85 TLRgvrgNKIAMIFQEPMVslnplhtLEKQLYEVLSLhrGMRREAARGEILNCLDRVGirqAAKRLTDYP---------- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   617 gNQLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEG 695
Cdd:PRK15134 155 -HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKlADRVAVMQNG 233
                        250
                 ....*....|.
gi 2506117   696 SVCEQGTHLQL 706
Cdd:PRK15134 234 RCVEQNRAATL 244
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
479-702 1.64e-17

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 83.36  E-value: 1.64e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   479 LVKFQDVSFAYPNhpNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPlVQYDHH---YLH 555
Cdd:PRK13636   5 ILKVEELNYNYSD--GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKP-IDYSRKglmKLR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   556 TQVAAVGQEP--LLFGRSFRENIAYGLT--RTPTMEEITAV--AMESGAHDFISGFPQgydtevgetgNQLSGGQRQAVA 629
Cdd:PRK13636  82 ESVGMVFQDPdnQLFSASVYQDVSFGAVnlKLPEDEVRKRVdnALKRTGIEHLKDKPT----------HCLSFGQKKRVA 151
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2506117   630 LARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSL-AERAHHILFLKEGSVCEQGT 702
Cdd:PRK13636 152 IAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIvPLYCDNVFVMKEGRVILQGN 225
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
494-662 2.13e-17

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 81.46  E-value: 2.13e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   494 NVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDH----HYLHTQVAAvgqEPLLfg 569
Cdd:PRK13539  14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVaeacHYLGHRNAM---KPAL-- 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   570 rSFRENIA-----YGLTRTPTMEEITAVAMESGAHdfisgFPQGYdtevgetgnqLSGGQRQAVALARALIRKPRLLILD 644
Cdd:PRK13539  89 -TVAENLEfwaafLGGEELDIAAALEAVGLAPLAH-----LPFGY----------LSAGQKRRVALARLLVSNRPIWILD 152
                        170
                 ....*....|....*...
gi 2506117   645 DATSALDAGNQLRVQRLL 662
Cdd:PRK13539 153 EPTAALDAAAVALFAELI 170
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
474-650 2.48e-17

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 85.46  E-value: 2.48e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  474 LNMKGLVKfqdvSFaypnhPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYD-HH 552
Cdd:COG3845   6 LELRGITK----RF-----GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSpRD 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  553 YLHTQVAAVGQEPLLFGR-SFRENIAYGLTRTPTM--------EEITAVAMEsgahdfiSGFPQGYDTEVGetgnQLSGG 623
Cdd:COG3845  77 AIALGIGMVHQHFMLVPNlTVAENIVLGLEPTKGGrldrkaarARIRELSER-------YGLDVDPDAKVE----DLSVG 145
                       170       180
                ....*....|....*....|....*..
gi 2506117  624 QRQAVALARALIRKPRLLILDDATSAL 650
Cdd:COG3845 146 EQQRVEILKALYRGARILILDEPTAVL 172
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
482-696 2.98e-17

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 85.63  E-value: 2.98e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  482 FQDVSFAypnHPNVQVL-QGLTFTLYPGKVTALVGPNGSGKSTvaaLLQ---NLYQPTGGKVLL-DGEplvqydhhylht 556
Cdd:COG4178 365 LEDLTLR---TPDGRPLlEDLSLSLKPGERLLITGPSGSGKST---LLRaiaGLWPYGSGRIARpAGA------------ 426
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  557 QVAAVGQEPLLFGRSFRENIAY-GLTRTPTMEEITAVAMESGAHDFISGFpqgyDTEVgETGNQLSGGQRQAVALARALI 635
Cdd:COG4178 427 RVLFLPQRPYLPLGTLREALLYpATAEAFSDAELREALEAVGLGHLAERL----DEEA-DWDQVLSLGEQQRLAFARLLL 501
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2506117  636 RKPRLLILDDATSALDAGNQLRVQRLLYEspEWASRTVLLITQQLSLAERAHHILFLKEGS 696
Cdd:COG4178 502 HKPDWLFLDEATSALDEENEAALYQLLRE--ELPGTTVISVGHRSTLAAFHDRVLELTGDG 560
CeuD COG4604
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ...
480-707 3.94e-17

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


Pssm-ID: 443654 [Multi-domain]  Cd Length: 252  Bit Score: 81.67  E-value: 3.94e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  480 VKFQDVSFAYPNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQVA 559
Cdd:COG4604   2 IEIKNVSKRYGGKV---VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLA 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  560 AVGQEPLLFGR-SFRENIAYGltRTP------TMEEITAVA-------MESGAHDFIsgfpqgydtevgetgNQLSGGQR 625
Cdd:COG4604  79 ILRQENHINSRlTVRELVAFG--RFPyskgrlTAEDREIIDeaiayldLEDLADRYL---------------DELSGGQR 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  626 QAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGTHL 704
Cdd:COG4604 142 QRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCyADHIVAMKDGRVVAQGTPE 221

                ...
gi 2506117  705 QLM 707
Cdd:COG4604 222 EII 224
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
508-702 4.92e-17

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


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 83.93  E-value: 4.92e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   508 GKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLH----TQVAAVGQE-PLLFGRSFRENIAYGLT- 581
Cdd:PRK10070  54 GEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrKKIAMVFQSfALMPHMTVLDNTAFGMEl 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   582 --------RTPTMEEITAVAMESGAHdfisGFPqgydtevgetgNQLSGGQRQAVALARALIRKPRLLILDDATSALDAG 653
Cdd:PRK10070 134 aginaeerREKALDALRQVGLENYAH----SYP-----------DELSGGMRQRVGLARALAINPDILLMDEAFSALDPL 198
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 2506117   654 NQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGT 702
Cdd:PRK10070 199 IRTEMQDELVKLQAKHQRTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGT 248
ABC_6TM_ABCB8_like cd18574
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ...
233-426 6.12e-17

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


Pssm-ID: 350018 [Multi-domain]  Cd Length: 295  Bit Score: 81.82  E-value: 6.12e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  233 MHSRVHGEVFRAVLHQETGFFLKNPTGSITSRVTEDT----SNVCESISDKLNLFLWYLGRGLCLlaFMIwgSFYLTVVT 308
Cdd:cd18574  73 VAARLRNDLFSSLLRQDIAFFDTHRTGELVNRLTADVqefkSSFKQCVSQGLRSVTQTVGCVVSL--YLI--SPKLTLLL 148
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  309 LLSLPLLFLLPRRLGKVYQSLAVKVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKeaLAYVTE 388
Cdd:cd18574 149 LVIVPVVVLVGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYEEEVEKAAKLNEK--LGLGIG 226
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 2506117  389 VWTM----SVSGMLLkvGILYLGGQLVVRGAVSSGNLVSFVL 426
Cdd:cd18574 227 IFQGlsnlALNGIVL--GVLYYGGSLVSRGELTAGDLMSFLV 266
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
497-684 7.87e-17

Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.


Pssm-ID: 213198 [Multi-domain]  Cd Length: 201  Bit Score: 79.46  E-value: 7.87e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  497 VLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYlHTQVAAVGQEPLLFGR-SFREN 575
Cdd:cd03231  15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSI-ARGLLYLGHAPGIKTTlSVLEN 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  576 IAY--GLTRTPTMEEITAVAMESGAHDFISgfpqgydtevgetgNQLSGGQRQAVALARALIRKPRLLILDDATSALDAG 653
Cdd:cd03231  94 LRFwhADHSDEQVEEALARVGLNGFEDRPV--------------AQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKA 159
                       170       180       190
                ....*....|....*....|....*....|.
gi 2506117  654 NQLRVQRLLYESPEWASRTVLLITQQLSLAE 684
Cdd:cd03231 160 GVARFAEAMAGHCARGGMVVLTTHQDLGLSE 190
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
478-701 1.02e-16

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: 79.88  E-value: 1.02e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  478 GLVKFQDVSFAYPNHPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGeplvqydhhylhtQ 557
Cdd:cd03220  18 SSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG-------------R 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  558 VAA-----VGQEPLLFGrsfRENI-----AYGLTRtptmEEITAVAmesgahDFISGFpqgydTEVGETGNQ----LSGG 623
Cdd:cd03220  85 VSSllglgGGFNPELTG---RENIylngrLLGLSR----KEIDEKI------DEIIEF-----SELGDFIDLpvktYSSG 146
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2506117  624 QRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQLSLAER-AHHILFLKEGSVCEQG 701
Cdd:cd03220 147 MKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLK-QGKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
480-690 1.04e-16

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: 77.96  E-value: 1.04e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  480 VKFQDVSFAYPNHPnvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVlldgeplvqydHHYLHTQVA 559
Cdd:cd03223   1 IELENLSLATPDGR--VLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI-----------GMPEGEDLL 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  560 AVGQEPLLFGRSFRENIAYgltrtPTMEEitavamesgahdfisgfpqgydtevgetgnqLSGGQRQAVALARALIRKPR 639
Cdd:cd03223  68 FLPQRPYLPLGTLREQLIY-----PWDDV-------------------------------LSGGEQQRLAFARLLLHKPK 111
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 2506117  640 LLILDDATSALDAGNQLRVQRLLYEspewASRTVLLITQQLSLAERAHHIL 690
Cdd:cd03223 112 FVFLDEATSALDEESEDRLYQLLKE----LGITVISVGHRPSLWKFHDRVL 158
SufC COG0396
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ...
494-722 1.05e-16

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


Pssm-ID: 440165 [Multi-domain]  Cd Length: 245  Bit Score: 80.11  E-value: 1.05e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  494 NVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNL--YQPTGGKVLLDGEPLV----------------QY------ 549
Cdd:COG0396  12 GKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDILelspderaragiflafQYpveipg 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  550 --DHHYLHTQVAAVGQEPLLFgRSFRENIAygltrtptmEEITAVAMesgAHDFIsgfpqgyDTEVGETgnqLSGGQRQA 627
Cdd:COG0396  92 vsVSNFLRTALNARRGEELSA-REFLKLLK---------EKMKELGL---DEDFL-------DRYVNEG---FSGGEKKR 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  628 VALARALIRKPRLLILD--------DATSALDAG-NQLRvqrllyeSPEwasRTVLLITQQLSLAE--RAHHILFLKEGS 696
Cdd:COG0396 149 NEILQMLLLEPKLAILDetdsgldiDALRIVAEGvNKLR-------SPD---RGILIITHYQRILDyiKPDFVHVLVDGR 218
                       250       260
                ....*....|....*....|....*....
gi 2506117  697 VCEQGTH---LQLMERGgcYRSMVEALAA 722
Cdd:COG0396 219 IVKSGGKelaLELEEEG--YDWLKEEAAA 245
cbiO PRK13646
energy-coupling factor transporter ATPase;
480-702 1.53e-16

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 80.59  E-value: 1.53e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   480 VKFQDVSFAYPNHP--NVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQY--DHHYLH 555
Cdd:PRK13646   3 IRFDNVSYTYQKGTpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKtkDKYIRP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   556 T--QVAAVGQ--EPLLFGRSFRENIAYGltrtPTMEEITAVAMESGAHDFIS--GFPQGYdteVGETGNQLSGGQRQAVA 629
Cdd:PRK13646  83 VrkRIGMVFQfpESQLFEDTVEREIIFG----PKNFKMNLDEVKNYAHRLLMdlGFSRDV---MSQSPFQMSGGQMRKIA 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2506117   630 LARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLS-LAERAHHILFLKEGSVCEQGT 702
Cdd:PRK13646 156 IVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNeVARYADEVIVMKEGSIVSQTS 229
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
495-664 1.75e-16

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: 79.02  E-value: 1.75e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  495 VQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLldgeplvqYDHHYLHTQVAAVGQEPLLFGRsfRE 574
Cdd:COG4778  24 LPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSIL--------VRHDGGWVDLAQASPREILALR--RR 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  575 NIAY------GLTRTPTMEeitaVAMESGAHdfisgfpQGYDTEV-----GETGNQL--------------SGGQRQAVA 629
Cdd:COG4778  94 TIGYvsqflrVIPRVSALD----VVAEPLLE-------RGVDREEararaRELLARLnlperlwdlppatfSGGEQQRVN 162
                       170       180       190
                ....*....|....*....|....*....|....*
gi 2506117  630 LARALIRKPRLLILDDATSALDAGNQLRVQRLLYE 664
Cdd:COG4778 163 IARGFIADPPLLLLDEPTASLDAANRAVVVELIEE 197
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
486-685 2.40e-16

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: 78.91  E-value: 2.40e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  486 SFAYPNHPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGE-PLVQYDHHyLHTQVAAVGQE 564
Cdd:cd03267  25 SLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLvPWKRRKKF-LRRIGVVFGQK 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  565 PLLF-----GRSFRENIA-YGLTR---TPTMEEITAvAMESGAHdfisgfpqgYDTEVgetgNQLSGGQRQAVALARALI 635
Cdd:cd03267 104 TQLWwdlpvIDSFYLLAAiYDLPParfKKRLDELSE-LLDLEEL---------LDTPV----RQLSLGQRMRAEIAAALL 169
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 2506117  636 RKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQL----SLAER 685
Cdd:cd03267 170 HEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMkdieALARR 223
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
478-697 2.82e-16

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: 79.51  E-value: 2.82e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  478 GLVKFQDVSFAYPNHPNVqVLQGLTFTLYPGKVTALVGPNGSGKSTV-AALLQNLYqpTGGKVLLDGeplVQYDHHYLHT 556
Cdd:cd03289   1 GQMTVKDLTAKYTEGGNA-VLENISFSISPGQRVGLLGRTGSGKSTLlSAFLRLLN--TEGDIQIDG---VSWNSVPLQK 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  557 QVAAVG---QEPLLFGRSFRENI-AYGLTRTptmEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALAR 632
Cdd:cd03289  75 WRKAFGvipQKVFIFSGTFRKNLdPYGKWSD---EEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLAR 151
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2506117  633 ALIRKPRLLILDDATSALDAGNQLRVQRLLYESpeWASRTVLLITQQLSLAERAHHILFLKEGSV 697
Cdd:cd03289 152 SVLSKAKILLLDEPSAHLDPITYQVIRKTLKQA--FADCTVILSEHRIEAMLECQRFLVIEENKV 214
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
476-697 2.83e-16

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 82.85  E-value: 2.83e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   476 MKGLVKFQDVSFAYPN-HPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYL 554
Cdd:PRK10535   1 MTALLELKDIRRSYPSgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADAL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   555 htqvAAVGQEPllFGRSFREniaYGLTRTPTME---EITAV-------AMESGAHDFISGFpqGYDTEVGETGNQLSGGQ 624
Cdd:PRK10535  81 ----AQLRREH--FGFIFQR---YHLLSHLTAAqnvEVPAVyaglerkQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQ 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2506117   625 RQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQLSLAERAHHILFLKEGSV 697
Cdd:PRK10535 150 QQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRD-RGHTVIIVTHDPQVAAQAERVIEIRDGEI 221
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
476-702 3.52e-16

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 79.36  E-value: 3.52e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   476 MKGLVKFQDVSFAYPNHPNVQ---VLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHH 552
Cdd:PRK13633   1 MNEMIKCKNVSYKYESNEESTeklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   553 Y-LHTQVAAVGQEP--LLFGRSFRENIAYG---LTRTPtmEEITAVAMES----GAHDFISGFPqgydtevgetgNQLSG 622
Cdd:PRK13633  81 WdIRNKAGMVFQNPdnQIVATIVEEDVAFGpenLGIPP--EEIRERVDESlkkvGMYEYRRHAP-----------HLLSG 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   623 GQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAERAHHILFLKEGSVCEQGT 702
Cdd:PRK13633 148 GQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGT 227
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
498-702 3.53e-16

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: 78.18  E-value: 3.53e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  498 LQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQyDHHYLHTQVAAVGQEPLLFGR-SFRENI 576
Cdd:cd03265  16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLSVDDElTGWENL 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  577 A-----YGLTRTPTMEEITAVAmesgahDFIsgfpqgydtEVGETGNQL----SGGQRQAVALARALIRKPRLLILDDAT 647
Cdd:cd03265  95 YiharlYGVPGAERRERIDELL------DFV---------GLLEAADRLvktySGGMRRRLEIARSLVHRPEVLFLDEPT 159
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 2506117  648 SALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGT 702
Cdd:cd03265 160 IGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGT 215
ABC_6TM_Tm288_like cd18547
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ...
180-455 4.13e-16

Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349991 [Multi-domain]  Cd Length: 298  Bit Score: 79.75  E-value: 4.13e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  180 AIPFFTGRITDWILQDKTAPS------FARNMWLMCILTIASTVLEFagdgIYNITMGHMHSRV----HGEVFRAVLHQE 249
Cdd:cd18547  17 LGPYLLGKAIDLIIEGLGGGGgvdfsgLLRILLLLLGLYLLSALFSY----LQNRLMARVSQRTvydlRKDLFEKLQRLP 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  250 TGFFLKNPTGSITSRVTEDTSNVCESISDKLNLFLwylgRGLCL----LAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKV 325
Cdd:cd18547  93 LSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLI----SSILTivgtLIMMLYISPLLTLIVLVTVPLSLLVTKFIAKR 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  326 YQSLAVKVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKK-EALAYVTEVWTMSVSGMLLkVGIL 404
Cdd:cd18547 169 SQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFKaQFYSGLLMPIMNFINNLGY-VLVA 247
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 2506117  405 YLGGQLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKI 455
Cdd:cd18547 248 VVGGLLVINGALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAGAERV 298
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
493-652 4.15e-16

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 81.88  E-value: 4.15e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   493 PNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPlVQYDH--HYLHTQVAAVGQE----PL 566
Cdd:PRK11288  15 PGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQE-MRFASttAALAAGVAIIYQElhlvPE 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   567 LfgrSFRENI-------AYGLTRTPTMEEITAVAMESGAHDFISGFPQGYdtevgetgnqLSGGQRQAVALARALIRKPR 639
Cdd:PRK11288  94 M---TVAENLylgqlphKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKY----------LSIGQRQMVEIAKALARNAR 160
                        170
                 ....*....|...
gi 2506117   640 LLILDDATSALDA 652
Cdd:PRK11288 161 VIAFDEPTSSLSA 173
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
497-652 4.79e-16

heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]


Pssm-ID: 273491 [Multi-domain]  Cd Length: 198  Bit Score: 77.01  E-value: 4.79e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    497 VLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYlHTQVAAVGQEPLLFGR-SFREN 575
Cdd:TIGR01189  15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEP-HENILYLGHLPGLKPElSALEN 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    576 I----AYGLTRTPTMEEITAVAMESGAHDFISgfpqgydtevgetgNQLSGGQRQAVALARALIRKPRLLILDDATSALD 651
Cdd:TIGR01189  94 LhfwaAIHGGAQRTIEDALAAVGLTGFEDLPA--------------AQLSAGQQRRLALARLWLSRRPLWILDEPTTALD 159

                  .
gi 2506117    652 A 652
Cdd:TIGR01189 160 K 160
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
496-701 8.04e-16

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 78.09  E-value: 8.04e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   496 QVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGE----------PLVQYDHHYLH---TQVAAVG 562
Cdd:PRK10619  19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQtinlvrdkdgQLKVADKNQLRllrTRLTMVF 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   563 QEPLLFGR-SFRENI------AYGLTRTPTMEEITAVAMESGahdfISGFPQGydtevgETGNQLSGGQRQAVALARALI 635
Cdd:PRK10619  99 QHFNLWSHmTVLENVmeapiqVLGLSKQEARERAVKYLAKVG----IDERAQG------KYPVHLSGGQQQRVSIARALA 168
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   636 RKPRLLILDDATSALD---AGNQLRVQRLLYESpewaSRTVLLITQQLSLAER-AHHILFLKEGSVCEQG 701
Cdd:PRK10619 169 MEPEVLLFDEPTSALDpelVGEVLRIMQQLAEE----GKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEG 234
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
497-706 8.06e-16

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: 78.36  E-value: 8.06e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  497 VLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGeplvqydhhylhtQVAAVGQEPLLFGRSFRENI 576
Cdd:cd03291  52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWIMPGTIKENI 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  577 AYGLT----RTPTMeeITAVAMESGahdfISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDATSALDa 652
Cdd:cd03291 119 IFGVSydeyRYKSV--VKACQLEED----ITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLD- 191
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 2506117  653 gnqLRVQRLLYES---PEWASRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQL 706
Cdd:cd03291 192 ---VFTEKEIFEScvcKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
480-677 9.24e-16

ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.


Pssm-ID: 213188 [Multi-domain]  Cd Length: 144  Bit Score: 74.79  E-value: 9.24e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  480 VKFQDVSFAYPNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGeplvqydhhylhtqva 559
Cdd:cd03221   1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS---------------- 61
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  560 avgqepllfgrsfRENIAYgltrtptmeeitavamesgahdfisgFPqgydtevgetgnQLSGGQRQAVALARALIRKPR 639
Cdd:cd03221  62 -------------TVKIGY--------------------------FE------------QLSGGEKMRLALAKLLLENPN 90
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 2506117  640 LLILDDATSALDAGNQLRVQRLLYESPewasRTVLLIT 677
Cdd:cd03221  91 LLLLDEPTNHLDLESIEALEEALKEYP----GTVILVS 124
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
480-661 9.26e-16

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


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 79.50  E-value: 9.26e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   480 VKFQDVSFAYPNhpNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDG------EPlVQYDhhy 553
Cdd:PRK11650   4 LKLQAVRKSYDG--KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGrvvnelEP-ADRD--- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   554 lhtqVAAVGQEPLLFGR-SFRENIAYGLT--RTPTmEEI------TAVAMESGAhdFISGFPQgydtevgetgnQLSGGQ 624
Cdd:PRK11650  78 ----IAMVFQNYALYPHmSVRENMAYGLKirGMPK-AEIeervaeAARILELEP--LLDRKPR-----------ELSGGQ 139
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 2506117   625 RQAVALARALIRKPRLLILDDATSALDAgnQLRVQ-RL 661
Cdd:PRK11650 140 RQRVAMGRAIVREPAVFLFDEPLSNLDA--KLRVQmRL 175
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
497-697 9.67e-16

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: 81.88  E-value: 9.67e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117     497 VLQGLTFTLYPGKVTALVGPNGSGKSTV-AALLQNLyqPTGGKVLLDGeplVQYDHHYLHTQVAAVG---QEPLLFGRSF 572
Cdd:TIGR01271 1234 VLQDLSFSVEGGQRVGLLGRTGSGKSTLlSALLRLL--STEGEIQIDG---VSWNSVTLQTWRKAFGvipQKVFIFSGTF 1308
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117     573 RENIaygltrTP----TMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDATS 648
Cdd:TIGR01271 1309 RKNL------DPyeqwSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSA 1382
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 2506117     649 ALDAGNQLRVQRLLYESpeWASRTVLLITQQLSLAERAHHILFLKEGSV 697
Cdd:TIGR01271 1383 HLDPVTLQIIRKTLKQS--FSNCTVILSEHRVEALLECQQFLVIEGSSV 1429
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
497-706 1.48e-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: 81.11  E-value: 1.48e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117     497 VLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGeplvqydhhylhtQVAAVGQEPLLFGRSFRENI 576
Cdd:TIGR01271  441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPGTIKDNI 507
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117     577 AYGLTRTPTmeEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDATSALDagnqL 656
Cdd:TIGR01271  508 IFGLSYDEY--RYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLD----V 581
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2506117     657 RVQRLLYES---PEWASRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQL 706
Cdd:TIGR01271  582 VTEKEIFESclcKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSEL 634
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
485-703 1.84e-15

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 76.59  E-value: 1.84e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   485 VSFAYPNHpnvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEplvQYDHHY---------LH 555
Cdd:PRK11124   8 INCFYGAH---QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGN---HFDFSKtpsdkaireLR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   556 TQVAAVGQE----PLLfgrSFRENI------AYGLTRTPTMEEitavAMESGAH----DFISGFPQgydtevgetgnQLS 621
Cdd:PRK11124  82 RNVGMVFQQynlwPHL---TVQQNLieapcrVLGLSKDQALAR----AEKLLERlrlkPYADRFPL-----------HLS 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   622 GGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQLSLAER-AHHILFLKEGSVCEQ 700
Cdd:PRK11124 144 GGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAE-TGITQVIVTHEVEVARKtASRVVYMENGHIVEQ 222

                 ...
gi 2506117   701 GTH 703
Cdd:PRK11124 223 GDA 225
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
479-685 2.30e-15

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 76.74  E-value: 2.30e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   479 LVKFQDVSFAYPNHPNVQvlqGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQ--PTG---GKVLLDGEPLvqYDHHY 553
Cdd:PRK14243  10 VLRTENLNVYYGSFLAVK---NVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGFrveGKVTFHGKNL--YAPDV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   554 ----LHTQVAAVGQEPLLFGRSFRENIAYG---LTRTPTMEEITAVAMESGAHdfisgfpqgYDtEVG----ETGNQLSG 622
Cdd:PRK14243  85 dpveVRRRIGMVFQKPNPFPKSIYDNIAYGariNGYKGDMDELVERSLRQAAL---------WD-EVKdklkQSGLSLSG 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2506117   623 GQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEwaSRTVLLITQQLSLAER 685
Cdd:PRK14243 155 GQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKE--QYTIIIVTHNMQQAAR 215
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
474-652 2.39e-15

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 79.59  E-value: 2.39e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   474 LNMKGLVKfqdvSFaypnhPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYqPTG---GKVLLDGEPLVQyd 550
Cdd:PRK13549   6 LEMKNITK----TF-----GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHGtyeGEIIFEGEELQA-- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   551 HHYLHTQ---VAAVGQEPLLF-GRSFRENIAYGltrtptmEEITA------VAMESGAHDFISGFPQGYD--TEVGETGn 618
Cdd:PRK13549  74 SNIRDTEragIAIIHQELALVkELSVLENIFLG-------NEITPggimdyDAMYLRAQKLLAQLKLDINpaTPVGNLG- 145
                        170       180       190
                 ....*....|....*....|....*....|....
gi 2506117   619 qlsGGQRQAVALARALIRKPRLLILDDATSALDA 652
Cdd:PRK13549 146 ---LGQQQLVEIAKALNKQARLLILDEPTASLTE 176
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
495-701 2.65e-15

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: 75.77  E-value: 2.65e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  495 VQVLQGLTFTLYPGKVTALVGPNGSGKST----VAALLQNLYQpTGGKVLLDGEPLvqyDHHYLHTQVAAVGQ-EPLLFG 569
Cdd:cd03234  20 ARILNDVSLHVESGQVMAILGSSGSGKTTlldaISGRVEGGGT-TSGQILFNGQPR---KPDQFQKCVAYVRQdDILLPG 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  570 RSFRENIAYGLT-RTPT---------MEEIT---AVAMESGAHDFISGfpqgydtevgetgnqLSGGQRQAVALARALIR 636
Cdd:cd03234  96 LTVRETLTYTAIlRLPRkssdairkkRVEDVllrDLALTRIGGNLVKG---------------ISGGERRRVSIAVQLLW 160
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2506117  637 KPRLLILDDATSALDAGNQLRVQRLLYESPEwASRTVLL-ITQQLS-LAERAHHILFLKEGSVCEQG 701
Cdd:cd03234 161 DPKVLILDEPTSGLDSFTALNLVSTLSQLAR-RNRIVILtIHQPRSdLFRLFDRILLLSSGEIVYSG 226
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
479-651 3.45e-15

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 78.95  E-value: 3.45e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  479 LVKFQDVSFAYPNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLdGEPLVQ-Y---DHHYL 554
Cdd:COG0488 315 VLELEGLSKSYGDKT---LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVKIgYfdqHQEEL 390
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  555 HTqvaavgqepllfGRSFRENIAYGLtrtPTMEEITAVAMesgAHDFisGFPqGYD--TEVGEtgnqLSGGQRQAVALAR 632
Cdd:COG0488 391 DP------------DKTVLDELRDGA---PGGTEQEVRGY---LGRF--LFS-GDDafKPVGV----LSGGEKARLALAK 445
                       170
                ....*....|....*....
gi 2506117  633 ALIRKPRLLILDDATSALD 651
Cdd:COG0488 446 LLLSPPNVLLLDEPTNHLD 464
hmuV PRK13547
heme ABC transporter ATP-binding protein;
497-725 3.84e-15

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 76.40  E-value: 3.84e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   497 VLQGLTFTLYPGKVTALVGPNGSGKSTV----AALLQNLYQPTG----GKVLLDGEPLVQYDHHYLHTQVAAVGQ--EPl 566
Cdd:PRK13547  16 ILRDLSLRIEPGRVTALLGRNGAGKSTLlkalAGDLTGGGAPRGarvtGDVTLNGEPLAAIDAPRLARLRAVLPQaaQP- 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   567 LFGRSFRENIAYGltRTPTMEEITAVAMESGAHDFISGFPQGYDTEVGETGNQLSGGQRQAVALARAL---------IRK 637
Cdd:PRK13547  95 AFAFSAREIVLLG--RYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQP 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   638 PRLLILDDATSALDAGNQLR----VQRLlyeSPEWaSRTVLLITQQLSLAER-AHHILFLKEGSVCEQGTHLQLMER--- 709
Cdd:PRK13547 173 PRYLLLDEPTAALDLAHQHRlldtVRRL---ARDW-NLGVLAIVHDPNLAARhADRIAMLADGAIVAHGAPADVLTPahi 248
                        250
                 ....*....|....*.
gi 2506117   710 GGCYRSMVEALAAPSD 725
Cdd:PRK13547 249 ARCYGFAVRLVDAGDG 264
ABC_6TM_Pgp_ABCB1 cd18558
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ...
206-453 4.24e-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: 76.93  E-value: 4.24e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  206 WLMCILTIASTVLEFAGDGIYNITMGHMHSRVHGEVFRAVLHQETGFFLKNPTGSITSRVTEDTSNVCESISDKLNLFLW 285
Cdd:cd18558  63 YYYLIIGAIVLITAYIQGSFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIFQ 142
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  286 YLGR-GLCLLAFMIWGsFYLTVVTLLSLPLLFLLPRRLGKVYQSLAVKVQESLAKSTQVALEALSAMPTVRSFANEEGEA 364
Cdd:cd18558 143 NIATfGTGFIIGFIRG-WKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEE 221
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  365 QKFRQKLEEMKPLNKKEAlayVTEVWTMSVSGMLLKVG---ILYLGGQLVVRGAVSSGNLVSFVLYQLQFT-RAVEVLLS 440
Cdd:cd18558 222 TRYAQNLEIAKRNGIKKA---ITFNISMGAAFLLIYASyalAFWYGTYLVTQQEYSIGEVLTVFFSVLIGAfSAGQQVPS 298
                       250
                ....*....|...
gi 2506117  441 IYPSMQKSVGASE 453
Cdd:cd18558 299 IEAFANARGAAYH 311
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
476-682 5.38e-15

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 75.54  E-value: 5.38e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   476 MKGLVKFQDVSFAYPNHpnvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLH 555
Cdd:PRK09544   1 MTSLVSLENVSVSFGQR---RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   556 TQVAAvgqePLLFGRSFRenIAYGLTRT---PTMEEITAvamesgAHdfISGFPQgydtevgetgNQLSGGQRQAVALAR 632
Cdd:PRK09544  78 LDTTL----PLTVNRFLR--LRPGTKKEdilPALKRVQA------GH--LIDAPM----------QKLSGGETQRVLLAR 133
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 2506117   633 ALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSL 682
Cdd:PRK09544 134 ALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHL 183
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
480-702 6.97e-15

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 75.83  E-value: 6.97e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   480 VKFQDVSFAY-PNHPNVQ-VLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLdGEPLV-----QYDHH 552
Cdd:PRK13634   3 ITFQKVEHRYqYKTPFERrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVItagkkNKKLK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   553 YLHTQVAAVGQ--EPLLFGRSFRENIAYGltrtPT---MEEITAVAMESGAHDFIsgfpqGYDTEVGETGN-QLSGGQRQ 626
Cdd:PRK13634  82 PLRKKVGIVFQfpEHQLFEETVEKDICFG----PMnfgVSEEDAKQKAREMIELV-----GLPEELLARSPfELSGGQMR 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2506117   627 AVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGT 702
Cdd:PRK13634 153 RVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGT 229
ABC_6TM_YwjA_like cd18549
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ...
178-447 7.35e-15

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: 75.95  E-value: 7.35e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  178 EMAIPFFTGRITDWILQDKTAPSFARNMWLMCILTIASTVLEFagdgiYNITMGH-----MHSRVHGEVFRAVLHQETGF 252
Cdd:cd18549  18 DLVFPLIVRYIIDDLLPSKNLRLILIIGAILLALYILRTLLNY-----FVTYWGHvmgarIETDMRRDLFEHLQKLSFSF 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  253 FLKNPTGSITSRVTEDTSNVCE------------------------SISDKLNLFLwylgrgLCLLAFMIWGSFYLTvvt 308
Cdd:cd18549  93 FDNNKTGQLMSRITNDLFDISElahhgpedlfisiitiigsfiillTINVPLTLIV------FALLPLMIIFTIYFN--- 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  309 llslpllfllprrlGKVYQSLAvKVQESLAK-STQVAlEALSAMPTVRSFANEEGEAQKFRQKLEEMKpLNKKEAlaYVT 387
Cdd:cd18549 164 --------------KKMKKAFR-RVREKIGEiNAQLE-DSLSGIRVVKAFANEEYEIEKFDEGNDRFL-ESKKKA--YKA 224
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2506117  388 EVWTMSVSGM---LLKVGILYLGGQLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQK 447
Cdd:cd18549 225 MAYFFSGMNFftnLLNLVVLVAGGYFIIKGEITLGDLVAFLLYVNVFIKPIRRLVNFTEQYQK 287
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
495-700 9.37e-15

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 74.05  E-value: 9.37e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   495 VQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHylhtQVAAVGQEPLLF-GRSFr 573
Cdd:PRK10584  23 LSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEE----ARAKLRAKHVGFvFQSF- 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   574 eniayglTRTPTM---EEITAVAMESGAHDFISG------FPQ-GYDTEVGETGNQLSGGQRQAVALARALIRKPRLLIL 643
Cdd:PRK10584  98 -------MLIPTLnalENVELPALLRGESSRQSRngakalLEQlGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFA 170
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 2506117   644 DDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAERAHHILFLKEGSVCEQ 700
Cdd:PRK10584 171 DEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQLQEE 227
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
497-697 9.69e-15

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: 72.85  E-value: 9.69e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  497 VLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVqydhhylhtqvaavgqepllfGRSFRENI 576
Cdd:cd03215  15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVT---------------------RRSPRDAI 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  577 AYGltrtptmeeITAVAMESGAHDFISGFPqgydteVGE---TGNQLSGGQRQAVALARALIRKPRLLILDDATSALDAG 653
Cdd:cd03215  74 RAG---------IAYVPEDRKREGLVLDLS------VAEniaLSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVG 138
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 2506117  654 NQLRVQRLLYESPEwASRTVLLITQQLS-LAERAHHILFLKEGSV 697
Cdd:cd03215 139 AKAEIYRLIRELAD-AGKAVLLISSELDeLLGLCDRILVMYEGRI 182
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
494-701 1.29e-14

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: 72.94  E-value: 1.29e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  494 NVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNL--YQPTGGKVLLDGEPLVQYDHHylhtQVAAVG-----QEPl 566
Cdd:cd03217  12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPE----ERARLGiflafQYP- 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  567 lfgrsfreniaygltrtptmEEITAVAMEsgahDFISgfpqgydtEVGETgnqLSGGQRQAVALARALIRKPRLLILDDA 646
Cdd:cd03217  87 --------------------PEIPGVKNA----DFLR--------YVNEG---FSGGEKKRNEILQLLLLEPDLAILDEP 131
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2506117  647 TSALDAGNqLR-----VQRLLYEspewaSRTVLLITQQLSLAE--RAHHILFLKEGSVCEQG 701
Cdd:cd03217 132 DSGLDIDA-LRlvaevINKLREE-----GKSVLIITHYQRLLDyiKPDRVHVLYDGRIVKSG 187
ABC_6TM_exporter_like cd18550
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
179-455 1.97e-14

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


Pssm-ID: 349994 [Multi-domain]  Cd Length: 294  Bit Score: 74.44  E-value: 1.97e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  179 MAIPFFTGRITDWILQDKTAPSFARNMWLMCILTIASTVLEFAgDGIYNITMGH--MHS-RVhgEVFRAVLHQETGFFLK 255
Cdd:cd18550  16 LLPPLLLREIIDDALPQGDLGLLVLLALGMVAVAVASALLGVV-QTYLSARIGQgvMYDlRV--QLYAHLQRMSLAFFTR 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  256 NPTGSITSRVTEDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQSLAVKVQE 335
Cdd:cd18550  93 TRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVLPTRRVGRRRRKLTREQQE 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  336 SLAKSTQVALEALSA--MPTVRSFANEEGEAQKFRQKLEEMKPLNKKEALAYVTEVWTMSVSGMLLKVGILYLGGQLVVR 413
Cdd:cd18550 173 KLAELNSIMQETLSVsgALLVKLFGREDDEAARFARRSRELRDLGVRQALAGRWFFAALGLFTAIGPALVYWVGGLLVIG 252
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 2506117  414 GAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKI 455
Cdd:cd18550 253 GGLTIGTLVAFTALLGRLYGPLTQLLNIQVDLMTSLALFERI 294
PTZ00243 PTZ00243
ABC transporter; Provisional
508-722 2.45e-14

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 77.13  E-value: 2.45e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    508 GKVTALVGPNGSGKSTvaaLLQNL---YQPTGGKVLLDgeplvqydhhylhTQVAAVGQEPLLFGRSFRENIAYgLTRTP 584
Cdd:PTZ00243  686 GKLTVVLGATGSGKST---LLQSLlsqFEISEGRVWAE-------------RSIAYVPQQAWIMNATVRGNILF-FDEED 748
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    585 TMEEITAVAMESGAHDfISGFPQGYDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYE 664
Cdd:PTZ00243  749 AARLADAVRVSQLEAD-LAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVEECFL 827
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2506117    665 SpEWASRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQLMErggcyRSMVEALAA 722
Cdd:PTZ00243  828 G-ALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMR-----TSLYATLAA 879
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
500-664 2.54e-14

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 74.74  E-value: 2.54e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   500 GLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHT---QVAAVGQEPL--LFGR-SFR 573
Cdd:PRK15079  39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAvrsDIQMIFQDPLasLNPRmTIG 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   574 ENIAYGL-------TRTPTMEEITAVAMESG-AHDFISGFPqgydtevgetgNQLSGGQRQAVALARALIRKPRLLILDD 645
Cdd:PRK15079 119 EIIAEPLrtyhpklSRQEVKDRVKAMMLKVGlLPNLINRYP-----------HEFSGGQCQRIGIARALILEPKLIICDE 187
                        170
                 ....*....|....*....
gi 2506117   646 ATSALDAGNQLRVQRLLYE 664
Cdd:PRK15079 188 PVSALDVSIQAQVVNLLQQ 206
cbiO PRK13649
energy-coupling factor transporter ATPase;
480-702 3.65e-14

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 73.63  E-value: 3.65e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   480 VKFQDVSFAYPNHPNVQ--VLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPL----VQYDHHY 553
Cdd:PRK13649   3 INLQNVSYTYQAGTPFEgrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstsKNKDIKQ 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   554 LHTQVAAVGQ--EPLLFGRSFRENIAYGltrtP-----TMEEITAVAMESGAHDFISgfpqgyDTEVGETGNQLSGGQRQ 626
Cdd:PRK13649  83 IRKKVGLVFQfpESQLFEETVLKDVAFG----PqnfgvSQEEAEALAREKLALVGIS------ESLFEKNPFELSGGQMR 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2506117   627 AVALARALIRKPRLLILDDATSALDAGNQLRVQRlLYESPEWASRTVLLITQQL-SLAERAHHILFLKEGSVCEQGT 702
Cdd:PRK13649 153 RVAIAGILAMEPKILVLDEPTAGLDPKGRKELMT-LFKKLHQSGMTIVLVTHLMdDVANYADFVYVLEKGKLVLSGK 228
cbiO PRK13637
energy-coupling factor transporter ATPase;
480-702 4.96e-14

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 73.16  E-value: 4.96e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   480 VKFQDVSFAY-PNHP-NVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLV--QYDHHYLH 555
Cdd:PRK13637   3 IKIENLTHIYmEGTPfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDIR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   556 TQVAAVGQEP--LLFGRSFRENIAYGLTRTP-TMEEI---TAVAMEsgahdfISGFPqgYDTEVGETGNQLSGGQRQAVA 629
Cdd:PRK13637  83 KKVGLVFQYPeyQLFEETIEKDIAFGPINLGlSEEEIenrVKRAMN------IVGLD--YEDYKDKSPFELSGGQKRRVA 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2506117   630 LARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLS-LAERAHHILFLKEGSVCEQGT 702
Cdd:PRK13637 155 IAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEdVAKLADRIIVMNKGKCELQGT 228
ABC_6TM_YknV_like cd18545
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ...
179-455 7.04e-14

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


Pssm-ID: 349989 [Multi-domain]  Cd Length: 293  Bit Score: 72.89  E-value: 7.04e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  179 MAIPFFTGRITDWILQDKTAPSfarnMWLMCILTIASTVLEFAGDGIYNITMGHMHSRV-HG---EVFRAVLHQETGFFL 254
Cdd:cd18545  17 LAGPYLIKIAIDEYIPNGDLSG----LLIIALLFLALNLVNWVASRLRIYLMAKVGQRIlYDlrqDLFSHLQKLSFSFFD 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  255 KNPTGSITSRVTEDTSNVCE--------SISDKLNLFlwylgrglCLLAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVY 326
Cdd:cd18545  93 SRPVGKILSRVINDVNSLSDllsnglinLIPDLLTLV--------GIVIIMFSLNVRLALVTLAVLPLLVLVVFLLRRRA 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  327 QSLAVKVQESLAK-STQVAlEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKeALAYVTEVW-TMSVSGMLLKVGIL 404
Cdd:cd18545 165 RKAWQRVRKKISNlNAYLH-ESISGIRVIQSFAREDENEEIFDELNRENRKANMR-AVRLNALFWpLVELISALGTALVY 242
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 2506117  405 YLGGQLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKI 455
Cdd:cd18545 243 WYGGKLVLGGAITVGVLVAFIGYVGRFWQPIRNLSNFYNQLQSAMASAERI 293
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
499-692 1.40e-13

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 70.22  E-value: 1.40e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   499 QGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYlHTQVAAVGQ----EPLLfgrSFRE 574
Cdd:PRK13538  18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEY-HQDLLYLGHqpgiKTEL---TALE 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   575 NIAYGLT-RTPTMEEITAVAMEsgahdfisgfpqgydtEVGETG------NQLSGGQRQAVALARALIRKPRLLILDDAT 647
Cdd:PRK13538  94 NLRFYQRlHGPGDDEALWEALA----------------QVGLAGfedvpvRQLSAGQQRRVALARLWLTRAPLWILDEPF 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 2506117   648 SALDAGNQLRVQRLLYESpewASR--TVLLIT-QQLSLAERAHHILFL 692
Cdd:PRK13538 158 TAIDKQGVARLEALLAQH---AEQggMVILTThQDLPVASDKVRKLRL 202
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
476-650 1.74e-13

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 73.50  E-value: 1.74e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   476 MKGLVKFQDVSFAYPNhpnVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHylH 555
Cdd:PRK10762   1 MQALLQLKGIDKAFPG---VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPK--S 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   556 TQVAAVG---QEPLLFGR-SFRENIAYGLTRTPTMEEITAVAMESGAHDFIS--GFPQGYDTEVGEtgnqLSGGQRQAVA 629
Cdd:PRK10762  76 SQEAGIGiihQELNLIPQlTIAENIFLGREFVNRFGRIDWKKMYAEADKLLArlNLRFSSDKLVGE----LSIGEQQMVE 151
                        170       180
                 ....*....|....*....|.
gi 2506117   630 LARALIRKPRLLILDDATSAL 650
Cdd:PRK10762 152 IAKVLSFESKVIIMDEPTDAL 172
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
476-687 2.07e-13

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


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 70.29  E-value: 2.07e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   476 MKGLVKFQDVSFAYPNhpnVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYD-HHYL 554
Cdd:PRK11614   2 EKVMLSFDKVSAHYGK---IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQtAKIM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   555 HTQVAAVGQEPLLFGR-SFRENIAYG---LTRTPTMEEITAVamesgaHDFisgFPQGYDTEVGETGNqLSGGQRQAVAL 630
Cdd:PRK11614  79 REAVAIVPEGRRVFSRmTVEENLAMGgffAERDQFQERIKWV------YEL---FPRLHERRIQRAGT-MSGGEQQMLAI 148
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   631 ARALIRKPRLLILDDATSAL---------DAGNQLRVQRLlyespewasrTVLLI----TQQLSLAERAH 687
Cdd:PRK11614 149 GRALMSQPRLLLLDEPSLGLapiiiqqifDTIEQLREQGM----------TIFLVeqnaNQALKLADRGY 208
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
475-650 2.20e-13

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 73.28  E-value: 2.20e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   475 NMKGLVKFQDVSFAYPNhpnVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGeplVQYDH--H 552
Cdd:PRK09700   1 MATPYISMAGIGKSFGP---VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINN---INYNKldH 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   553 YLHTQ--VAAVGQEPLLFGR-SFRENIAYGltRTPT-------------MEEITAVAMesgahdFISGFPQGYDTEVGEt 616
Cdd:PRK09700  75 KLAAQlgIGIIYQELSVIDElTVLENLYIG--RHLTkkvcgvniidwreMRVRAAMML------LRVGLKVDLDEKVAN- 145
                        170       180       190
                 ....*....|....*....|....*....|....
gi 2506117   617 gnqLSGGQRQAVALARALIRKPRLLILDDATSAL 650
Cdd:PRK09700 146 ---LSISHKQMLEIAKTLMLDAKVIIMDEPTSSL 176
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
480-702 2.43e-13

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 71.68  E-value: 2.43e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   480 VKFQDVSFAYPNHpNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQP---TGGKVLLDGEPLVQYDHHYLHT 556
Cdd:PRK09473  15 VKDLRVTFSTPDG-DVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREILNLPEKELNK 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   557 ----QVAAVGQEPLL-------FGRSFRENIAY--GLTRTPTMEE----ITAVAMESgAHDFISGFPqgydtevgetgNQ 619
Cdd:PRK09473  94 lraeQISMIFQDPMTslnpymrVGEQLMEVLMLhkGMSKAEAFEEsvrmLDAVKMPE-ARKRMKMYP-----------HE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   620 LSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLS-LAERAHHILFLKEGSVC 698
Cdd:PRK09473 162 FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGvVAGICDKVLVMYAGRTM 241

                 ....
gi 2506117   699 EQGT 702
Cdd:PRK09473 242 EYGN 245
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
474-652 3.14e-13

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


Pssm-ID: 131681 [Multi-domain]  Cd Length: 500  Bit Score: 72.55  E-value: 3.14e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    474 LNMKGLVKfqdvSFAypnhpNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYqPTG---GKVLLDGEPLVQyd 550
Cdd:TIGR02633   2 LEMKGIVK----TFG-----GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHGtwdGEIYWSGSPLKA-- 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    551 HHYLHTQ---VAAVGQEPLLFGR-SFRENIAYGLTRTPTMEEITAVAMESGAHDFISGFpQGYDTEVGETGNQLSGGQRQ 626
Cdd:TIGR02633  70 SNIRDTEragIVIIHQELTLVPElSVAENIFLGNEITLPGGRMAYNAMYLRAKNLLREL-QLDADNVTRPVGDYGGGQQQ 148
                         170       180
                  ....*....|....*....|....*.
gi 2506117    627 AVALARALIRKPRLLILDDATSALDA 652
Cdd:TIGR02633 149 LVEIAKALNKQARLLILDEPSSSLTE 174
cbiO PRK13641
energy-coupling factor transporter ATPase;
480-695 3.30e-13

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 70.63  E-value: 3.30e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   480 VKFQDVSFAY-PNHP-NVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHY---- 553
Cdd:PRK13641   3 IKFENVDYIYsPGTPmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKnlkk 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   554 LHTQVAAVGQ--EPLLFGRSFRENIAYGltrtPTMEEITAVAMESGAHDFISGFpqGYDTEVGETGN-QLSGGQRQAVAL 630
Cdd:PRK13641  83 LRKKVSLVFQfpEAQLFENTVLKDVEFG----PKNFGFSEDEAKEKALKWLKKV--GLSEDLISKSPfELSGGQMRRVAI 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2506117   631 ARALIRKPRLLILDDATSALDAGNQLRVQRLLYESpEWASRTVLLITQQL-SLAERAHHILFLKEG 695
Cdd:PRK13641 157 AGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDY-QKAGHTVILVTHNMdDVAEYADDVLVLEHG 221
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
506-706 3.61e-13

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 70.51  E-value: 3.61e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   506 YPGK-VTALVGPNGSGKSTVAALLQNLYQPTGG-----KVLLDGEPLVQY-DHHYLHTQVAAVGQEPLLFGRSFRENIAY 578
Cdd:PRK14271  44 FPARaVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYrDVLEFRRRVGMLFQRPNPFPMSIMDNVLA 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   579 GLT----------RTPTMEEITAVAMESGAHDFISGFPqgydtevgetgNQLSGGQRQAVALARALIRKPRLLILDDATS 648
Cdd:PRK14271 124 GVRahklvprkefRGVAQARLTEVGLWDAVKDRLSDSP-----------FRLSGGQQQLLCLARTLAVNPEVLLLDEPTS 192
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   649 ALDAGNQLRVQRLLYespEWASR-TVLLITQQLSLAER-AHHILFLKEGSVCEQGTHLQL 706
Cdd:PRK14271 193 ALDPTTTEKIEEFIR---SLADRlTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQL 249
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
493-702 4.44e-13

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


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 72.39  E-value: 4.44e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    493 PNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNlYQPTG----GKVLLDGEPL-----------VQYDHHYLHTQ 557
Cdd:TIGR00955  36 PRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAF-RSPKGvkgsGSVLLNGMPIdakemraisayVQQDDLFIPTL 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    558 VAavgQEPLLFGRSFR--ENIAYGLTRTPTMEEITAVAMESGAHdfisgfpqgydTEVGETGNQ--LSGGQRQAVALARA 633
Cdd:TIGR00955 115 TV---REHLMFQAHLRmpRRVTKKEKRERVDEVLQALGLRKCAN-----------TRIGVPGRVkgLSGGERKRLAFASE 180
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    634 LIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLS-LAERAHHILFLKEGSVCEQGT 702
Cdd:TIGR00955 181 LLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSeLFELFDKIILMAEGRVAYLGS 250
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
496-644 5.06e-13

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


Pssm-ID: 440752 [Multi-domain]  Cd Length: 240  Bit Score: 69.29  E-value: 5.06e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  496 QVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHylhtQVAAVG-----QEPLLFGR 570
Cdd:COG1137  17 TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMH----KRARLGigylpQEASIFRK 92
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2506117  571 -SFRENIAYGL-TRTPTMEEITAvAMESGAHDF-IsgfpqgydTEVGET-GNQLSGGQRQAVALARALIRKPRLLILD 644
Cdd:COG1137  93 lTVEDNILAVLeLRKLSKKEREE-RLEELLEEFgI--------THLRKSkAYSLSGGERRRVEIARALATNPKFILLD 161
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
507-678 1.51e-12

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: 65.86  E-value: 1.51e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117     507 PGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVL-LDGEPLVQYDHHYLHtqvaavgqepllfgrsfreniaygltrtpt 585
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIyIDGEDILEEVLDQLL------------------------------ 50
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117     586 meeitavamesgahdfisgfpqgyDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQ-----R 660
Cdd:smart00382  51 ------------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleelR 106
                          170
                   ....*....|....*...
gi 2506117     661 LLYESPEWASRTVLLITQ 678
Cdd:smart00382 107 LLLLLKSEKNLTVILTTN 124
PRK10522 PRK10522
multidrug transporter membrane component/ATP-binding component; Provisional
482-699 2.65e-12

multidrug transporter membrane component/ATP-binding component; Provisional


Pssm-ID: 236707 [Multi-domain]  Cd Length: 547  Bit Score: 70.00  E-value: 2.65e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   482 FQDVSFAYPNhPNVQVlQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQVAAV 561
Cdd:PRK10522 325 LRNVTFAYQD-NGFSV-GPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAV 402
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   562 GQEPLLFGRsfreniayglTRTPTMEEITAVAMESGAHdfISGFPQGYDTEVGETGN-QLSGGQRQAVALARALIRKPRL 640
Cdd:PRK10522 403 FTDFHLFDQ----------LLGPEGKPANPALVEKWLE--RLKMAHKLELEDGRISNlKLSKGQKKRLALLLALAEERDI 470
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2506117   641 LILDDAtsALDAGNQLR---VQRLLYESPEwASRTVLLITQQLSLAERAHHILFLKEGSVCE 699
Cdd:PRK10522 471 LLLDEW--AADQDPHFRrefYQVLLPLLQE-MGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
496-708 2.68e-12

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 67.56  E-value: 2.68e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   496 QVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQ-----PTGGKVLLDGEPLVQYDHHYLHT--QVAAVGQEPLLF 568
Cdd:PRK14267  18 HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSPDVDPIEVrrEVGMVFQYPNPF 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   569 GR-SFRENIAYGL------TRTPTMEEITAVAMESGA-----HDFISGFPqgydtevgetgNQLSGGQRQAVALARALIR 636
Cdd:PRK14267  98 PHlTIYDNVAIGVklnglvKSKKELDERVEWALKKAAlwdevKDRLNDYP-----------SNLSGGQRQRLVIARALAM 166
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2506117   637 KPRLLILDDATSALDAGNQLRVQRLLYESPEwaSRTVLLITQQLSLAER-AHHILFLKEGSVCEQGTHLQLME 708
Cdd:PRK14267 167 KPKILLMDEPTANIDPVGTAKIEELLFELKK--EYTIVLVTHSPAQAARvSDYVAFLYLGKLIEVGPTRKVFE 237
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
500-701 2.75e-12

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 67.42  E-value: 2.75e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   500 GLTFTLYPGKVTALVGPNGSGKS-TVAALLQNL---YQPTGGKVLLDGEPLVQYDHHYLHtqVAAVGQEPllfgRS-F-- 572
Cdd:PRK10418  21 GVSLTLQRGRVLALVGGSGSGKSlTCAAALGILpagVRQTAGRVLLDGKPVAPCALRGRK--IATIMQNP----RSaFnp 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   573 --------RENI-AYGLTRTPT--MEEITAVAMESgAHDFISGFPqgydtevgetgNQLSGGQRQAVALARALIRKPRLL 641
Cdd:PRK10418  95 lhtmhthaRETClALGKPADDAtlTAALEAVGLEN-AARVLKLYP-----------FEMSGGMLQRMMIALALLCEAPFI 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2506117   642 ILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQG 701
Cdd:PRK10418 163 IADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARlADDVAVMSHGRIVEQG 223
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
495-680 3.36e-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: 69.45  E-value: 3.36e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    495 VQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKV-LLDGEPLVQ-----YDHHYLHTQ-VAAVGQEPLL 567
Cdd:TIGR03269 297 VKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnVRVGDEWVDmtkpgPDGRGRAKRyIGILHQEYDL 376
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    568 FG-RSFRENiaygLTRTPTMEEITAVAMESGAHDFIS-GFPQGYDTEVGET-GNQLSGGQRQAVALARALIRKPRLLILD 644
Cdd:TIGR03269 377 YPhRTVLDN----LTEAIGLELPDELARMKAVITLKMvGFDEEKAEEILDKyPDELSEGERHRVALAQVLIKEPRIVILD 452
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2506117    645 DATSALDAGNQLRVQRLLYESPEWASRTVLLITQQL 680
Cdd:TIGR03269 453 EPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDM 488
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
498-701 3.41e-12

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 67.26  E-value: 3.41e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   498 LQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLL---DGEPLVQYD------HHYLHTQVAAVGQEP--- 565
Cdd:PRK11701  22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrDGQLRDLYAlseaerRRLLRTEWGFVHQHPrdg 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   566 LLFGRSFRENIA----------YGLTRTPTMEEITAVAMESgahDFISGFPQGYdtevgetgnqlSGGQRQAVALARALI 635
Cdd:PRK11701 102 LRMQVSAGGNIGerlmavgarhYGDIRATAGDWLERVEIDA---ARIDDLPTTF-----------SGGMQQRLQIARNLV 167
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2506117   636 RKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAeR--AHHILFLKEGSVCEQG 701
Cdd:PRK11701 168 THPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVA-RllAHRLLVMKQGRVVESG 234
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
484-682 4.08e-12

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127 [Multi-domain]  Cd Length: 200  Bit Score: 65.74  E-value: 4.08e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   484 DVSFAYPNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPlVQYDHHYLHTQVAAVGQ 563
Cdd:PRK13540   6 ELDFDYHDQP---LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQS-IKKDLCTYQKQLCFVGH 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   564 E----PLLfgrSFRENIAYGLTRTPTMEEITAVAMESGAHDFISgFPQGYdtevgetgnqLSGGQRQAVALARALIRKPR 639
Cdd:PRK13540  82 RsginPYL---TLRENCLYDIHFSPGAVGITELCRLFSLEHLID-YPCGL----------LSSGQKRQVALLRLWMSKAK 147
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 2506117   640 LLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSL 682
Cdd:PRK13540 148 LWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQDLPL 190
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
619-702 4.23e-12

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 67.84  E-value: 4.23e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   619 QLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSL-AERAHHILFLKEGSV 697
Cdd:PRK11022 153 QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALvAEAAHKIIVMYAGQV 232

                 ....*
gi 2506117   698 CEQGT 702
Cdd:PRK11022 233 VETGK 237
PvdE COG4615
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...
403-546 5.40e-12

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: 69.06  E-value: 5.40e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  403 ILYLGGQLvvrGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKIfEYLDRTPCSPLSGSLAPLNMKGLVKF 482
Cdd:COG4615 250 ILFLLPAL---GWADPAVLSGFVLVLLFLRGPLSQLVGALPTLSRANVALRKI-EELELALAAAEPAAADAAAPPAPADF 325
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2506117  483 Q-----DVSFAYPN--HPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPL 546
Cdd:COG4615 326 QtlelrGVTYRYPGedGDEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPV 396
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
493-702 8.28e-12

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 68.34  E-value: 8.28e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   493 PNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHY--LHTQ------------V 558
Cdd:PRK10261  27 QKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRQVieLSEQsaaqmrhvrgadM 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   559 AAVGQEPLL-------FGRSFRENIAY--GLTRTPTMEEITAVAME---SGAHDFISGFPqgydtevgetgNQLSGGQRQ 626
Cdd:PRK10261 107 AMIFQEPMTslnpvftVGEQIAESIRLhqGASREEAMVEAKRMLDQvriPEAQTILSRYP-----------HQLSGGMRQ 175
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2506117   627 AVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLS-LAERAHHILFLKEGSVCEQGT 702
Cdd:PRK10261 176 RVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGvVAEIADRVLVMYQGEAVETGS 252
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
483-677 9.02e-12

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


Pssm-ID: 274744 [Multi-domain]  Cd Length: 552  Bit Score: 68.04  E-value: 9.02e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    483 QDVSFAYPnhPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYdhhylhtqvaaVG 562
Cdd:TIGR03719   8 NRVSKVVP--PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKVGY-----------LP 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    563 QEPLL-FGRSFRENIAYGLTRTP-TMEEITAVAME------------------------SGAHDFISGF---------PQ 607
Cdd:TIGR03719  75 QEPQLdPTKTVRENVEEGVAEIKdALDRFNEISAKyaepdadfdklaaeqaelqeiidaADAWDLDSQLeiamdalrcPP 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2506117    608 GyDTEVgetgNQLSGGQRQAVALARALIRKPRLLILDDATSALDAgnqlrvqrllyESPEWASR-------TVLLIT 677
Cdd:TIGR03719 155 W-DADV----TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDA-----------ESVAWLERhlqeypgTVVAVT 215
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
454-723 1.03e-11

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


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 66.65  E-value: 1.03e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  454 KIFEYLDRTPcsPLSGSLaplnmKGLVKfqdvsfayPNHPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQ 533
Cdd:COG4586   9 KTYRVYEKEP--GLKGAL-----KGLFR--------REYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILV 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  534 PTGGKVLLDGepLVQYDH--HYLHtQVAAV-GQE-------PLLfgRSFRENIA-YGLTRT---PTMEEITAVaMEsgah 599
Cdd:COG4586  74 PTSGEVRVLG--YVPFKRrkEFAR-RIGVVfGQRsqlwwdlPAI--DSFRLLKAiYRIPDAeykKRLDELVEL-LD---- 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  600 dfISGFpqgYDTEVgetgNQLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQ 679
Cdd:COG4586 144 --LGEL---LDTPV----RQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHD 214
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 2506117  680 LS----LAERahhILFLKEGSVCEQGTHLQLMERGGCYRSMVEALAAP 723
Cdd:COG4586 215 MDdieaLCDR---VIVIDHGRIIYDGSLEELKERFGPYKTIVLELAEP 259
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
497-697 1.44e-11

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 67.35  E-value: 1.44e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  497 VLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVqydhhyLHTQVAAVGQ-----------EP 565
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVR------IRSPRDAIRAgiayvpedrkgEG 340
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  566 LLFGRSFRENIA---------YGLTRTPTMEEITAvamesgahDFISGF---PQGYDTEVGetgnQLSGGQRQAVALARA 633
Cdd:COG1129 341 LVLDLSIRENITlasldrlsrGGLLDRRRERALAE--------EYIKRLrikTPSPEQPVG----NLSGGNQQKVVLAKW 408
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2506117  634 LIRKPRLLILDDATSALDAGNQLRVQRLLYESpewASR--TVLLITQQLS-LAERAHHILFLKEGSV 697
Cdd:COG1129 409 LATDPKVLILDEPTRGIDVGAKAEIYRLIREL---AAEgkAVIVISSELPeLLGLSDRILVMREGRI 472
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
476-716 1.74e-11

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 65.03  E-value: 1.74e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   476 MKGLVKFQDVSFAYPNHpnvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLY---QPTGGKVLLDG-----EPLV 547
Cdd:PRK09984   1 MQTIIRVEKLAKTFNQH---QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGrtvqrEGRL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   548 QYDHHYLHTQVAAVGQEPLLFGR-SFRENIAYG-LTRTP----------------TMEEITAVAMESGAHDFISgfpqgy 609
Cdd:PRK09984  78 ARDIRKSRANTGYIFQQFNLVNRlSVLENVLIGaLGSTPfwrtcfswftreqkqrALQALTRVGMVHFAHQRVS------ 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   610 dtevgetgnQLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHH 688
Cdd:PRK09984 152 ---------TLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRyCER 222
                        250       260       270
                 ....*....|....*....|....*....|
gi 2506117   689 ILFLKEGSVCEQGTHLQL-MER-GGCYRSM 716
Cdd:PRK09984 223 IVALRQGHVFYDGSSQQFdNERfDHLYRSI 252
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
483-677 2.07e-11

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 67.07  E-value: 2.07e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   483 QDVSFAYPnhPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGK-VLLDGeplvqydhhylhtqvAAV 561
Cdd:PRK11819  10 NRVSKVVP--PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEaRPAPG---------------IKV 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   562 G---QEPLL-FGRSFRENIAYG-------LTR---------TPtMEEITAVAMESG----------AHDFIS-------- 603
Cdd:PRK11819  73 GylpQEPQLdPEKTVRENVEEGvaevkaaLDRfneiyaayaEP-DADFDALAAEQGelqeiidaadAWDLDSqleiamda 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   604 -GFPQGyDTEVGetgnQLSGGQRQAVALARALIRKPRLLILDDATSALDAgnqlrvqrllyESPEWASR-------TVLL 675
Cdd:PRK11819 152 lRCPPW-DAKVT----KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA-----------ESVAWLEQflhdypgTVVA 215

                 ..
gi 2506117   676 IT 677
Cdd:PRK11819 216 VT 217
ABC_6TM_PCAT1_LagD_like cd18570
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ...
179-455 2.48e-11

Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.


Pssm-ID: 350014 [Multi-domain]  Cd Length: 294  Bit Score: 65.16  E-value: 2.48e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  179 MAIPFFTGRITDWILQDKTAPSFARNMWLMCILTIASTVLEFagdgIYNITMGHMHSRVHGEV----FRAVLHQETGFFL 254
Cdd:cd18570  19 IAGSFFFQILIDDIIPSGDINLLNIISIGLILLYLFQSLLSY----IRSYLLLKLSQKLDIRLilgyFKHLLKLPLSFFE 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  255 KNPTGSITSRVTeDTSNVCESISDK-----LNLFLwylgrGLCLLAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQSL 329
Cdd:cd18570  95 TRKTGEIISRFN-DANKIREAISSTtislfLDLLM-----VIISGIILFFYNWKLFLITLLIIPLYILIILLFNKPFKKK 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  330 AVKVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKEA-LAYVTEVWTMSVSGmLLKVGILYLGG 408
Cdd:cd18570 169 NREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGkLSNLQSSIKGLISL-IGSLLILWIGS 247
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 2506117  409 QLVVRGAVSSGNLVSFvlYQLQ--FTRAVEVLLSIYPSMQKSVGASEKI 455
Cdd:cd18570 248 YLVIKGQLSLGQLIAF--NALLgyFLGPIENLINLQPKIQEAKVAADRL 294
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
494-707 2.87e-11

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 64.18  E-value: 2.87e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   494 NVQV---LQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYqPTGGKVLLDGEPLVQYDHH-------YLHTQVAAVGQ 563
Cdd:PRK03695   5 DVAVstrLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAelarhraYLSQQQTPPFA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   564 EPLlfgrsFRENIAYGLTRTPTMEEITAVamesgaHDFISGFpqGYDTEVGETGNQLSGGQRQAVALARALIR-----KP 638
Cdd:PRK03695  84 MPV-----FQYLTLHQPDKTRTEAVASAL------NEVAEAL--GLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdiNP 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2506117   639 --RLLILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQLS-LAERAHHILFLKEGSVCEQGTHLQLM 707
Cdd:PRK03695 151 agQLLLLDEPMNSLDVAQQAALDRLLSELCQ-QGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVL 221
SapD COG4170
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
618-709 3.35e-11

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


Pssm-ID: 443330 [Multi-domain]  Cd Length: 331  Bit Score: 65.31  E-value: 3.35e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  618 NQLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQL-SLAERAHHILFLKEGS 696
Cdd:COG4170 157 HELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLeSISQWADTITVLYCGQ 236
                        90
                ....*....|...
gi 2506117  697 VCEQGTHLQLMER 709
Cdd:COG4170 237 TVESGPTEQILKS 249
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
495-708 4.38e-11

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 66.03  E-value: 4.38e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   495 VQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGE---PLVQYDHHYLHTQVAAVGQEP------ 565
Cdd:PRK10261 337 VHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridTLSPGKLQALRRDIQFIFQDPyasldp 416
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   566 ----------------LLFGRSFRENIAYGLTRTPTMEEitavamesgaHDFisGFPqgydtevgetgNQLSGGQRQAVA 629
Cdd:PRK10261 417 rqtvgdsimeplrvhgLLPGKAAAARVAWLLERVGLLPE----------HAW--RYP-----------HEFSGGQRQRIC 473
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   630 LARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGTHLQLME 708
Cdd:PRK10261 474 IARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERiSHRVAVMYLGQIVEIGPRRAVFE 553
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
475-645 6.41e-11

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 63.63  E-value: 6.41e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   475 NMKGLVKFQDVSFAYPNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYL 554
Cdd:PRK11831   3 SVANLVDMRGVSFTRGNRC---IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   555 HT---QVAAVGQEPLLF-GRSFRENIAYGL---TRTP-------TMEEITAVAMESGAHDFISgfpqgydtevgetgnQL 620
Cdd:PRK11831  80 YTvrkRMSMLFQSGALFtDMNVFDNVAYPLrehTQLPapllhstVMMKLEAVGLRGAAKLMPS---------------EL 144
                        170       180
                 ....*....|....*....|....*
gi 2506117   621 SGGQRQAVALARALIRKPRLLILDD 645
Cdd:PRK11831 145 SGGMARRAALARAIALEPDLIMFDE 169
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
501-706 1.14e-10

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: 65.42  E-value: 1.14e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117     501 LTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPlVQYDHHYLHTQVAAVGQEPLLFGR-SFRENIAYG 579
Cdd:TIGR01257  949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKD-IETNLDAVRQSLGMCPQHNILFHHlTVAEHILFY 1027
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117     580 LTRTPTMEEITAVAMESGAHDfisgfpQGYDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQ 659
Cdd:TIGR01257 1028 AQLKGRSWEEAQLEMEAMLED------TGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIW 1101
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 2506117     660 RLL--YESpewaSRTVLLITQQLSLAE-RAHHILFLKEGSVCEQGTHLQL 706
Cdd:TIGR01257 1102 DLLlkYRS----GRTIIMSTHHMDEADlLGDRIAIISQGRLYCSGTPLFL 1147
PLN03211 PLN03211
ABC transporter G-25; Provisional
497-695 1.47e-10

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 64.52  E-value: 1.47e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   497 VLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTG--GKVLLDGEPLV-----------QYDHHYLHTQVaavgQ 563
Cdd:PLN03211  83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTkqilkrtgfvtQDDILYPHLTV----R 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   564 EPLLFGRSFReniaygLTRTPTMEEITAVAmESGAHDFisGFPQGYDTEVGETGNQ-LSGGQRQAVALARALIRKPRLLI 642
Cdd:PLN03211 159 ETLVFCSLLR------LPKSLTKQEKILVA-ESVISEL--GLTKCENTIIGNSFIRgISGGERKRVSIAHEMLINPSLLI 229
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 2506117   643 LDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLS-LAERAHHILFLKEG 695
Cdd:PLN03211 230 LDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSrVYQMFDSVLVLSEG 283
ABC_6TM_exporter_like cd18778
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
180-455 1.84e-10

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


Pssm-ID: 350051 [Multi-domain]  Cd Length: 293  Bit Score: 62.55  E-value: 1.84e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  180 AIPFFTGRITDWILQDKTAPSFARNMWLMCILTIASTVLEFAGDGIYNITMG-HMHSRVHGEVFRAVLHQETGFFLKNPT 258
Cdd:cd18778  17 VPPWLIRELVDLVTIGSKSLGLLLGLALLLLGAYLLRALLNFLRIYLNHVAEqKVVADLRSDLYDKLQRLSLRYFDDRQT 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  259 GSITSRVTEDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQSLAVKVQESLA 338
Cdd:cd18778  97 GDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLALGAWLYSKKVRPRYRKVREALG 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  339 KSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKplnkkEALAYVTEVW-----TMSVSGMLLKVGILYLGGQLVVR 413
Cdd:cd18778 177 ELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYR-----KAQLRAMKLWaifhpLMEFLTSLGTVLVLGFGGRLVLA 251
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 2506117  414 GAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKI 455
Cdd:cd18778 252 GELTIGDLVAFLLYLGLFYEPITSLHGLNEMLQRALAGAERV 293
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
504-676 2.98e-10

The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.


Pssm-ID: 213204 [Multi-domain]  Cd Length: 246  Bit Score: 61.27  E-value: 2.98e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  504 TLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPlVQYDHHY------------LHTQVAAVGQEPllfgrS 571
Cdd:cd03237  21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDT-VSYKPQYikadyegtvrdlLSSITKDFYTHP-----Y 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  572 FRENIAYGLtrtpTMEEItavamesgahdfisgfpqgYDTEVgetgNQLSGGQRQAVALARALIRKPRLLILDDATSALD 651
Cdd:cd03237  95 FKTEIAKPL----QIEQI-------------------LDREV----PELSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147
                       170       180
                ....*....|....*....|....*
gi 2506117  652 AGNQLRVQRLLYESPEWASRTVLLI 676
Cdd:cd03237 148 VEQRLMASKVIRRFAENNEKTAFVV 172
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
486-652 4.82e-10

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: 59.58  E-value: 4.82e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  486 SFAYPNHPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTG---GKVLLDGEPLVQYDHHYlHTQVAAVG 562
Cdd:cd03233  11 FTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNGIPYKEFAEKY-PGEIIYVS 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  563 QE----PLLfgrsfreniaygltrtpTMEEITAVAMESGAHDFISGFpqgydtevgetgnqlSGGQRQAVALARALIRKP 638
Cdd:cd03233  90 EEdvhfPTL-----------------TVRETLDFALRCKGNEFVRGI---------------SGGERKRVSIAEALVSRA 137
                       170
                ....*....|....
gi 2506117  639 RLLILDDATSALDA 652
Cdd:cd03233 138 SVLCWDNSTRGLDS 151
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
496-702 5.55e-10

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 60.29  E-value: 5.55e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   496 QVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGE-----PLvqydHHYLHTQVAAVGQEPLLFGR 570
Cdd:PRK10895  17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdisllPL----HARARRGIGYLPQEASIFRR 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   571 -SFRENIAYGLTrtpTMEEITAVAMESGAHDFISGFPQGYDTEvgETGNQLSGGQRQAVALARALIRKPRLLILDDATSA 649
Cdd:PRK10895  93 lSVYDNLMAVLQ---IRDDLSAEQREDRANELMEEFHIEHLRD--SMGQSLSGGERRRVEIARALAANPKFILLDEPFAG 167
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 2506117   650 LDAGNQLRVQRLLYESPEwaSRTVLLIT-----QQLSLAERAHhilFLKEGSVCEQGT 702
Cdd:PRK10895 168 VDPISVIDIKRIIEHLRD--SGLGVLITdhnvrETLAVCERAY---IVSQGHLIAHGT 220
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
480-701 5.87e-10

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 61.26  E-value: 5.87e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   480 VKFQDVSFAY----PNHpnVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKV---LLDGEPLVQYDHH 552
Cdd:PRK13651   3 IKVKNIVKIFnkklPTE--LKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewiFKDEKNKKKTKEK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   553 Y---------------------LHTQVAAVGQ--EPLLFGRSFRENIAYGltrtPTMEEITAVAMESGAHDFIS--GFPQ 607
Cdd:PRK13651  81 EkvleklviqktrfkkikkikeIRRRVGVVFQfaEYQLFEQTIEKDIIFG----PVSMGVSKEEAKKRAAKYIElvGLDE 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   608 GYdteVGETGNQLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQL-SLAERA 686
Cdd:PRK13651 157 SY---LQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNK-QGKTIILVTHDLdNVLEWT 232
                        250
                 ....*....|....*
gi 2506117   687 HHILFLKEGSVCEQG 701
Cdd:PRK13651 233 KRTIFFKDGKIIKDG 247
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
495-702 6.00e-10

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 61.40  E-value: 6.00e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   495 VQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLL---------DGEPLVQY-------DHHYLHTQV 558
Cdd:PRK13631  39 LVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkkNNHELITNpyskkikNFKELRRRV 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   559 AAVGQEP--LLFGRSFRENIAYGltrtPTMEEITAVAMESGAHDFISGFPQGYD-TEVGETGnqLSGGQRQAVALARALI 635
Cdd:PRK13631 119 SMVFQFPeyQLFKDTIEKDIMFG----PVALGVKKSEAKKLAKFYLNKMGLDDSyLERSPFG--LSGGQKRRVAIAGILA 192
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2506117   636 RKPRLLILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQL-SLAERAHHILFLKEGSVCEQGT 702
Cdd:PRK13631 193 IQPEILIFDEPTAGLDPKGEHEMMQLILDAKA-NNKTVFVITHTMeHVLEVADEVIVMDKGKILKTGT 259
GguA NF040905
sugar ABC transporter ATP-binding protein;
474-650 6.05e-10

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 62.11  E-value: 6.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   474 LNMKGLVKfqdvSFaypnhPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYqPTG---GKVLLDGEP----- 545
Cdd:NF040905   2 LEMRGITK----TF-----PGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHGsyeGEILFDGEVcrfkd 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   546 LVQYDHH---YLHTQVAAVgqePLLfgrSFRENI-------AYGL-----TRTPTMEEITAVamesgahdfisGFPQGYD 610
Cdd:NF040905  72 IRDSEALgivIIHQELALI---PYL---SIAENIflgneraKRGVidwneTNRRARELLAKV-----------GLDESPD 134
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 2506117   611 TEVGETGNqlsgGQRQAVALARALIRKPRLLILDDATSAL 650
Cdd:NF040905 135 TLVTDIGV----GKQQLVEIAKALSKDVKLLILDEPTAAL 170
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
480-651 1.01e-09

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: 61.49  E-value: 1.01e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    480 VKFQDVSFAYPNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLdGEPLvqydhhylhtQVA 559
Cdd:TIGR03719 323 IEAENLTKAFGDKL---LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV----------KLA 388
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    560 AVGQ--EPLLFGRSFRENIAYGLtrtpTMEEITAVAMESGAhdFISGFP-QGYDTE--VGetgnQLSGGQRQAVALARAL 634
Cdd:TIGR03719 389 YVDQsrDALDPNKTVWEEISGGL----DIIKLGKREIPSRA--YVGRFNfKGSDQQkkVG----QLSGGERNRVHLAKTL 458
                         170
                  ....*....|....*..
gi 2506117    635 IRKPRLLILDDATSALD 651
Cdd:TIGR03719 459 KSGGNVLLLDEPTNDLD 475
PLN03073 PLN03073
ABC transporter F family; Provisional
479-651 1.42e-09

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 61.41  E-value: 1.42e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   479 LVKFQDVSFAYPNHPnvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQ-YDHHylHTQ 557
Cdd:PLN03073 508 IISFSDASFGYPGGP--LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAvFSQH--HVD 583
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   558 VAAVGQEPLLFgrsfreniaygltrtptMEEITAVAMESGAHDFISGFpqgydtevGETGN-------QLSGGQRQAVAL 630
Cdd:PLN03073 584 GLDLSSNPLLY-----------------MMRCFPGVPEQKLRAHLGSF--------GVTGNlalqpmyTLSGGQKSRVAF 638
                        170       180
                 ....*....|....*....|.
gi 2506117   631 ARALIRKPRLLILDDATSALD 651
Cdd:PLN03073 639 AKITFKKPHILLLDEPSNHLD 659
3a01203 TIGR00954
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...
404-693 1.96e-09

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: 60.92  E-value: 1.96e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    404 LYLGGQLVVRGAVSSGNLVSFV--LYQLQ-FTRAVEVLLSIYPSMQK------SVGASEKIFEYLDRTPCSPLSGSLapL 474
Cdd:TIGR00954 369 FYNNGRLLLKAADALGRLMLAGrdMTRLAgFTARVDTLLQVLDDVKSgnfkrpRVEEIESGREGGRNSNLVPGRGIV--E 446
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    475 NMKGLVKFQDVSFAYPNhpNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYdhhyl 554
Cdd:TIGR00954 447 YQDNGIKFENIPLVTPN--GDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFY----- 519
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    555 htqvaaVGQEPLLFGRSFRENIAYGLT---------RTPTMEEItavaMESGAHDFISGFPQGYDTeVGETGNQLSGGQR 625
Cdd:TIGR00954 520 ------VPQRPYMTLGTLRDQIIYPDSsedmkrrglSDKDLEQI----LDNVQLTHILEREGGWSA-VQDWMDVLSGGEK 588
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2506117    626 QAVALARALIRKPRLLILDDATSALdagnQLRVQRLLYESPEWASRTVLLITQQLSLAEraHHILFLK 693
Cdd:TIGR00954 589 QRIAMARLFYHKPQFAILDECTSAV----SVDVEGYMYRLCREFGITLFSVSHRKSLWK--YHEYLLY 650
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
483-685 1.97e-09

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 60.43  E-value: 1.97e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  483 QDVSfaYPNHPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYD-HHYLHTQVAAV 561
Cdd:COG3845 261 ENLS--VRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSpRERRRLGVAYI 338
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  562 GQEPLLFG----RSFRENIAYGLTRTPTMEE---ITAVAMESGAHDFISGF---PQGYDTEVGetgnQLSGGQRQAVALA 631
Cdd:COG3845 339 PEDRLGRGlvpdMSVAENLILGRYRRPPFSRggfLDRKAIRAFAEELIEEFdvrTPGPDTPAR----SLSGGNQQKVILA 414
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 2506117  632 RALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQL----SLAER 685
Cdd:COG3845 415 RELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRD-AGAAVLLISEDLdeilALSDR 471
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
502-682 5.59e-09

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: 57.38  E-value: 5.59e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  502 TFTLY------PGKVTALVGPNGSGKSTVAALLQNLYQPTGGKvlLDGEP-------------LVQYDHHYLHTQVAAVg 562
Cdd:cd03236  14 SFKLHrlpvprEGQVLGLVGPNGIGKSTALKILAGKLKPNLGK--FDDPPdwdeildefrgseLQNYFTKLLEGDVKVI- 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  563 QEPL---LFGRSFRENIAYGLTRTPtmeeitavamESGAHDFIS---GFPQGYDTEVgetgNQLSGGQRQAVALARALIR 636
Cdd:cd03236  91 VKPQyvdLIPKAVKGKVGELLKKKD----------ERGKLDELVdqlELRHVLDRNI----DQLSGGELQRVAIAAALAR 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 2506117  637 KPRLLILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQLSL 682
Cdd:cd03236 157 DADFYFFDEPSSYLDIKQRLNAARLIRELAE-DDNYVLVVEHDLAV 201
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
502-653 5.64e-09

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 59.25  E-value: 5.64e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   502 TFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLV-QYDHHYLHTQVAAVGQEP----LLFGRSFRENI 576
Cdd:PRK10762 272 SFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVtRSPQDGLANGIVYISEDRkrdgLVLGMSVKENM 351
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   577 --------AYGLTRTPTMEEITAVAmesgahDFISGF----PqGYDTEVGEtgnqLSGGQRQAVALARALIRKPRLLILD 644
Cdd:PRK10762 352 sltalryfSRAGGSLKHADEQQAVS------DFIRLFniktP-SMEQAIGL----LSGGNQQKVAIARGLMTRPKVLILD 420

                 ....*....
gi 2506117   645 DATSALDAG 653
Cdd:PRK10762 421 EPTRGVDVG 429
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
493-650 9.66e-09

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 58.20  E-value: 9.66e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   493 PNVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPlVQY--DHHYLHTQVAAVGQE-PLLFG 569
Cdd:PRK10982   9 PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKE-IDFksSKEALENGISMVHQElNLVLQ 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   570 RSFRENIAYGltRTPTMEEItaVAMESGAHDFISGFPQ-GYDTEVGETGNQLSGGQRQAVALARALIRKPRLLILDDATS 648
Cdd:PRK10982  88 RSVMDNMWLG--RYPTKGMF--VDQDKMYRDTKAIFDElDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTS 163

                 ..
gi 2506117   649 AL 650
Cdd:PRK10982 164 SL 165
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
495-681 1.04e-08

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


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 58.97  E-value: 1.04e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117     495 VQVLQGLTFTLYPGKVTALVGPNGSGKST-VAALLQNLYQ---PTGGKVLLDGEPLVQYDHHY-----------LHTQVA 559
Cdd:TIGR00956   74 FDILKPMDGLIKPGELTVVLGRPGSGCSTlLKTIASNTDGfhiGVEGVITYDGITPEEIKKHYrgdvvynaetdVHFPHL 153
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117     560 AVGqEPLLFGRSFR--ENIAYGLTRTPTMEEITAVAMEsgahdfISGFPQGYDTEVG-ETGNQLSGGQRQAVALARALIR 636
Cdd:TIGR00956  154 TVG-ETLDFAARCKtpQNRPDGVSREEYAKHIADVYMA------TYGLSHTRNTKVGnDFVRGVSGGERKRVSIAEASLG 226
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 2506117     637 KPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLS 681
Cdd:TIGR00956  227 GAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAIYQCS 271
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
495-709 1.13e-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: 58.28  E-value: 1.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    495 VQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNL--YQPTGGKVL----------------LDGEPLVQYDHHYLHT 556
Cdd:TIGR03269  13 KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyverpsKVGEPCPVCGGTLEPE 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    557 QVAAVGQEPLLFgRSFRENIAYGLTRT--------------PTMEEITAVAMES--GAHDFISGFPQGYdtEVGETGNQL 620
Cdd:TIGR03269  93 EVDFWNLSDKLR-RRIRKRIAIMLQRTfalygddtvldnvlEALEEIGYEGKEAvgRAVDLIEMVQLSH--RITHIARDL 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    621 SGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQLS--LAERAHHILFLKEGSVC 698
Cdd:TIGR03269 170 SGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVK-ASGISMVLTSHWPevIEDLSDKAIWLENGEIK 248
                         250
                  ....*....|.
gi 2506117    699 EQGTHLQLMER 709
Cdd:TIGR03269 249 EEGTPDEVVAV 259
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
497-677 1.54e-08

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


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 55.73  E-value: 1.54e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  497 VLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLY--QPTGGKVLLDGEPLVQydhhylhtqvaavgQEPLLfgrsfrE 574
Cdd:COG2401  45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQFGR--------------EASLI------D 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  575 NIAYGLTRTPTMEEITAVAMeSGAHDFISGFPqgydtevgetgnQLSGGQRQAVALARALIRKPRLLILDDATSALDAGN 654
Cdd:COG2401 105 AIGRKGDFKDAVELLNAVGL-SDAVLWLRRFK------------ELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQT 171
                       170       180
                ....*....|....*....|...
gi 2506117  655 QLRVQRLLYESPEWASRTVLLIT 677
Cdd:COG2401 172 AKRVARNLQKLARRAGITLVVAT 194
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
496-695 2.26e-08

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


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 57.81  E-value: 2.26e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117     496 QVLQGLTFTLYPGKVTALVGPNGSGKSTvaaLLQNLYQPTGGKVLLDGEPLV-----------------QYDhhyLHTQV 558
Cdd:TIGR00956  777 VILNNVDGWVKPGTLTALMGASGAGKTT---LLNVLAERVTTGVITGGDRLVngrpldssfqrsigyvqQQD---LHLPT 850
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117     559 AAVgQEPLLFGRSFREniAYGLTRTPTMEEITAV----AMESGAhdfisgfpqgyDTEVGETGNQLSGGQRQAVALARAL 634
Cdd:TIGR00956  851 STV-RESLRFSAYLRQ--PKSVSKSEKMEYVEEVikllEMESYA-----------DAVVGVPGEGLNVEQRKRLTIGVEL 916
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2506117     635 IRKPRLLI-LDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQLS--LAERAHHILFLKEG 695
Cdd:TIGR00956  917 VAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLAD-HGQAILCTIHQPSaiLFEEFDRLLLLQKG 979
sufC PRK09580
cysteine desulfurase ATPase component; Reviewed
496-651 2.49e-08

cysteine desulfurase ATPase component; Reviewed


Pssm-ID: 181965 [Multi-domain]  Cd Length: 248  Bit Score: 55.57  E-value: 2.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   496 QVLQGLTFTLYPGKVTALVGPNGSGKSTVAALL--QNLYQPTGGKVLLDGEPLV----------------QY-------- 549
Cdd:PRK09580  15 AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLelspedragegifmafQYpveipgvs 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   550 DHHYLHTQVAAV----GQEPLlfGR-SFRENIAygltrtptmEEITAVAMesgahdfisgfPQGYDTEVGETGnqLSGGQ 624
Cdd:PRK09580  95 NQFFLQTALNAVrsyrGQEPL--DRfDFQDLME---------EKIALLKM-----------PEDLLTRSVNVG--FSGGE 150
                        170       180
                 ....*....|....*....|....*..
gi 2506117   625 RQAVALARALIRKPRLLILDDATSALD 651
Cdd:PRK09580 151 KKRNDILQMAVLEPELCILDESDSGLD 177
ABC_6TM_HetC_like cd18568
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ...
180-424 2.57e-08

Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.


Pssm-ID: 350012 [Multi-domain]  Cd Length: 294  Bit Score: 56.03  E-value: 2.57e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  180 AIPFFTGRITDWILQDKTAPSFARNMWLMCILTIASTVLEFagdgIYNITMGHMHSRVH----GEVFRAVLHQETGFFLK 255
Cdd:cd18568  20 ALPLFTQIILDRVLVHKNISLLNLILIGLLIVGIFQILLSA----VRQYLLDYFANRIDlsllSDFYKHLLSLPLSFFAS 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  256 NPTGSITSRVTED-------TSNVCESISDKLNLFLwYLGrglcllaFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQS 328
Cdd:cd18568  96 RKVGDIITRFQENqkirrflTRSALTTILDLLMVFI-YLG-------LMFYYNLQLTLIVLAFIPLYVLLTLLSSPKLKR 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  329 LAVKVQESLAKSTQVALEALSAMPTVRSFANEegeaQKFRQKLEE--MKPLN---KKEALAYVTEVwTMSVSGMLLKVGI 403
Cdd:cd18568 168 NSREIFQANAEQQSFLVEALTGIATIKALAAE----RPIRWRWENkfAKALNtrfRGQKLSIVLQL-ISSLINHLGTIAV 242
                       250       260
                ....*....|....*....|.
gi 2506117  404 LYLGGQLVVRGAVSSGNLVSF 424
Cdd:cd18568 243 LWYGAYLVISGQLTIGQLVAF 263
ABC_6TM_Rv0194_D1_like cd18543
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ...
180-455 3.35e-08

Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349987 [Multi-domain]  Cd Length: 291  Bit Score: 55.57  E-value: 3.35e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  180 AIPFFTGRITDwilqDKTAPSFARNMWLMCILTIASTVLEFAGDGIYNITMGHMHSRVH----GEVFRAVLHQETGFFLK 255
Cdd:cd18543  17 AIPLLTRRAID----GPIAHGDRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEhdlrTDLFAHLQRLDGAFHDR 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  256 NPTGSITSRVTEDTSnvceSISDKLNLFLWYLGRGLCL---LAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQSLAVK 332
Cdd:cd18543  93 WQSGQLLSRATSDLS----LVQRFLAFGPFLLGNLLTLvvgLVVMLVLSPPLALVALASLPPLVLVARRFRRRYFPASRR 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  333 VQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMkplnkkealaYVTEV----------WTMSVSGMLLKVG 402
Cdd:cd18543 169 AQDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAARRL----------RATRLraarlrarfwPLLEALPELGLAA 238
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 2506117  403 ILYLGGQLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKI 455
Cdd:cd18543 239 VLALGGWLVANGSLTLGTLVAFSAYLTMLVWPVRMLGWLLAMAQRARAAAERV 291
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
480-706 3.35e-08

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 56.19  E-value: 3.35e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   480 VKFQDVSFAYPNhpnVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDG------EP-------L 546
Cdd:PRK11000   4 VTLRNVTKAYGD---VVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEkrmndvPPaergvgmV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   547 VQYDHHYLHTQVAavgqepllfgrsfrENIAYGL-----------TRTPTMEEITAVAmesgaHdFISGFPQGydtevge 615
Cdd:PRK11000  81 FQSYALYPHLSVA--------------ENMSFGLklagakkeeinQRVNQVAEVLQLA-----H-LLDRKPKA------- 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   616 tgnqLSGGQRQAVALARALIRKPRLLILDDATSALDAGnqLRVQ----------RLlyespewaSRTVLLITQ-QLSLAE 684
Cdd:PRK11000 134 ----LSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAA--LRVQmrieisrlhkRL--------GRTMIYVTHdQVEAMT 199
                        250       260
                 ....*....|....*....|..
gi 2506117   685 RAHHILFLKEGSVCEQGTHLQL 706
Cdd:PRK11000 200 LADKIVVLDAGRVAQVGKPLEL 221
ABCG_PDR_domain2 cd03232
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...
496-695 3.68e-08

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: 54.17  E-value: 3.68e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  496 QVLQGLTFTLYPGKVTALVGPNGSGKSTvaaLLQNLYQPT-----GGKVLLDGEPLVQY--------DHHYLHTQVAAVg 562
Cdd:cd03232  21 QLLNNISGYVKPGTLTALMGESGAGKTT---LLDVLAGRKtagviTGEILINGRPLDKNfqrstgyvEQQDVHSPNLTV- 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  563 QEPLLFGRSFREniaygltrtptmeeitavamesgahdfisgfpqgydtevgetgnqLSGGQRQAVALARALIRKPRLLI 642
Cdd:cd03232  97 REALRFSALLRG---------------------------------------------LSVEQRKRLTIGVELAAKPSILF 131
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 2506117  643 LDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQLS--LAERAHHILFLKEG 695
Cdd:cd03232 132 LDEPTSGLDSQAAYNIVRFLKKLAD-SGQAILCTIHQPSasIFEKFDRLLLLKRG 185
ABC_6TM_Tm287_like cd18548
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ...
332-430 4.65e-08

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: 55.10  E-value: 4.65e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  332 KVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKK-EALAYVTEVWTMSVSGMLLkVGILYLGGQL 410
Cdd:cd18548 169 KVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKaGRLMALLNPLMMLIMNLAI-VAILWFGGHL 247
                        90       100
                ....*....|....*....|
gi 2506117  411 VVRGAVSSGNLVSFVLYQLQ 430
Cdd:cd18548 248 INAGSLQVGDLVAFINYLMQ 267
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
498-701 9.14e-08

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 54.12  E-value: 9.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   498 LQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLhtqVAAVGQE-------PLL--- 567
Cdd:PRK15056  23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VAYVPQSeevdwsfPVLved 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   568 ---FGRSFReniaYGLTRTPTMEE---ITAVAMESGAHDFisgfpqgYDTEVGEtgnqLSGGQRQAVALARALIRKPRLL 641
Cdd:PRK15056 100 vvmMGRYGH----MGWLRRAKKRDrqiVTAALARVDMVEF-------RHRQIGE----LSGGQKKRVFLARAIAQQGQVI 164
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2506117   642 ILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQL-SLAERAHHILFLKeGSVCEQG 701
Cdd:PRK15056 165 LLDEPFTGVDVKTEARIISLLRELRD-EGKTMLVSTHNLgSVTEFCDYTVMVK-GTVLASG 223
sufC TIGR01978
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ...
497-651 1.03e-07

FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 273907 [Multi-domain]  Cd Length: 243  Bit Score: 53.42  E-value: 1.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    497 VLQGLTFTLYPGKVTALVGPNGSGKSTVAALL--QNLYQPTGGKVLLDGEPLV----------------QY--------D 550
Cdd:TIGR01978  15 ILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIagHPSYEVTSGTILFKGQDLLelepderaraglflafQYpeeipgvsN 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    551 HHYLHTQVAAV----GQEPL---LFGRSFRENIAygltrtptmeeitAVAM-ESGAHDFIS-GFpqgydtevgetgnqlS 621
Cdd:TIGR01978  95 LEFLRSALNARrsarGEEPLdllDFEKLLKEKLA-------------LLDMdEEFLNRSVNeGF---------------S 146
                         170       180       190
                  ....*....|....*....|....*....|
gi 2506117    622 GGQRQAVALARALIRKPRLLILDDATSALD 651
Cdd:TIGR01978 147 GGEKKRNEILQMALLEPKLAILDEIDSGLD 176
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
504-660 1.07e-07

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 55.20  E-value: 1.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   504 TLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVllDGEPLVQYDHHYLHTQVAAVGQEpLL------FGRSF-RENI 576
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV--DPELKISYKPQYIKPDYDGTVED-LLrsitddLGSSYyKSEI 437
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   577 AYGLtrtpTMEEItavamesgahdfisgfpqgYDTEVGEtgnqLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQL 656
Cdd:PRK13409 438 IKPL----QLERL-------------------LDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRL 490

                 ....
gi 2506117   657 RVQR 660
Cdd:PRK13409 491 AVAK 494
cbiO PRK13645
energy-coupling factor transporter ATPase;
474-706 1.41e-07

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 53.86  E-value: 1.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   474 LNMKGLVKFQDVSFAYPNHP--NVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQ--- 548
Cdd:PRK13645   1 FDFSKDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAnlk 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   549 --YDHHYLHTQVAAVGQEP--LLFGRSFRENIAYG-LTRTPTMEEITAVAMEsgAHDFISgFPQGYdteVGETGNQLSGG 623
Cdd:PRK13645  81 kiKEVKRLRKEIGLVFQFPeyQLFQETIEKDIAFGpVNLGENKQEAYKKVPE--LLKLVQ-LPEDY---VKRSPFELSGG 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   624 QRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLSLAER-AHHILFLKEGSVCEQGT 702
Cdd:PRK13645 155 QKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRiADEVIVMHEGKVISIGS 234

                 ....
gi 2506117   703 HLQL 706
Cdd:PRK13645 235 PFEI 238
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
510-651 2.04e-07

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 53.72  E-value: 2.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   510 VTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVqyDHH---YLHTQVAAVG---QEPLLFGR-SFRENIAYGLTR 582
Cdd:PRK11144  26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLF--DAEkgiCLPPEKRRIGyvfQDARLFPHyKVRGNLRYGMAK 103
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2506117   583 TPTMEEITAVAMESGAHdFISGFPQGydtevgetgnqLSGGQRQAVALARALIRKPRLLILDDATSALD 651
Cdd:PRK11144 104 SMVAQFDKIVALLGIEP-LLDRYPGS-----------LSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
480-651 2.92e-07

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 53.58  E-value: 2.92e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   480 VKFQDVSFAYPNhpnvQVL-QGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLdGEPLvqydhhylhtQV 558
Cdd:PRK11819 325 IEAENLSKSFGD----RLLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV----------KL 389
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   559 AAVGQepllfgrsFRENIAYGLTrtpTMEEItavameSGAHDFIS---------------GFpQGYDTE--VGetgnQLS 621
Cdd:PRK11819 390 AYVDQ--------SRDALDPNKT---VWEEI------SGGLDIIKvgnreipsrayvgrfNF-KGGDQQkkVG----VLS 447
                        170       180       190
                 ....*....|....*....|....*....|
gi 2506117   622 GGQRQAVALARALIRKPRLLILDDATSALD 651
Cdd:PRK11819 448 GGERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
PRK13546 PRK13546
teichoic acids export ABC transporter ATP-binding subunit TagH;
490-680 4.65e-07

teichoic acids export ABC transporter ATP-binding subunit TagH;


Pssm-ID: 184131 [Multi-domain]  Cd Length: 264  Bit Score: 51.74  E-value: 4.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   490 PNHPN--VQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHHYLHTQVAAVgqepll 567
Cdd:PRK13546  30 PKHKNktFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAISAGLSGQLTGI------ 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   568 fgrsfrENIAY-----GLTRtptmEEITAVAMEsgahdfISGFpqgydTEVGETGNQ----LSGGQRQAVALARALIRKP 638
Cdd:PRK13546 104 ------ENIEFkmlcmGFKR----KEIKAMTPK------IIEF-----SELGEFIYQpvkkYSSGMRAKLGFSINITVNP 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 2506117   639 RLLILDDatsALDAGNQLRVQRLL---YESPEwASRTVLLITQQL 680
Cdd:PRK13546 163 DILVIDE---ALSVGDQTFAQKCLdkiYEFKE-QNKTIFFVSHNL 203
ABC_6TM_ABCC_D2 cd18580
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ...
190-458 4.65e-07

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: 52.12  E-value: 4.65e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  190 DWILQDKTAPSFARNMWLMCILTIASTVLEFAGDGIYNITMGHMHSR----VHGEVFRAVLHQETGFFLKNPTGSITSRV 265
Cdd:cd18580  23 DWWSSDWSSSPNSSSGYYLGVYAALLVLASVLLVLLRWLLFVLAGLRasrrLHDKLLRSVLRAPMSFFDTTPSGRILNRF 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  266 TEDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTVVTllslPLLFLLPRRLGKVYQ--SLAVKVQESLAKS--- 340
Cdd:cd18580 103 SKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVL----PPLLVVYYLLQRYYLrtSRQLRRLESESRSply 178
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  341 TQVaLEALSAMPTVRSFANEEGEAQKFRQKLEE-MKPLNkkeaLAYVTEVW-----TMSVSGMLLKVGILylggqLVVRG 414
Cdd:cd18580 179 SHF-SETLSGLSTIRAFGWQERFIEENLRLLDAsQRAFY----LLLAVQRWlglrlDLLGALLALVVALL-----AVLLR 248
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 2506117  415 AVSSGNLVSFVLYQ-LQFTRAVEVLLSIYPSMQKSVGASEKIFEY 458
Cdd:cd18580 249 SSISAGLVGLALTYaLSLTGSLQWLVRQWTELETSMVSVERILEY 293
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
491-695 4.96e-07

ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.


Pssm-ID: 213194 [Multi-domain]  Cd Length: 162  Bit Score: 50.05  E-value: 4.96e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  491 NHPNVQVLQGLTFTlyPGKVTALVGPNGSGKSTVAallqnlyqptggkvlldgeplvqydhhylhTQVAAVgqeplLFGR 570
Cdd:cd03227   6 RFPSYFVPNDVTFG--EGSLTIITGPNGSGKSTIL------------------------------DAIGLA-----LGGA 48
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  571 SFRENIAYGLTRTptmEEITAVAMEsgahdFISGFPQgydtevgetgnqLSGGQRQAVALARALI---RKPR-LLILDDA 646
Cdd:cd03227  49 QSATRRRSGVKAG---CIVAAVSAE-----LIFTRLQ------------LSGGEKELSALALILAlasLKPRpLYILDEI 108
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 2506117  647 TSALDAGNQLRVQRLLYE-SPEwaSRTVLLITQQLSLAERA---HHILFLKEG 695
Cdd:cd03227 109 DRGLDPRDGQALAEAILEhLVK--GAQVIVITHLPELAELAdklIHIKKVITG 159
ABC_6TM_exporter_like cd18564
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
188-455 6.55e-07

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


Pssm-ID: 350008 [Multi-domain]  Cd Length: 307  Bit Score: 51.74  E-value: 6.55e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  188 ITDWILQDKTAPSFA--------RNM---WLMCILTIASTVLEFAGDGIYNITMG----HMHSRVHGEVFRAVLHQETGF 252
Cdd:cd18564  25 VIDDVLGDKPLPGLLglapllgpDPLallLLAAAALVGIALLRGLASYAGTYLTAlvgqRVVLDLRRDLFAHLQRLSLSF 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  253 FLKNPTGSITSRVTEDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQSLAVK 332
Cdd:cd18564 105 HDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGVMFWLDWQLALIALAVAPLLLLAARRFSRRIKEASRE 184
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  333 VQESLAKSTQVALEALSAMPTVRSFANEEGEAQKF----RQKLEE-MKPLNKKEALAYVTEVwTMSVSGMLlkvgILYLG 407
Cdd:cd18564 185 QRRREGALASVAQESLSAIRVVQAFGREEHEERRFarenRKSLRAgLRAARLQALLSPVVDV-LVAVGTAL----VLWFG 259
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 2506117  408 GQLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKI 455
Cdd:cd18564 260 AWLVLAGRLTPGDLLVFLAYLKNLYKPVRDLAKLTGRIAKASASAERV 307
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
483-651 6.91e-07

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 52.65  E-value: 6.91e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   483 QDVSFAYPNHpnvQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLdGEPL-VQY-DHHYlhtqvAA 560
Cdd:PRK11147 323 ENVNYQIDGK---QLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTKLeVAYfDQHR-----AE 393
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   561 VGQEpllfgRSFRENIAYGltrtptMEEITAVAMESGAHDFISGF---PQGYDTEVgetgNQLSGGQRQAVALARALIRK 637
Cdd:PRK11147 394 LDPE-----KTVMDNLAEG------KQEVMVNGRPRHVLGYLQDFlfhPKRAMTPV----KALSGGERNRLLLARLFLKP 458
                        170
                 ....*....|....
gi 2506117   638 PRLLILDDATSALD 651
Cdd:PRK11147 459 SNLLILDEPTNDLD 472
ycf16 CHL00131
sulfate ABC transporter protein; Validated
494-550 8.10e-07

sulfate ABC transporter protein; Validated


Pssm-ID: 214372 [Multi-domain]  Cd Length: 252  Bit Score: 50.80  E-value: 8.10e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 2506117   494 NVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQN--LYQPTGGKVLLDGEPLVQYD 550
Cdd:CHL00131  19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLE 77
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
504-662 1.98e-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: 50.94  E-value: 1.98e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  504 TLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVllDGEPLVQYDHHYLHTQVAAVGQEPLlfgrsfRENIAYGLTRT 583
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV--DEDLKISYKPQYISPDYDGTVEEFL------RSANTDDFGSS 433
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  584 PTMEEITavamesgahdfisgFPQG----YDTEVGEtgnqLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQ 659
Cdd:COG1245 434 YYKTEII--------------KPLGleklLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVA 495

                ...
gi 2506117  660 RLL 662
Cdd:COG1245 496 KAI 498
PRK15093 PRK15093
peptide ABC transporter ATP-binding protein SapD;
485-707 2.29e-06

peptide ABC transporter ATP-binding protein SapD;


Pssm-ID: 185049 [Multi-domain]  Cd Length: 330  Bit Score: 50.19  E-value: 2.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   485 VSFAYPNHPnVQVLQGLTFTLYPGKVTALVGPNGSGKSTVA----ALLQNLYQPTGGKVLLDGEPLVQYD----HHYLHT 556
Cdd:PRK15093  11 IEFKTSDGW-VKAVDRVSMTLTEGEIRGLVGESGSGKSLIAkaicGVTKDNWRVTADRMRFDDIDLLRLSprerRKLVGH 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   557 QVAAVGQEPLL-------FGRSFRENIA-----------YGLTRTPTMEEITAVAMESgAHDFISGFPQgydtevgetgn 618
Cdd:PRK15093  90 NVSMIFQEPQScldpserVGRQLMQNIPgwtykgrwwqrFGWRKRRAIELLHRVGIKD-HKDAMRSFPY----------- 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   619 QLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEWASRTVLLITQQLS-LAERAHHILFLKEGSV 697
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQmLSQWADKINVLYCGQT 237
                        250
                 ....*....|
gi 2506117   698 CEQGTHLQLM 707
Cdd:PRK15093 238 VETAPSKELV 247
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
508-705 2.35e-06

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: 48.34  E-value: 2.35e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  508 GKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDgeplvqydhhylhtqvaavgqepllfgrsfRENIAYGltrtptme 587
Cdd:cd03222  25 GEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWD------------------------------GITPVYK-------- 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  588 eitavamesgahdfisgfPQGYDtevgetgnqLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPE 667
Cdd:cd03222  67 ------------------PQYID---------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSE 119
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 2506117  668 WASRTVLLITQQLSLAERAHHILFLKEGSVCEQGTHLQ 705
Cdd:cd03222 120 EGKKTALVVEHDLAVLDYLSDRIHVFEGEPGVYGIASQ 157
ABC_6TM_exporter_like cd18565
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
206-432 3.84e-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: 350009 [Multi-domain]  Cd Length: 313  Bit Score: 49.49  E-value: 3.84e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  206 WLMCILTIASTVLEFAGDGIYNITMGH-----MHS-RVhgEVFRAVLHQETGFFLKNPTGSITSRVTEDTSNVCESISDK 279
Cdd:cd18565  54 WLLGGLTVAAFLLESLFQYLSGVLWRRfaqrvQHDlRT--DTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDG 131
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  280 LNLFLWYLGRGLCLLAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQSLAVKVQESLAK-STQvaLE-ALSAMPTVRSF 357
Cdd:cd18565 132 ANSIIRVVVTVLGIGAILFYLNWQLALVALLPVPLIIAGTYWFQRRIEPRYRAVREAVGDlNAR--LEnNLSGIAVIKAF 209
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  358 ANEEGEAQKFRQKLEEMKPLNK---KEALAYVTEVWTMSVSGMLLkvgILYLGGQLVVRGAV------SSGNLVSFVLYQ 428
Cdd:cd18565 210 TAEDFERERVADASEEYRDANWraiRLRAAFFPVIRLVAGAGFVA---TFVVGGYWVLDGPPlftgtlTVGTLVTFLFYT 286

                ....
gi 2506117  429 LQFT 432
Cdd:cd18565 287 QRLL 290
ABC_6TM_CyaB_HlyB_like cd18588
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ...
180-446 3.91e-06

Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunits of T1SS, such as CyaG and HlyB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. Additionally, CyaB is part of the three T1SS complex proteins for adenylate cyclase toxin CyaA, which is a primary virulence factor in Bordetella pertussis: CyaB (an ABC transporter) CyaD (a membrane fusion protein), and CyaE (an outer membrane protein).


Pssm-ID: 350032 [Multi-domain]  Cd Length: 294  Bit Score: 49.42  E-value: 3.91e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  180 AIPFFTGRITDWILQDKTAPSFARNMWLMCILTIASTVLEFAGDGIYNitmgHMHSRVHGE----VFRAVLHQETGFFLK 255
Cdd:cd18588  20 VTPLFFQVIIDKVLVHRSLSTLDVLAIGLLVVALFEAVLSGLRTYLFS----HTTNRIDAElgarLFRHLLRLPLSYFES 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  256 NPTGSITSRVTEdtsnvCESISDklnlFLwyLGRGLCL----------LAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKV 325
Cdd:cd18588  96 RQVGDTVARVRE-----LESIRQ----FL--TGSALTLvldlvfsvvfLAVMFYYSPTLTLIVLASLPLYALLSLLVTPI 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  326 YQSLAVKVQESLAKSTQVALEALSAMPTVRSFANEegeaQKFRQKLEEMkplnkkeaLA-YVTEV--------WTMSVSG 396
Cdd:cd18588 165 LRRRLEEKFQRGAENQSFLVETVTGIETVKSLAVE----PQFQRRWEEL--------LArYVKASfktanlsnLASQIVQ 232
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 2506117  397 MLLK---VGILYLGGQLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQ 446
Cdd:cd18588 233 LIQKlttLAILWFGAYLVMDGELTIGQLIAFNMLAGQVSQPVLRLVQLWQDFQ 285
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
497-651 5.73e-06

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 49.78  E-value: 5.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   497 VLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGeplvqydhhylHTQVAAVGQE-PLLF------- 568
Cdd:PRK10636  16 LLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPG-----------NWQLAWVNQEtPALPqpaleyv 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   569 ---GRSFRE-----------NIAYGL-TRTPTMEEITAVAMESGAHDFIS--GFPQgydTEVGETGNQLSGGQRQAVALA 631
Cdd:PRK10636  85 idgDREYRQleaqlhdanerNDGHAIaTIHGKLDAIDAWTIRSRAASLLHglGFSN---EQLERPVSDFSGGWRMRLNLA 161
                        170       180
                 ....*....|....*....|
gi 2506117   632 RALIRKPRLLILDDATSALD 651
Cdd:PRK10636 162 QALICRSDLLLLDEPTNHLD 181
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
502-697 8.20e-06

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 49.14  E-value: 8.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   502 TFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVqydhhyLHTQVAAV-----------GQEPLLFGR 570
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPID------IRSPRDAIragimlcpedrKAEGIIPVH 346
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   571 SFRENIAygltrtptmeeITAVAMESGAHDFISGfpqGYDTEVGET-----------GNQ----LSGGQRQAVALARALI 635
Cdd:PRK11288 347 SVADNIN-----------ISARRHHLRAGCLINN---RWEAENADRfirslniktpsREQlimnLSGGNQQKAILGRWLS 412
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2506117   636 RKPRLLILDDATSALDAGNQLRVQRLLYESPEwASRTVLLITQQL----SLAERahhILFLKEGSV 697
Cdd:PRK11288 413 EDMKVILLDEPTRGIDVGAKHEIYNVIYELAA-QGVAVLFVSSDLpevlGVADR---IVVMREGRI 474
PLN03073 PLN03073
ABC transporter F family; Provisional
586-651 9.86e-06

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 49.09  E-value: 9.86e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2506117   586 MEEITAVAMESGAHDFISGFPQGYDTEVGETgNQLSGGQRQAVALARALIRKPRLLILDDATSALD 651
Cdd:PLN03073 312 LELIDAYTAEARAASILAGLSFTPEMQVKAT-KTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
ABC_6TM_YOR1_D2_like cd18606
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ...
211-373 1.20e-05

Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.


Pssm-ID: 350050 [Multi-domain]  Cd Length: 290  Bit Score: 47.85  E-value: 1.20e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  211 LTIASTVLEFAGdGIYNITMGHMHSRV-HGEVFRAVLHQETGFFLKNPTGSITSRVTEDTSNVCESISDKLNLFLwylgr 289
Cdd:cd18606  44 LGVLQAIFLFLF-GLLLAYLGIRASKRlHNKALKRVLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFL----- 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  290 glcLLAFMIWGSFYLTVVT----LLSLPLLFLLPRRLGKVYQSLA--VKVQESLAKSTQVAL--EALSAMPTVRSFanee 361
Cdd:cd18606 118 ---YTLSSIIGTFILIIIYlpwfAIALPPLLVLYYFIANYYRASSreLKRLESILRSFVYANfsESLSGLSTIRAY---- 190
                       170
                ....*....|..
gi 2506117  362 GEAQKFRQKLEE 373
Cdd:cd18606 191 GAQDRFIKKNEK 202
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
620-698 1.33e-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: 48.28  E-value: 1.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117    620 LSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYespEWASRTVLLITQQLSLAE---RAHHILFLKEGS 696
Cdd:TIGR02633 404 LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLIN---QLAQEGVAIIVVSSELAEvlgLSDRVLVIGEGK 480

                  ..
gi 2506117    697 VC 698
Cdd:TIGR02633 481 LK 482
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
479-651 1.44e-05

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 48.41  E-value: 1.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   479 LVKFQDVSFAYPNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTvaaLLQNLyqptGGKVLLD---------------- 542
Cdd:PRK11147   3 LISIHGAWLSFSDAP---LLDNAELHIEDNERVCLVGRNGAGKST---LMKIL----NGEVLLDdgriiyeqdlivarlq 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   543 ----------------------GEPLVQYdHHYLHTqvaaVGQEPllfgrsfRENIaygLTRTPTMEEITAVA----MES 596
Cdd:PRK11147  73 qdpprnvegtvydfvaegieeqAEYLKRY-HDISHL----VETDP-------SEKN---LNELAKLQEQLDHHnlwqLEN 137
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 2506117   597 GAHDFISGFPQGYDTEVGEtgnqLSGG-QRQAvALARALIRKPRLLILDDATSALD 651
Cdd:PRK11147 138 RINEVLAQLGLDPDAALSS----LSGGwLRKA-ALGRALVSNPDVLLLDEPTNHLD 188
ABC_6TM_PrtD_LapB_HlyB_like cd18782
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ...
179-446 1.88e-05

uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.


Pssm-ID: 350055 [Multi-domain]  Cd Length: 294  Bit Score: 47.20  E-value: 1.88e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  179 MAIPFFTGRITDWILQDKTAPSFARNMWLMCILTIASTVLEFAGDGIYNITMGHMHSRVHGEVFRAVLHQETGFFLKNPT 258
Cdd:cd18782  19 LANPLLFQVIIDKVLVQQDLATLYVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGTIIDHLLRLPLGFFDKRPV 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  259 GSITSRVTEdtsnvcesiSDKLNLFLwyLGRGLCL----------LAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQS 328
Cdd:cd18782  99 GELSTRISE---------LDTIRGFL--TGTALTTlldvlfsviyIAVLFSYSPLLTLVVLATVPLQLLLTFLFGPILRR 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  329 LAVKVQESLAKSTQVALEALSAMPTVRSFANEEgeaqKFRQKLEEmkplnkkEALAYVTEVWTMSVSGMLL--------- 399
Cdd:cd18782 168 QIRRRAEASAKTQSYLVESLTGIQTVKAQNAEL----KARWRWQN-------RYARSLGEGFKLTVLGTTSgslsqflnk 236
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 2506117  400 --KVGILYLGGQLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQ 446
Cdd:cd18782 237 lsSLLVLWVGAYLVLRGELTLGQLIAFRILSGYVTGPILRLSTLWQQFQ 285
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
501-653 4.64e-05

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 46.58  E-value: 4.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   501 LTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEplvqydhhylhtqvaavgqepLLFGRSFRENIAYGL 580
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGK---------------------EINALSTAQRLARGL 340
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   581 TRTPTMEEITAVAMESG--------AHDFISGFPQ-GYDTEVGET-----------GNQ----LSGGQRQAVALARALIR 636
Cdd:PRK15439 341 VYLPEDRQSSGLYLDAPlawnvcalTHNRRGFWIKpARENAVLERyrralnikfnhAEQaartLSGGNQQKVLIAKCLEA 420
                        170
                 ....*....|....*..
gi 2506117   637 KPRLLILDDATSALDAG 653
Cdd:PRK15439 421 SPQLLIVDEPTRGVDVS 437
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
503-664 6.37e-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: 46.32  E-value: 6.37e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  503 FTLY------PGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVllDGEPlvQYD---HHYLHTQVaavgQEPLlfgrsfr 573
Cdd:COG1245  88 FRLYglpvpkKGKVTGILGPNGIGKSTALKILSGELKPNLGDY--DEEP--SWDevlKRFRGTEL----QDYF------- 152
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  574 ENIAYGltrtptmeEITaVAMESGAHDFIsgfPQGYDTEVG-------ETG-------------------NQLSGGQRQA 627
Cdd:COG1245 153 KKLANG--------EIK-VAHKPQYVDLI---PKVFKGTVRellekvdERGkldelaeklglenildrdiSELSGGELQR 220
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 2506117  628 VALARALIRKPRLLILDDATSALDAGNQLRVQRLLYE 664
Cdd:COG1245 221 VAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRE 257
PRK13543 PRK13543
heme ABC exporter ATP-binding protein CcmA;
473-662 6.63e-05

heme ABC exporter ATP-binding protein CcmA;


Pssm-ID: 184129 [Multi-domain]  Cd Length: 214  Bit Score: 44.84  E-value: 6.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   473 PLNMKGLVKFQDVSFAYPNHPnvqVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQYDHh 552
Cdd:PRK13543   5 LHTAPPLLAAHALAFSRNEEP---VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDR- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   553 ylHTQVAAVGQEPLLFGR-SFRENIAY--GLT-RTPTMEEITAVAmesgahdfISGFPQGYDTEVgetgNQLSGGQRQAV 628
Cdd:PRK13543  81 --SRFMAYLGHLPGLKADlSTLENLHFlcGLHgRRAKQMPGSALA--------IVGLAGYEDTLV----RQLSAGQKKRL 146
                        170       180       190
                 ....*....|....*....|....*....|....
gi 2506117   629 ALARALIRKPRLLILDDATSALDAGNQLRVQRLL 662
Cdd:PRK13543 147 ALARLWLSPAPLWLLDEPYANLDLEGITLVNRMI 180
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
468-711 8.40e-05

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 45.50  E-value: 8.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   468 SGSLAPLNMKGLVKfqdvsfaypNHPNVQVLQGLTFTLYPGKVTALVGPNGSGKSTvAALLQNLYQPTGGKvlldgEP-- 545
Cdd:NF000106   8 NGARNAVEVRGLVK---------HFGEVKAVDGVDLDVREGTVLGVLGP*GAA**R-GALPAHV*GPDAGR-----RPwr 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   546 LVQYDHHYLHTQVAAVGQEPLLFGR----SFRENIaYGLTRTPTMEEITAVAMesgAHDFISGFpqGYDTEVGETGNQLS 621
Cdd:NF000106  73 F*TWCANRRALRRTIG*HRPVR*GRresfSGRENL-YMIGR*LDLSRKDARAR---ADELLERF--SLTEAAGRAAAKYS 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   622 GGQRQAVALARALIRKPRLLILDDATSALDAgnqlRVQRLLYESPEWASR---TVLLITQQLSLAER-AHHILFLKEGSV 697
Cdd:NF000106 147 GGMRRRLDLAASMIGRPAVLYLDEPTTGLDP----RTRNEVWDEVRSMVRdgaTVLLTTQYMEEAEQlAHELTVIDRGRV 222
                        250
                 ....*....|....
gi 2506117   698 CEQGTHLQLMERGG 711
Cdd:NF000106 223 IADGKVDELKTKVG 236
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
497-662 8.90e-05

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 45.78  E-value: 8.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   497 VLQGLTFTLYPGKVTALVGPNGSGKSTVAALLqnlyqpTGGkvlldgeplvqydhhylHTQvaAVGQEPLLFGR------ 570
Cdd:PRK10938 275 ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLI------TGD-----------------HPQ--GYSNDLTLFGRrrgsge 329
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   571 ---SFRENIAYgLTRTPTME-----EITAVAMeSGAHDFISGFPQ----------------GYDTEVGETGNQ-LSGGQR 625
Cdd:PRK10938 330 tiwDIKKHIGY-VSSSLHLDyrvstSVRNVIL-SGFFDSIGIYQAvsdrqqklaqqwldilGIDKRTADAPFHsLSWGQQ 407
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 2506117   626 QAVALARALIRKPRLLILDDATSALDAGNQLRVQRLL 662
Cdd:PRK10938 408 RLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFV 444
ABC_6TM_Sav1866_like cd18554
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ...
252-455 9.94e-05

Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.


Pssm-ID: 349998 [Multi-domain]  Cd Length: 299  Bit Score: 45.10  E-value: 9.94e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  252 FFLKNPTGSITSRVTEDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQSLAV 331
Cdd:cd18554  96 YYANNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLVIFPFYILAVKYFFGRLRKLTK 175
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  332 KVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLE--EMKPLNKKEALAY-VTEVWTMSVSGMLLKVGIlylGG 408
Cdd:cd18554 176 ERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGhfLTRALKHTRWNAKtFSAVNTITDLAPLLVIGF---AA 252
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 2506117  409 QLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKI 455
Cdd:cd18554 253 YLVIEGNLTVGTLVAFVGYMERMYSPLRRLVNSFTTLTQSFASMDRV 299
PRK13541 PRK13541
cytochrome c biogenesis protein CcmA; Provisional
494-662 1.03e-04

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184128 [Multi-domain]  Cd Length: 195  Bit Score: 44.09  E-value: 1.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   494 NVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDG-------EPLVQYDHHYLHTQVAAVGQEPL 566
Cdd:PRK13541  12 EQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNcninniaKPYCTYIGHNLGLKLEMTVFENL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   567 LFGRSFRENIaygltrtptmEEITAVAMESGAHDFISgfpqgydtevgETGNQLSGGQRQAVALARALIRKPRLLILDDA 646
Cdd:PRK13541  92 KFWSEIYNSA----------ETLYAAIHYFKLHDLLD-----------EKCYSLSSGMQKIVAIARLIACQSDLWLLDEV 150
                        170
                 ....*....|....*.
gi 2506117   647 TSALDAGNQLRVQRLL 662
Cdd:PRK13541 151 ETNLSKENRDLLNNLI 166
ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 cd18560
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ...
182-449 1.31e-04

Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group represents the Atm1/ABCB7/HMT1/ABCB6 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia. ABCB6 is originally identified as a porphyrin transporter present in the outer membrane of mitochondria. It is highly expressed in cells resistance to arsenic and protects against arsenic cytotoxicity. Moreover, Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster.


Pssm-ID: 350004 [Multi-domain]  Cd Length: 292  Bit Score: 44.52  E-value: 1.31e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  182 PFFTGRITDwILQDKTAPSFARNMW---LMCILTIASTVLEFAGDGIYNITMGHMHSRVHGEVFRAVLHQETGFFLKNPT 258
Cdd:cd18560  16 PLFLGRAVN-ALTLAKVKDLESAVTlilLYALLRFSSKLLKELRSLLYRRVQQNAYRELSLKTFAHLHSLSLDWHLSKKT 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  259 GSITSRVTEDTsnvcESISDKLNLFLWYLGR-----GLCLLAFMIWGSFYLTVVTLLSLPllfllprrlgkVYQSLAVKV 333
Cdd:cd18560  95 GEVVRIMDRGT----ESANTLLSYLVFYLVPtllelIVVSVVFAFHFGAWLALIVFLSVL-----------LYGVFTIKV 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  334 QESLAK-----------STQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKEALAYVTEVWTMSVSGMLLKVG 402
Cdd:cd18560 160 TEWRTKfrraankkdneAHDIAVDSLLNFETVKYFTNEKYEVDRYGEAVKEYQKSSVKVQASLSLLNVGQQLIIQLGLTL 239
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 2506117  403 ILYLGGQLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSV 449
Cdd:cd18560 240 GLLLAGYRVVDGGLSVGDFVAVNTYIFQLFQPLNFLGTIYRMIIQSL 286
ABC_6TM_Rv0194_D2_like cd18546
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ...
346-455 1.61e-04

Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349990 [Multi-domain]  Cd Length: 292  Bit Score: 44.40  E-value: 1.61e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  346 EALSAMPTVRSFANEEGEAQKFRQkleemkpLNKKEALAYVTEVWTMSV-------SGMLLKVGILYLGGQLVVRGAVSS 418
Cdd:cd18546 183 ETLAGIRVVQAFRRERRNAERFAE-------LSDDYRDARLRAQRLVAIyfpgvelLGNLATAAVLLVGAWRVAAGTLTV 255
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 2506117  419 GNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKI 455
Cdd:cd18546 256 GVLVAFLLYLRRFFAPIQQLSQVFDSYQQARAALEKI 292
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
503-676 2.15e-04

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 44.41  E-value: 2.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   503 FTLY------PGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVllDGEPlvQYDH---HYLHTQvaavgqeplLFgrSFR 573
Cdd:PRK13409  88 FKLYglpipkEGKVTGILGPNGIGKTTAVKILSGELIPNLGDY--EEEP--SWDEvlkRFRGTE---------LQ--NYF 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   574 ENIAYGltrtptmeEITAVamesgaH-----DFIsgfPQGYDTEVG-------ETG-------------------NQLSG 622
Cdd:PRK13409 153 KKLYNG--------EIKVV------HkpqyvDLI---PKVFKGKVRellkkvdERGkldevverlglenildrdiSELSG 215
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 2506117   623 GQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYESPEwaSRTVLLI 676
Cdd:PRK13409 216 GELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAE--GKYVLVV 267
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
619-653 3.47e-04

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 43.76  E-value: 3.47e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 2506117   619 QLSGGQRQAVALARALIRKPRLLILDDATSALDAG 653
Cdd:PRK13549 405 RLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVG 439
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
480-712 4.92e-04

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 43.57  E-value: 4.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   480 VKFQDVSFAYPNhpnVQVLQGLTFTLYPGKVTALVGPNGSGKSTVAALLqnlyqpTGGKVLLDGEPLV----QYDHHYLh 555
Cdd:NF033858   2 ARLEGVSHRYGK---TVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLI------AGARKIQQGRVEVlggdMADARHR- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   556 tqvAAVGQE----PLLFGR------SFRENIA-----YGLTRTPTMEEITAVAMESGAHDFISGfPQGydtevgetgnQL 620
Cdd:NF033858  72 ---RAVCPRiaymPQGLGKnlyptlSVFENLDffgrlFGQDAAERRRRIDELLRATGLAPFADR-PAG----------KL 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   621 SGGQRQAVALARALIRKPRLLILDDATSALD--AGNQ-------LRVQRllyespewASRTVLLITQQLSLAERAHHILF 691
Cdd:NF033858 138 SGGMKQKLGLCCALIHDPDLLILDEPTTGVDplSRRQfwelidrIRAER--------PGMSVLVATAYMEEAERFDWLVA 209
                        250       260
                 ....*....|....*....|.
gi 2506117   692 LKEGSVCEQGTHLQLMERGGC 712
Cdd:NF033858 210 MDAGRVLATGTPAELLARTGA 230
ABC_6TM_CvaB_RaxB_like cd18567
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ...
345-435 5.39e-04

Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium.


Pssm-ID: 350011 [Multi-domain]  Cd Length: 294  Bit Score: 42.45  E-value: 5.39e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  345 LEALSAMPTVRSFANEEGEAQKFRQKLEEMkpLNKKEALAYVTeVWTMSVSGMLL---KVGILYLGGQLVVRGAVSSGNL 421
Cdd:cd18567 184 LETIRGIQTIKLFGREAEREARWLNLLVDA--INADIRLQRLQ-ILFSAANGLLFgleNILVIYLGALLVLDGEFTVGML 260
                        90
                ....*....|....
gi 2506117  422 VSFVLYQLQFTRAV 435
Cdd:cd18567 261 FAFLAYKDQFSSRA 274
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
515-651 5.69e-04

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 43.19  E-value: 5.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   515 GPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLvqyDHHYLHT--QVAAVGQEPLLFGR-SFRENIA-----YGLTRTPTM 586
Cdd:NF033858 299 GSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV---DAGDIATrrRVGYMSQAFSLYGElTVRQNLElharlFHLPAAEIA 375
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2506117   587 EEITAVAMESGAHDFISGFPqgydtevgetgNQLSGGQRQAVALARALIRKPRLLILDDATSALD 651
Cdd:NF033858 376 ARVAEMLERFDLADVADALP-----------DSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
ABC_6TM_exporter_like cd18540
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
252-455 5.99e-04

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: 42.47  E-value: 5.99e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  252 FFLKNPTGSITSRVTEDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQSLAV 331
Cdd:cd18540  92 YFDKTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVPVLAVVSIYFQKKILKAYR 171
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  332 KVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKEAL---AYVTEVWTMSVSGMLLkvgILYLGG 408
Cdd:cd18540 172 KVRKINSRITGAFNEGITGAKTTKTLVREEKNLREFKELTEEMRRASVRAARlsaLFLPIVLFLGSIATAL---VLWYGG 248
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 2506117  409 QLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKI 455
Cdd:cd18540 249 ILVLAGAITIGTLVAFISYATQFFEPIQQLARVLAELQSAQASAERV 295
tagH PRK13545
teichoic acids export protein ATP-binding subunit; Provisional
476-681 1.23e-03

teichoic acids export protein ATP-binding subunit; Provisional


Pssm-ID: 184130 [Multi-domain]  Cd Length: 549  Bit Score: 42.18  E-value: 1.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   476 MKGLVKFQDVSFAYP--NHPNVQV---------------LQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGK 538
Cdd:PRK13545   1 MNYKVKFEHVTKKYKmyNKPFDKLkdlffrskdgeyhyaLNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117   539 VLLDGEPLVQYDHHYLHTQVAAVgqepllfgrsfrENIAY-GLTRTPTMEEITAVAmesgahdfisgfPQGYD-TEVGET 616
Cdd:PRK13545  81 VDIKGSAALIAISSGLNGQLTGI------------ENIELkGLMMGLTKEKIKEII------------PEIIEfADIGKF 136
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2506117   617 GNQ----LSGGQRQAVALARALIRKPRLLILDDatsALDAGNQLRVQRLLYESPEWAS--RTVLLITQQLS 681
Cdd:PRK13545 137 IYQpvktYSSGMKSRLGFAISVHINPDILVIDE---ALSVGDQTFTKKCLDKMNEFKEqgKTIFFISHSLS 204
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
475-665 1.56e-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: 1.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117     475 NMKGLVKFQDVSFAYPNHPNVQVlQGLTFTLYPGKVTALVGPNGSGKSTVAALLQNLYQPTGGKVLLDGEPLVQyDHHYL 554
Cdd:TIGR01257 1933 NKTDILRLNELTKVYSGTSSPAV-DRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDV 2010
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117     555 HTQVAAVGQ----EPLLFGRsfrENI-AYGLTRTPTMEEITAVAMESgahdfISGFpqGYDTEVGETGNQLSGGQRQAVA 629
Cdd:TIGR01257 2011 HQNMGYCPQfdaiDDLLTGR---EHLyLYARLRGVPAEEIEKVANWS-----IQSL--GLSLYADRLAGTYSGGNKRKLS 2080
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 2506117     630 LARALIRKPRLLILDDATSALDAgnqlRVQRLLYES 665
Cdd:TIGR01257 2081 TAIALIGCPPLVLLDEPTTGMDP----QARRMLWNT 2112
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
608-664 2.48e-03

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 40.87  E-value: 2.48e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 2506117   608 GYDTEVGetgnQLSGGQRQAVALARALIRKPRLLILDDATSALDAGNQLRVQRLLYE 664
Cdd:PRK10982 384 GHRTQIG----SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAE 436
SRP54 pfam00448
SRP54-type protein, GTPase domain; This family includes relatives of the G-domain of the SRP54 ...
509-541 3.65e-03

SRP54-type protein, GTPase domain; This family includes relatives of the G-domain of the SRP54 family of proteins.


Pssm-ID: 459814 [Multi-domain]  Cd Length: 193  Bit Score: 39.06  E-value: 3.65e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2506117    509 KVTALVGPNGSGKSTVAALLQNLYQPTGGKVLL 541
Cdd:pfam00448   1 NVILLVGLQGSGKTTTIAKLAAYLKKKGKKVLL 33
COG3910 COG3910
Predicted ATPase [General function prediction only];
488-523 5.00e-03

Predicted ATPase [General function prediction only];


Pssm-ID: 443116 [Multi-domain]  Cd Length: 239  Bit Score: 39.36  E-value: 5.00e-03
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 2506117  488 AYPNH-PNVQVLQGLTFTlypGKVTALVGPNGSGKST 523
Cdd:COG3910  19 AYPFNlPAVRNLEGLEFH---PPVTFFVGENGSGKST 52
ABC_6TM_MRP7_D2_like cd18605
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ...
236-372 5.70e-03

Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).


Pssm-ID: 350049 [Multi-domain]  Cd Length: 300  Bit Score: 39.44  E-value: 5.70e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  236 RVHGEVFRAVLHQETGFFLKNPTGSITSRVTEDTSNVCESISDKLNLFLWYLGRGLCLLAFMIWGSFYLTVVTllslPLL 315
Cdd:cd18605  76 RLHNKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQLFGLLGYLVVICYQLPWLLLLL----LPL 151
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2506117  316 FLLPRRLGKVYQSLA--VKVQESLAKS---TQVAlEALSAMPTVRSFANEEGEAQKFRQKLE 372
Cdd:cd18605 152 AFIYYRIQRYYRATSreLKRLNSVNLSplyTHFS-ETLKGLVTIRAFRKQERFLKEYLEKLE 212
AAA_23 pfam13476
AAA domain;
494-532 5.86e-03

AAA domain;


Pssm-ID: 463890 [Multi-domain]  Cd Length: 190  Bit Score: 38.63  E-value: 5.86e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2506117    494 NVQVLQGLTFTLYPGkVTALVGPNGSGKST-VAALLQNLY 532
Cdd:pfam13476   5 NFRSFRDQTIDFSKG-LTLITGPNGSGKTTiLDAIKLALY 43
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
502-522 6.07e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.92  E-value: 6.07e-03
                        10        20
                ....*....|....*....|.
gi 2506117  502 TFTLYPGkVTALVGPNGSGKS 522
Cdd:COG1196  19 TIPFEPG-ITAIVGPNGSGKS 38
COG4637 COG4637
Predicted ATPase [General function prediction only];
503-524 6.13e-03

Predicted ATPase [General function prediction only];


Pssm-ID: 443675 [Multi-domain]  Cd Length: 371  Bit Score: 39.53  E-value: 6.13e-03
                        10        20
                ....*....|....*....|..
gi 2506117  503 FTLYPGKVTALVGPNGSGKSTV 524
Cdd:COG4637  16 LELPLGPLTVLIGANGSGKSNL 37
ABC_6TM_T1SS_like cd18555
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ...
180-455 7.19e-03

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: 39.03  E-value: 7.19e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  180 AIPFFTGRITDWILQDKTAPSFARNMWLMCILTIASTVLEFAgDGIYNITMG-HMHSRVHGEVFRAVLHQETGFFLKNPT 258
Cdd:cd18555  20 LIPILTQYVIDNVIVPGNLNLLNVLGIGILILFLLYGLFSFL-RGYIIIKLQtKLDKSLMSDFFEHLLKLPYSFFENRSS 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  259 GSITSRVTED-------TSNVCESISDKLNLFLwylgrglcLLAFMIWGSFYLTVVTLLSLPLLFLLPRRLGKVYQSLAV 331
Cdd:cd18555  99 GDLLFRANSNvyirqilSNQVISLIIDLLLLVI--------YLIYMLYYSPLLTLIVLLLGLLIVLLLLLTRKKIKKLNQ 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506117  332 KVQESLAKSTQVALEALSAMPTVRSFANEEGEAQKFRQKLEEMKPLNKKEA--LAYVTevwTMSVS-GMLLKVGILYLGG 408
Cdd:cd18555 171 EEIVAQTKVQSYLTETLYGIETIKSLGSEKNIYKKWENLFKKQLKAFKKKErlSNILN---SISSSiQFIAPLLILWIGA 247
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 2506117  409 QLVVRGAVSSGNLVSFVLYQLQFTRAVEVLLSIYPSMQKSVGASEKI 455
Cdd:cd18555 248 YLVINGELTLGELIAFSSLAGSFLTPIVSLINSYNQFILLKSYLERL 294
 
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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