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Conserved domains on  [gi|2468698279|ref|XP_001166911|]
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antigen peptide transporter 1 [Pan troglodytes]

Protein Classification

3a01208 family protein( domain architecture ID 11490025)

3a01208 family protein

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]
18-740 0e+00

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


:

Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 962.26  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279  18 ASLAWL-GTVLLFLADWVLLRTALPRIFSLLVPTALPLLRVWAVGLSRWAVLWLGACGVLRATVGsksenagaqGWLAAL 96
Cdd:TIGR00958   1 AALAYLlPWFSLLLVDWALLRDLLQGIFGLLLPFEKGLYVLWLEGTLRLGVLWLGALGILLNKAG---------GLLAAV 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279  97 EPLAAALGLALPVLALFRELISWGAPGSADSTRLLHWGshpsAFVVSYAAALPAAALWHKLGSLWVP-----GGQGGSGD 171
Cdd:TIGR00958  72 KPLVAALCLATPSLSSLRALAFWEALDPAVRVALGLWS----WFVWSYGAALPAAALWAVLSSAGASekeaeQGQSETAD 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 172 SVRRLLGCLGSETRRLSLFLVLVVLSSLGEMAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGDGIYNN 251
Cdd:TIGR00958 148 LLFRLLGLSGRDWPWLISAFVFLTLSSLGEMFIPFYTGRVIDTLGGDKGPPALASAIFFMCLLSIASSVSAGLRGGSFNY 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 252 TMGHVHSHLQGEVFGAVLRQETEFFQQNQTGNITSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVT 331
Cdd:TIGR00958 228 TMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTMVT 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 332 LVTLPLLFLLPKKVGKWYQLLEVQVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVN 411
Cdd:TIGR00958 308 LINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRKALAYAGY 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 412 SWTTSISGMLLKVGILYIGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKIFEYLDRTPRCPPS 491
Cdd:TIGR00958 388 LWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLDRKPNIPLT 467
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 492 GLLTPLHLEGLVQFQDVSFAYPNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQ 571
Cdd:TIGR00958 468 GTLAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQ 547
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 572 YEHRYLHRQVAAVGQEPQVFGRSLQENIAYGLTQKPtMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAV 651
Cdd:TIGR00958 548 YDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTP-DEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRI 626
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 652 ALARALIRKPCVLILDDATSALDAnsqlQVEQLLYESPELYSRSVLLITQHLSLVEQADHILFLEGGTIREGGTHQQLME 731
Cdd:TIGR00958 627 AIARALVRKPRVLILDEATSALDA----ECEQLLQESRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLME 702

                  ....*....
gi 2468698279 732 KKGCYWAMV 740
Cdd:TIGR00958 703 DQGCYKHLV 711
 
Name Accession Description Interval E-value
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
18-740 0e+00

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 962.26  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279  18 ASLAWL-GTVLLFLADWVLLRTALPRIFSLLVPTALPLLRVWAVGLSRWAVLWLGACGVLRATVGsksenagaqGWLAAL 96
Cdd:TIGR00958   1 AALAYLlPWFSLLLVDWALLRDLLQGIFGLLLPFEKGLYVLWLEGTLRLGVLWLGALGILLNKAG---------GLLAAV 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279  97 EPLAAALGLALPVLALFRELISWGAPGSADSTRLLHWGshpsAFVVSYAAALPAAALWHKLGSLWVP-----GGQGGSGD 171
Cdd:TIGR00958  72 KPLVAALCLATPSLSSLRALAFWEALDPAVRVALGLWS----WFVWSYGAALPAAALWAVLSSAGASekeaeQGQSETAD 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 172 SVRRLLGCLGSETRRLSLFLVLVVLSSLGEMAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGDGIYNN 251
Cdd:TIGR00958 148 LLFRLLGLSGRDWPWLISAFVFLTLSSLGEMFIPFYTGRVIDTLGGDKGPPALASAIFFMCLLSIASSVSAGLRGGSFNY 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 252 TMGHVHSHLQGEVFGAVLRQETEFFQQNQTGNITSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVT 331
Cdd:TIGR00958 228 TMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTMVT 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 332 LVTLPLLFLLPKKVGKWYQLLEVQVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVN 411
Cdd:TIGR00958 308 LINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRKALAYAGY 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 412 SWTTSISGMLLKVGILYIGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKIFEYLDRTPRCPPS 491
Cdd:TIGR00958 388 LWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLDRKPNIPLT 467
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 492 GLLTPLHLEGLVQFQDVSFAYPNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQ 571
Cdd:TIGR00958 468 GTLAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQ 547
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 572 YEHRYLHRQVAAVGQEPQVFGRSLQENIAYGLTQKPtMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAV 651
Cdd:TIGR00958 548 YDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTP-DEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRI 626
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 652 ALARALIRKPCVLILDDATSALDAnsqlQVEQLLYESPELYSRSVLLITQHLSLVEQADHILFLEGGTIREGGTHQQLME 731
Cdd:TIGR00958 627 AIARALVRKPRVLILDEATSALDA----ECEQLLQESRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLME 702

                  ....*....
gi 2468698279 732 KKGCYWAMV 740
Cdd:TIGR00958 703 DQGCYKHLV 711
ABC_6TM_TAP1 cd18589
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ...
200-478 1.05e-165

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: 478.89  E-value: 1.05e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 200 GEMAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQN 279
Cdd:cd18589    11 GEMAIPYYTGRMTDWIMNKDAPEAFTAAITVMSLLTIASAVSEFVCDLIYNITMSRIHSRLQGLVFAAVLRQEIAFFDSN 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 280 QTGNITSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEVQVRES 359
Cdd:cd18589    91 QTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQQSLAVQVQKS 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 360 LAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSGAV 439
Cdd:cd18589   171 LARANQVAVETFSAMKTVRSFANEEGEAQRYRQRLQKTYRLNKKEAAAYAVSMWTSSFSGLALKVGILYYGGQLVTAGTV 250
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 2468698279 440 SSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18589   251 SSGDLVTFVLYELQFTSAVEVLLSYYPSVMKAVGSSEKI 289
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
201-742 1.77e-136

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


Pssm-ID: 224055 [Multi-domain]  Cd Length: 567  Bit Score: 414.52  E-value: 1.77e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 201 EMAIPFFTGRLTDWILQDgsADTFTRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQNQ 280
Cdd:COG1132    30 SLLLPLLIGRIIDALLAD--LGELLELLLLLLLLALLGGVLRALQSYLGSRLGQKIVADLRRDLFEKLLRLPLSFFDKAK 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 281 TGNITSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEVQVRESL 360
Cdd:COG1132   108 SGDLISRLTNDVEAVSNLVSTVLVLVFTSILLLIGSLVLLFSLSWRLALILLLILPLLALVLSLLARKSRKLSRRVREAL 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 361 AKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSGAVS 440
Cdd:COG1132   188 GELNARLLESLSGIRVIKAFGAEDRELKRFEEANEELRRANLRASRLEALLAPLMLLLSSLGTVLVLALGGFLVLSGSLT 267
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 441 SGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKIFEYLDRTPRCPPSGLLTPLhLEGLVQFQDVSFAYPNRPdvLV 520
Cdd:COG1132   268 VGALAAFILYLLRLLTPILQLGEVVSLLQRASAAAERLFELLDEEPEVEDPPDPLKD-TIGSIEFENVSFSYPGKK--PV 344
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 521 LQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQENIA 600
Cdd:COG1132   345 LKDISFSIEPGEKVAIVGPSGSGKSTLIKLLLRLYDPTSGEILIDGIDIRDISLDSLRKRIGIVSQDPLLFSGTIRENIA 424
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 601 YGLTQkPTMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQ 680
Cdd:COG1132   425 LGRPD-ATDEEIEEALKLANAHEFIANLPDGYDTIVGERGVNLSGGQRQRLAIARALLRNPPILILDEATSALDTETEAL 503
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2468698279 681 VEQLLYEspELYSRSVLLITQHLSLVEQADHILFLEGGTIREGGTHQQLMEKKGCYWAMVQA 742
Cdd:COG1132   504 IQDALKK--LLKGRTTLIIAHRLSTIKNADRIIVLDNGRIVERGTHEELLAKGGLYARLYQA 563
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
254-736 3.19e-71

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 243.39  E-value: 3.19e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 254 GHVHSHLQGEVFGAVLRQETEFFQQNQTGNITSRVTEDTSTLSDSLSENLSLflwyLVRG----LCLLGIMLWGSVSLTM 329
Cdd:PRK11176   94 GKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALIT----VVREgasiIGLFIMMFYYSWQLSL 169
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 330 VTLVTLPLLFLLPKKVGKWYQLLEVQVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYA 409
Cdd:PRK11176  170 ILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRQQGMKMVSASS 249
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 410 VNSWTTSISGMLLKVGILYIGGQLVTSGAVSSGNlVTFVLYQM-QFTQAVEVLLSIYPRVQKAVGSSEKIFEYLDRTPRc 488
Cdd:PRK11176  250 ISDPIIQLIASLALAFVLYAASFPSVMDTLTAGT-ITVVFSSMiALMRPLKSLTNVNAQFQRGMAACQTLFAILDLEQE- 327
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 489 PPSGLLTPLHLEGLVQFQDVSFAYPNRpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKP 568
Cdd:PRK11176  328 KDEGKRVIERAKGDIEFRNVTFTYPGK-EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHD 406
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 569 LPQYEHRYLHRQVAAVGQEPQVFGRSLQENIAYGLTQKPTMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQR 648
Cdd:PRK11176  407 LRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQR 486
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 649 QAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPElySRSVLLITQHLSLVEQADHILFLEGGTIREGGTHQQ 728
Cdd:PRK11176  487 QRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAE 564

                  ....*...
gi 2468698279 729 LMEKKGCY 736
Cdd:PRK11176  565 LLAQNGVY 572
ABC_membrane pfam00664
ABC transporter transmembrane region; This family represents a unit of six transmembrane ...
200-458 2.04e-58

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: 395537 [Multi-domain]  Cd Length: 274  Bit Score: 199.41  E-value: 2.04e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 200 GEMAIPFFTGRLTDWILQDGSADTF--TRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQ 277
Cdd:pfam00664  14 ISPAFPLVLGRILDVLLPDGDPETQalNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLFKKILRQPMSFFD 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 278 QNQTGNITSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEVQVR 357
Cdd:pfam00664  94 TNSVGELLSRLTNDTSKIRDGLGEKLGLLFQALATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVFAKILRKLSRKEQ 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 358 ESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSG 437
Cdd:pfam00664 174 KAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYALALWFGAYLVISG 253
                         250       260
                  ....*....|....*....|.
gi 2468698279 438 AVSSGNLVTFVLYQMQFTQAV 458
Cdd:pfam00664 254 ELSVGDLVAFLSLFAQLFGPL 274
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
530-702 8.60e-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: 63.55  E-value: 8.60e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279  530 PGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLldgkplpqyehrylhrqvaavgqepqvfgrslqeniaygltqkptm 609
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVI---------------------------------------------- 34
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279  610 eeitaaaVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQ-----LQVEQL 684
Cdd:smart00382  35 -------YIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEallllLEELRL 107
                          170
                   ....*....|....*...
gi 2468698279  685 LYESPELYSRSVLLITQH 702
Cdd:smart00382 108 LLLLKSEKNLTVILTTND 125
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
503-735 2.08e-06

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 411426 [Multi-domain]  Cd Length: 907  Bit Score: 51.28  E-value: 2.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPnrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRylhrqvA 582
Cdd:NF033858    2 ARLEGVSHRYG---KTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHR------R 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 583 AVGQE----PQVFGR------SLQENIA-----YGLTQ---KPTMEEITAAavkSGAHSFISgLPQGydtevgeagsQLS 644
Cdd:NF033858   73 AVCPRiaymPQGLGKnlyptlSVFENLDffgrlFGQDAaerRRRIDELLRA---TGLAPFAD-RPAG----------KLS 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 645 GGQRQAVALARALIRKPCVLILDDATSALDANSQLQ----VEQLLYESPELysrSVLLITQHLSLVEQADHILFLEGGTI 720
Cdd:NF033858  139 GGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQfwelIDRIRAERPGM---SVLVATAYMEEAERFDWLVAMDAGRV 215
                         250
                  ....*....|....*
gi 2468698279 721 REGGTHQQLMEKKGC 735
Cdd:NF033858  216 LATGTPAELLARTGA 230
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
637-748 1.06e-05

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 48.19  E-value: 1.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 637 GEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLyESPELYSRSVLLITQHLSLVEQADHIL-FL 715
Cdd:NF000106  139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEV-RSMVRDGATVLLTTQYMEEAEQLAHELtVI 217
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2468698279 716 EGGTIREGGTHQQLMEKKGCYWAMVQaPADAPE 748
Cdd:NF000106  218 DRGRVIADGKVDELKTKVGGRTLQIR-PAHAAE 249
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
526-674 1.29e-05

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 411426 [Multi-domain]  Cd Length: 907  Bit Score: 48.58  E-value: 1.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 526 FTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPlpqyehrylhrqVAA--------VGQEPQVFgrSL-- 595
Cdd:NF033858  287 FRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQP------------VDAgdiatrrrVGYMSQAF--SLyg 352
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 596 ----QENIA-----YGLTqkptmEEITAAAVKSGAHSFisGLpqgydTEVGEA-GSQLSGGQRQAVALARALIRKPCVLI 665
Cdd:NF033858  353 eltvRQNLElharlFHLP-----AAEIAARVAEMLERF--DL-----ADVADAlPDSLPLGIRQRLSLAVAVIHKPELLI 420

                  ....*....
gi 2468698279 666 LDDATSALD 674
Cdd:NF033858  421 LDEPTSGVD 429
 
Name Accession Description Interval E-value
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
18-740 0e+00

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 962.26  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279  18 ASLAWL-GTVLLFLADWVLLRTALPRIFSLLVPTALPLLRVWAVGLSRWAVLWLGACGVLRATVGsksenagaqGWLAAL 96
Cdd:TIGR00958   1 AALAYLlPWFSLLLVDWALLRDLLQGIFGLLLPFEKGLYVLWLEGTLRLGVLWLGALGILLNKAG---------GLLAAV 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279  97 EPLAAALGLALPVLALFRELISWGAPGSADSTRLLHWGshpsAFVVSYAAALPAAALWHKLGSLWVP-----GGQGGSGD 171
Cdd:TIGR00958  72 KPLVAALCLATPSLSSLRALAFWEALDPAVRVALGLWS----WFVWSYGAALPAAALWAVLSSAGASekeaeQGQSETAD 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 172 SVRRLLGCLGSETRRLSLFLVLVVLSSLGEMAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGDGIYNN 251
Cdd:TIGR00958 148 LLFRLLGLSGRDWPWLISAFVFLTLSSLGEMFIPFYTGRVIDTLGGDKGPPALASAIFFMCLLSIASSVSAGLRGGSFNY 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 252 TMGHVHSHLQGEVFGAVLRQETEFFQQNQTGNITSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVT 331
Cdd:TIGR00958 228 TMARINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTMVT 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 332 LVTLPLLFLLPKKVGKWYQLLEVQVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVN 411
Cdd:TIGR00958 308 LINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRKALAYAGY 387
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 412 SWTTSISGMLLKVGILYIGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKIFEYLDRTPRCPPS 491
Cdd:TIGR00958 388 LWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLDRKPNIPLT 467
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 492 GLLTPLHLEGLVQFQDVSFAYPNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQ 571
Cdd:TIGR00958 468 GTLAPLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQ 547
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 572 YEHRYLHRQVAAVGQEPQVFGRSLQENIAYGLTQKPtMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAV 651
Cdd:TIGR00958 548 YDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTP-DEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRI 626
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 652 ALARALIRKPCVLILDDATSALDAnsqlQVEQLLYESPELYSRSVLLITQHLSLVEQADHILFLEGGTIREGGTHQQLME 731
Cdd:TIGR00958 627 AIARALVRKPRVLILDEATSALDA----ECEQLLQESRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLME 702

                  ....*....
gi 2468698279 732 KKGCYWAMV 740
Cdd:TIGR00958 703 DQGCYKHLV 711
ABC_6TM_TAP1 cd18589
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ...
200-478 1.05e-165

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: 478.89  E-value: 1.05e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 200 GEMAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQN 279
Cdd:cd18589    11 GEMAIPYYTGRMTDWIMNKDAPEAFTAAITVMSLLTIASAVSEFVCDLIYNITMSRIHSRLQGLVFAAVLRQEIAFFDSN 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 280 QTGNITSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEVQVRES 359
Cdd:cd18589    91 QTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQQSLAVQVQKS 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 360 LAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSGAV 439
Cdd:cd18589   171 LARANQVAVETFSAMKTVRSFANEEGEAQRYRQRLQKTYRLNKKEAAAYAVSMWTSSFSGLALKVGILYYGGQLVTAGTV 250
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 2468698279 440 SSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18589   251 SSGDLVTFVLYELQFTSAVEVLLSYYPSVMKAVGSSEKI 289
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
201-742 1.77e-136

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


Pssm-ID: 224055 [Multi-domain]  Cd Length: 567  Bit Score: 414.52  E-value: 1.77e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 201 EMAIPFFTGRLTDWILQDgsADTFTRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQNQ 280
Cdd:COG1132    30 SLLLPLLIGRIIDALLAD--LGELLELLLLLLLLALLGGVLRALQSYLGSRLGQKIVADLRRDLFEKLLRLPLSFFDKAK 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 281 TGNITSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEVQVRESL 360
Cdd:COG1132   108 SGDLISRLTNDVEAVSNLVSTVLVLVFTSILLLIGSLVLLFSLSWRLALILLLILPLLALVLSLLARKSRKLSRRVREAL 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 361 AKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSGAVS 440
Cdd:COG1132   188 GELNARLLESLSGIRVIKAFGAEDRELKRFEEANEELRRANLRASRLEALLAPLMLLLSSLGTVLVLALGGFLVLSGSLT 267
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 441 SGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKIFEYLDRTPRCPPSGLLTPLhLEGLVQFQDVSFAYPNRPdvLV 520
Cdd:COG1132   268 VGALAAFILYLLRLLTPILQLGEVVSLLQRASAAAERLFELLDEEPEVEDPPDPLKD-TIGSIEFENVSFSYPGKK--PV 344
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 521 LQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQENIA 600
Cdd:COG1132   345 LKDISFSIEPGEKVAIVGPSGSGKSTLIKLLLRLYDPTSGEILIDGIDIRDISLDSLRKRIGIVSQDPLLFSGTIRENIA 424
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 601 YGLTQkPTMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQ 680
Cdd:COG1132   425 LGRPD-ATDEEIEEALKLANAHEFIANLPDGYDTIVGERGVNLSGGQRQRLAIARALLRNPPILILDEATSALDTETEAL 503
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2468698279 681 VEQLLYEspELYSRSVLLITQHLSLVEQADHILFLEGGTIREGGTHQQLMEKKGCYWAMVQA 742
Cdd:COG1132   504 IQDALKK--LLKGRTTLIIAHRLSTIKNADRIIVLDNGRIVERGTHEELLAKGGLYARLYQA 563
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
492-720 1.56e-135

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: 399.15  E-value: 1.56e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 492 GLLTPLHLEGLVQFQDVSFAYPNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQ 571
Cdd:cd03248     1 GSLAPDHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 572 YEHRYLHRQVAAVGQEPQVFGRSLQENIAYGLTQKPtMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAV 651
Cdd:cd03248    81 YEHKYLHSKVSLVGQEPVLFARSLQDNIAYGLQSCS-FECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRV 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2468698279 652 ALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPElySRSVLLITQHLSLVEQADHILFLEGGTI 720
Cdd:cd03248   160 AIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPE--RRTVLVIAHRLSTVERADQILVLDGGRI 226
MsbA_rel TIGR02204
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ...
260-736 3.03e-106

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: 336.29  E-value: 3.03e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 260 LQGEVFGAVLRQETEFFQQNQTGNITSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLF 339
Cdd:TIGR02204  93 IRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTSLVLLAVPLVL 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 340 LLPKKVGKWYQLLEVQVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFReklQEIKTLNQKEAVAYAVNSWTTSISG 419
Cdd:TIGR02204 173 LPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFG---GAVEKAYEAARQRIRTRALLTAIVI 249
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 420 MLL---KVGILYIGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKIFEYLDRTP--RCPPSGLL 494
Cdd:TIGR02204 250 VLVfgaIVGVLWVGAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGAAERLIELLQAEPdiKAPAHPKT 329
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 495 TPLHLEGLVQFQDVSFAYPNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEH 574
Cdd:TIGR02204 330 LPVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDP 409
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 575 RYLHRQVAAVGQEPQVFGRSLQENIAYGltqKP--TMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAVA 652
Cdd:TIGR02204 410 AELRARMALVPQDPVLFAASVMENIRYG---RPdaTDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIA 486
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 653 LARALIRKPCVLILDDATSALDANSQLQVEQLLyesPELYS-RSVLLITQHLSLVEQADHILFLEGGTIREGGTHQQLME 731
Cdd:TIGR02204 487 IARAILKDAPILLLDEATSALDAESEQLVQQAL---ETLMKgRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIA 563

                  ....*
gi 2468698279 732 KKGCY 736
Cdd:TIGR02204 564 KGGLY 568
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
202-737 4.66e-105

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


Pssm-ID: 225183 [Multi-domain]  Cd Length: 709  Bit Score: 336.89  E-value: 4.66e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 202 MAIPFFTGRLTDWILQDGSADTftrnLTLMSILTIASAVLEFVGD---GIYNNTMG-HVHSHLQGEVFGAVLRQETEFFQ 277
Cdd:COG2274   171 LATPLFSQIVIDKVLPDASRST----LTVLAIGLLLAALFEALLRllrTYLIAHLGkRLDLELSGRFFRHLLRLPLSYFE 246
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 278 QNQTGNITSRVTEDTSTLSDSLSENLSLFLwYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKwyqLLEVQVR 357
Cdd:COG2274   247 KRSVGEIISRVRELEQIREFLTGSILTLII-DLLFALIFLAVMFLYSWKLTLIVLAAIPLNVLITLIFQP---LLRRKTR 322
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 358 ESLAKSSQVA---IEALSAMPTVRSFANEEGEAQKFREKLQE-IKTLNQKEAVAYAVNSWTTSISGmLLKVGILYIGGQL 433
Cdd:COG2274   323 KLIEESAEQQsflVETIKGIETVKALAAEPRFRSQWDNRLAKqVNIGFKTEKLALILNTIKSLLQQ-LSSVLILWFGAIL 401
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 434 VTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKIFEYLDRTP-RCPPSGLLTPLHLEGLVQFQDVSFAY 512
Cdd:COG2274   402 VLEGELTLGQLVAFNMLAGYFISPITRLSQLWTDFQQAKVALERLGDILDTPPeQEGDKTLIHLPKLQGEIEFENVSFRY 481
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 513 PNRpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFG 592
Cdd:COG2274   482 GPD-DPPVLEDLSLEIPPGEKVAIVGRSGSGKSTLLKLLLGLYKPQQGRILLDGVDLNDIDLASLRRQVGYVLQDPFLFS 560
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 593 RSLQENIAYGLTQkPTMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATSA 672
Cdd:COG2274   561 GSIRENIALGNPE-ATDEEIIEAAQLAGAHEFIENLPMGYDTPVGEGGANLSGGQRQRLALARALLSKPKILLLDEATSA 639
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2468698279 673 LDANSQLQVEQLLyeSPELYSRSVLLITQHLSLVEQADHILFLEGGTIREGGTHQQLMEKKGCYW 737
Cdd:COG2274   640 LDPETEAIILQNL--LQILQGRTVIIIAHRLSTIRSADRIIVLDQGKIVEQGSHEELLAQGGLYA 702
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
503-742 2.40e-99

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: 306.00  E-value: 2.40e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQVA 582
Cdd:cd03249     1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 583 AVGQEPQVFGRSLQENIAYGLTqKPTMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPC 662
Cdd:cd03249    81 LVSQEPVLFDGTIAENIRYGKP-DATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 663 VLILDDATSALDANSQLQVEQLLYESPElySRSVLLITQHLSLVEQADHILFLEGGTIREGGTHQQLMEKKGCYWAMVQA 742
Cdd:cd03249   160 ILLLDEATSALDAESEKLVQEALDRAMK--GRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKA 237
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
205-736 1.49e-96

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: 310.50  E-value: 1.49e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 205 PFFTGRLTDwILQDGSADTFTRNLTLMSILTIASAVLE----FVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQNQ 280
Cdd:TIGR02203  31 STLAALLKP-LLDDGFGGRDRSVLWWVPLVVIGLAVLRgicsFVSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQP 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 281 TGNITSRVTEDTSTLSDSLSENLSLflwyLVRG----LCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEVQV 356
Cdd:TIGR02203 110 TGTLLSRITFDSEQVASAATDAFIV----LVREtltvIGLFIVLLYYSWQLTLIVVVMLPVLSILMRRVSKRLRRISKEI 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 357 RESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTS 436
Cdd:TIGR02203 186 QNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSAGSISSPITQLIASLALAVVLFIALFQAQA 265
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 437 GAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKIFEYLDRTPRcPPSGLLTPLHLEGLVQFQDVSFAYPNRp 516
Cdd:TIGR02203 266 GSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPPE-KDTGTRAIERARGDVEFRNVTFRYPGR- 343
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 517 DVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQ 596
Cdd:TIGR02203 344 DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIA 423
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 597 ENIAYGLTQKPTMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDAN 676
Cdd:TIGR02203 424 NNIAYGRTEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNE 503
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 677 SQLQVEQLLYESPElySRSVLLITQHLSLVEQADHILFLEGGTIREGGTHQQLMEKKGCY 736
Cdd:TIGR02203 504 SERLVQAALERLMQ--GRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNGLY 561
ABC_6TM_TAP cd18572
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ...
200-478 2.78e-93

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: 292.14  E-value: 2.78e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 200 GEMAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQN 279
Cdd:cd18572    11 SELAIPHYTGAVIDAVVADGSREAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDAT 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 280 QTGNITSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEVQVRES 359
Cdd:cd18572    91 KTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRYYRKLSKEIQDA 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 360 LAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSGAV 439
Cdd:cd18572   171 LAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFYGGHLVLSGRM 250
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 2468698279 440 SSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18572   251 SAGQLVTFMLYQQQLGEAFQSLGDVFSSLMQAVGAAEKV 289
ABC_6TM_TAP_ABCB8_10_like cd18557
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ...
200-478 7.31e-85

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: 270.20  E-value: 7.31e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 200 GEMAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQN 279
Cdd:cd18557    11 AQLLLPYLIGRLIDTIIKGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLRQEIAFFDKH 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 280 QTGNITSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEVQVRES 359
Cdd:cd18557    91 KTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIRKLSKEVQDA 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 360 LAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSGAV 439
Cdd:cd18557   171 LAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWYGGYLVLSGQL 250
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 2468698279 440 SSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18557   251 TVGELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289
ABC_6TM_ABCB9_like cd18784
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ...
200-478 5.82e-77

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: 249.54  E-value: 5.82e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 200 GEMAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQN 279
Cdd:cd18784    11 GEIFIPYYTGQVIDGIVIEKSQDKFSRAIIIMGLLAIASSVAAGIRGGLFTLAMARLNIRIRNLLFRSIVSQEIGFFDTV 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 280 QTGNITSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEVQVRES 359
Cdd:cd18784    91 KTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYYKKLSKAVQDS 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 360 LAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSGAV 439
Cdd:cd18784   171 LAKANEVAEETISSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEALAYGGYVWSNELTELALTVSTLYYGGHLVITGQI 250
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 2468698279 440 SSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18784   251 SGGNLISFILYQLELGSCLESVGSVYTGLMQAVGAAEKV 289
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
503-737 3.20e-76

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: 245.60  E-value: 3.20e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPNRPDvLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQVA 582
Cdd:cd03251     1 VEFKNVTFRYPGDGP-PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 583 AVGQEPQVFGRSLQENIAYGlTQKPTMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPC 662
Cdd:cd03251    80 LVSQDVFLFNDTVAENIAYG-RPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPP 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2468698279 663 VLILDDATSALDANSQLQVEQLLYESPElySRSVLLITQHLSLVEQADHILFLEGGTIREGGTHQQLMEKKGCYW 737
Cdd:cd03251   159 ILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYA 231
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
501-734 9.41e-76

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: 244.06  E-value: 9.41e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 501 GLVQFQDVSFAYpnRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQ 580
Cdd:cd03254     1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 581 VAAVGQEPQVFGRSLQENIAYGlTQKPTMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRK 660
Cdd:cd03254    79 IGVVLQDTFLFSGTIMENIRLG-RPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRD 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2468698279 661 PCVLILDDATSALDANSQLQVEQLLYESPElySRSVLLITQHLSLVEQADHILFLEGGTIREGGTHQQLMEKKG 734
Cdd:cd03254   158 PKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
type_I_sec_HlyB TIGR01846
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ...
226-736 1.12e-75

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: 258.13  E-value: 1.12e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 226 RNLTLMSILTIAS---AVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQ----ETEFFQQNQTGNITSRVTEdTSTLSDS 298
Cdd:TIGR01846 173 RGLSTLSVLALAMlavAIFEPALGGLRTYLFAHLTSRIDVELGARLYRHllglPLGYFESRRVGDTVARVRE-LEQIRNF 251
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 299 LSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKwyqLLEVQVRESLAKSSQVA---IEALSAMP 375
Cdd:TIGR01846 252 LTGSALTVVLDLLFVVVFLAVMFFYSPTLTGVVIGSLVCYALLSVFVGP---ILRKRVEDKFERSAAATsflVESVTGIE 328
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 376 TVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSGAVSSGNLVTFVLYQMQFT 455
Cdd:TIGR01846 329 TIKATATEPQFQNRWDRQLAAYVAASFRVTNLGNIAGQAIELIQKLTFAILLWFGAHLVIGGALSPGQLVAFNMLAGRVT 408
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 456 QAVEVLLSIYPRVQKAVGSSEKIFEYLDrTPRCP-PSGLLTPLHLEGLVQFQDVSFAY-PNRPDVLvlQGLTFTLRPGEV 533
Cdd:TIGR01846 409 QPVLRLAQLWQDFQQTGIALERLGDILN-SPTEPrSAGLAALPELRGAITFENIRFRYaPDSPEVL--SNLNLDIKPGEF 485
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 534 TALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQENIAYGLTQKPtMEEIT 613
Cdd:TIGR01846 486 IGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCNPGAP-FEHVI 564
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 614 AAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPElyS 693
Cdd:TIGR01846 565 HAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICR--G 642
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|...
gi 2468698279 694 RSVLLITQHLSLVEQADHILFLEGGTIREGGTHQQLMEKKGCY 736
Cdd:TIGR01846 643 RTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLY 685
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
254-736 3.19e-71

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 243.39  E-value: 3.19e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 254 GHVHSHLQGEVFGAVLRQETEFFQQNQTGNITSRVTEDTSTLSDSLSENLSLflwyLVRG----LCLLGIMLWGSVSLTM 329
Cdd:PRK11176   94 GKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALIT----VVREgasiIGLFIMMFYYSWQLSL 169
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 330 VTLVTLPLLFLLPKKVGKWYQLLEVQVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYA 409
Cdd:PRK11176  170 ILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRQQGMKMVSASS 249
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 410 VNSWTTSISGMLLKVGILYIGGQLVTSGAVSSGNlVTFVLYQM-QFTQAVEVLLSIYPRVQKAVGSSEKIFEYLDRTPRc 488
Cdd:PRK11176  250 ISDPIIQLIASLALAFVLYAASFPSVMDTLTAGT-ITVVFSSMiALMRPLKSLTNVNAQFQRGMAACQTLFAILDLEQE- 327
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 489 PPSGLLTPLHLEGLVQFQDVSFAYPNRpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKP 568
Cdd:PRK11176  328 KDEGKRVIERAKGDIEFRNVTFTYPGK-EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHD 406
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 569 LPQYEHRYLHRQVAAVGQEPQVFGRSLQENIAYGLTQKPTMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQR 648
Cdd:PRK11176  407 LRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQR 486
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 649 QAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPElySRSVLLITQHLSLVEQADHILFLEGGTIREGGTHQQ 728
Cdd:PRK11176  487 QRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAE 564

                  ....*...
gi 2468698279 729 LMEKKGCY 736
Cdd:PRK11176  565 LLAQNGVY 572
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
503-742 6.65e-70

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: 228.65  E-value: 6.65e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAY-PNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQV 581
Cdd:cd03253     1 IEFENVTFAYdPGRP---VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 582 AAVGQEPQVFGRSLQENIAYGlTQKPTMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKP 661
Cdd:cd03253    78 GVVPQDTVLFNDTIGYNIRYG-RPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNP 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 662 CVLILDDATSALDANSqlqvEQLLYESPE--LYSRSVLLITQHLSLVEQADHILFLEGGTIREGGTHQQLMEKKGCYWAM 739
Cdd:cd03253   157 PILLLDEATSALDTHT----EREIQAALRdvSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEM 232

                  ...
gi 2468698279 740 VQA 742
Cdd:cd03253   233 WKA 235
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
175-742 3.27e-69

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 237.94  E-value: 3.27e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 175 RLLGCLGSETRRLSLFLVLVVLSSLGEMAIPFFTGRLTDWIlqdgsadtfTRNLTLMSILTIasavleFVGDGIYNnTMG 254
Cdd:PRK13657    9 RVLQYLGAEKRLGILLAVANVLLAAATFAEPILFGRIIDAI---------SGKGDIFPLLAA------WAGFGLFN-IIA 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 255 HV----------HSHLQG---EVFGAVLRQETEFFQQNQTGNITSRVTEDTSTLS----DSLSENLSLFLWYLVrglcLL 317
Cdd:PRK13657   73 GVlvarhadrlaHRRRLAvltEYFERIIQLPLAWHSQRGSGRALHTLLRGTDALFglwlEFMREHLATLVALVV----LL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 318 GIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEVQVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFReklqei 397
Cdd:PRK13657  149 PLALFMNWRLSLVLVVLGIVYTLITTLVMRKTKDGQAAVEEHYHDLFAHVSDAIGNVSVVQSYNRIEAETQALR------ 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 398 KTLNQKEAVAYAVNSW------TTSISGMLLKVGILYIGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKA 471
Cdd:PRK13657  223 DIADNLLAAQMPVLSWwalasvLNRAASTITMLAILVLGAALVQKGQLRVGEVVAFVGFATLLIGRLDQVVAFINQVFMA 302
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 472 VGSSEKIFEYLDRTP-RCPPSGLLTPLHLEGLVQFQDVSFAYPNRPDVLvlQGLTFTLRPGEVTALVGPNGSGKSTVAAL 550
Cdd:PRK13657  303 APKLEEFFEVEDAVPdVRDPPGAIDLGRVKGAVEFDDVSFSYDNSRQGV--EDVSFEAKPGQTVAIVGPTGAGKSTLINL 380
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 551 LQNLYQPTEGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQENIAYGltqKP--TMEEITAAAVKSGAHSFISGL 628
Cdd:PRK13657  381 LQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVG---RPdaTDEEMRAAAERAQAHDFIERK 457
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 629 PQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPElySRSVLLITQHLSLVEQ 708
Cdd:PRK13657  458 PDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMK--GRTTFIIAHRLSTVRN 535
                         570       580       590
                  ....*....|....*....|....*....|....
gi 2468698279 709 ADHILFLEGGTIREGGTHQQLMEKKGCYWAMVQA 742
Cdd:PRK13657  536 ADRILVFDNGRVVESGSFDELVARGGRFAALLRA 569
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
503-741 5.68e-69

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: 226.60  E-value: 5.68e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYpnRPD-VLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQV 581
Cdd:cd03252     1 ITFEHVRFRY--KPDgPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 582 AAVGQEPQVFGRSLQENIAYGlTQKPTMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKP 661
Cdd:cd03252    79 GVVLQENVLFNRSIRDNIALA-DPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNP 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 662 CVLILDDATSALDANSQLQVEQLLYESpeLYSRSVLLITQHLSLVEQADHILFLEGGTIREGGTHQQLMEKKGCYWAMVQ 741
Cdd:cd03252   158 RILIFDEATSALDYESEHAIMRNMHDI--CAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQ 235
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
503-718 4.99e-67

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: 218.79  E-value: 4.99e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPNRPdVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQVA 582
Cdd:cd03228     1 IEFKNVSFSYPGRP-KPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 583 AVGQEPQVFGRSLQENIaygltqkptmeeitaaavksgahsfisglpqgydtevgeagsqLSGGQRQAVALARALIRKPC 662
Cdd:cd03228    80 YVPQDPFLFSGTIRENI-------------------------------------------LSGGQRQRIAIARALLRDPP 116
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2468698279 663 VLILDDATSALDANSQLQVEQLLYESPElySRSVLLITQHLSLVEQADHILFLEGG 718
Cdd:cd03228   117 ILILDEATSALDPETEALILEALRALAK--GKTVIVIAHRLSTIRDADRIIVLDDG 170
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
358-739 3.87e-66

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


Pssm-ID: 227590 [Multi-domain]  Cd Length: 497  Bit Score: 227.24  E-value: 3.87e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 358 ESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAV-NSWTTSISGMLLKVgILYIGGQLVTS 436
Cdd:COG5265   116 NADSDANAKAIDSLLNFETVKYFGNEEYEAVRYDHALETYEKAAIKVHVSLLVlNFGQTAIFSTGLRV-MMTMSALGVEE 194
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 437 GAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKIFEYLDR------TPRCPPsglLTPLHLeGLVQFQDVSF 510
Cdd:COG5265   195 GQLTVGDLVNVNALLFQLSIPLNFLGFSYREIRQALTDMEKMFDLLDVeaevsdAPDAPP---LWPVRL-GAVAFINVSF 270
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 511 AY-PNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQ 589
Cdd:COG5265   271 AYdPRRP---ILNGISFTIPLGKTVAIVGESGAGKSTILRLLFRFYDVNSGSITIDGQDIRDVTQQSLRRAIGIVPQDTV 347
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 590 VFGRSLQENIAYGLTqKPTMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDA 669
Cdd:COG5265   348 LFNDTIAYNIKYGRP-DATAEEVGAAAEAAQIHDFIQSLPEGYDTGVGERGLKLSGGEKQRVAIARTILKNPPILILDEA 426
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 670 TSALDANSQLQVEQLLYESPElySRSVLLITQHLSLVEQADHILFLEGGTIREGGTHQQLMEKKGCYWAM 739
Cdd:COG5265   427 TSALDTHTEQAIQAALREVSA--GRTTLVIAHRLSTIIDADEIIVLDNGRIVERGTHEELLAAGGLYAEM 494
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
371-742 5.15e-65

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


Pssm-ID: 227321 [Multi-domain]  Cd Length: 559  Bit Score: 225.99  E-value: 5.15e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 371 LSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKeAVAYAVNS-----WTTSISGMLlkvGILYIGGQLVTSGAVSSGNLV 445
Cdd:COG4988   186 LRGLETLRAFGRTEATEERIRKDSEDFRKATMS-VLRIAFLSsavleFFAYLSIAL---VAVYIGFRLLGEGDLTLFAGL 261
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 446 TFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKIFEYLDRTPRCPPSGLLTPLHLE--GLVQFQDVSFAYPNRPdvLVLQG 523
Cdd:COG4988   262 FVLILAPEFFQPLRDLGSFFHAAAAGEAAADKLFTLLESPVATPGSGEKAEVANEppIEISLENLSFRYPDGK--PALSD 339
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 524 LTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQENIAYGl 603
Cdd:COG4988   340 LNLTIKAGQLTALVGASGAGKSTLLNLLLGFLAPTQGEIRVNGIDLRDLSPEAWRKQISWVSQNPYLFAGTIRENILLA- 418
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 604 TQKPTMEEITAAAVKSGAHSFISGlPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQ 683
Cdd:COG4988   419 RPDASDEEIIAALDQAGLLEFVPK-PDGLDTVIGEGGAGLSGGQAQRLALARALLSPASLLLLDEPTAHLDAETEQIILQ 497
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2468698279 684 LLYESPElySRSVLLITQHLSLVEQADHILFLEGGTIREGGTHQQLMEKKGCYWAMVQA 742
Cdd:COG4988   498 ALQELAK--QKTVLVITHRLEDAADADRIVVLDNGRLVEQGTHEELSEKQGLYANLLKQ 554
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
501-720 9.47e-63

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: 208.98  E-value: 9.47e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 501 GLVQFQDVSFAYPNRPdVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQ 580
Cdd:cd03245     1 GRIEFRNVSFSYPNQE-IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 581 VAAVGQEPQVFGRSLQENIAYGLtQKPTMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRK 660
Cdd:cd03245    80 IGYVPQDVTLFYGTLRDNITLGA-PLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLND 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 661 PCVLILDDATSALDANSQLQVEQLLYESPElySRSVLLITQHLSLVEQADHILFLEGGTI 720
Cdd:cd03245   159 PPILLLDEPTSAMDMNSEERLKERLRQLLG--DKTLIIITHRPSLLDLVDRIIVMDSGRI 216
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
385-741 7.09e-61

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: 227320 [Multi-domain]  Cd Length: 573  Bit Score: 214.89  E-value: 7.09e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 385 GEAQKFREKL-QEIKTLNQKEAVAYAVNSWTTSIsgMLLKVGILYIGGQLVTSGAVSSGNL-----VTFVLYQMQFTQAV 458
Cdd:COG4987   215 GAEDAYRTALeATEASWLKAQRKQARFTGLSDAI--LLLIAGLLVIGLLLWMAAQVGAGALaqpgaALALLVIFAALEAF 292
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 459 EVLLSIYP-RVQKAVGSSEKIFEYLDRTPRCPPSGLLTPlHLEGLVQFQDVSFAYPNRPdVLVLQGLTFTLRPGEVTALV 537
Cdd:COG4987   293 EPLAPGAFqHLGQVIASARRLNDILDQKPEVTFPDEQTA-TTGQALELRNVSFTYPGQQ-TKALKNFNLTLAQGEKVAIL 370
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 538 GPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQENIaygLTQKP--TMEEITAA 615
Cdd:COG4987   371 GRSGSGKSTLLQLLAGAWDPQQGSITLNGVEIASLDEQALRETISVLTQRVHLFSGTLRDNL---RLANPdaSDEELWAA 447
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 616 AVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYEspELYSRS 695
Cdd:COG4987   448 LQQVGLEKLLESAPDGLNTWLGEGGRRLSGGERRRLALARALLHDAPLWLLDEPTEGLDPITERQVLALLFE--HAEGKT 525
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 2468698279 696 VLLITQHLSLVEQADHILFLEGGTIREGGTHQQLMEKKGCYWAMVQ 741
Cdd:COG4987   526 LLMVTHRLRGLERMDRIIVLDNGKIIEEGTHAELLANNGRYKRLYQ 571
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
275-742 5.91e-60

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


Pssm-ID: 130261 [Multi-domain]  Cd Length: 708  Bit Score: 215.37  E-value: 5.91e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 275 FFQQNQTGNITSRVTeDTSTLSDSL-SENLSLFL--WYLVrglcLLGIML-WGSVSLTMVTLVTLPLLFLLPKKVGKWYQ 350
Cdd:TIGR01193 246 FFSTRRTGEIVSRFT-DASSIIDALaSTILSLFLdmWILV----IVGLFLvRQNMLLFLLSLLSIPVYAVIIILFKRTFN 320
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 351 LLEVQVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQK----FREKLQEIKTLNQKEAVAYAVNSWTTSIsgmlLKVGI 426
Cdd:TIGR01193 321 KLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEAERYSKidseFGDYLNKSFKYQKADQGQQAIKAVTKLI----LNVVI 396
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 427 LYIGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKIFEYLDRTPRCPPSGLLTPL-HLEGLVQF 505
Cdd:TIGR01193 397 LWTGAYLVMRGKLTLGQLITFNALLSYFLTPLENIINLQPKLQAARVANNRLNEVYLVDSEFINKKKRTELnNLNGDIVI 476
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 506 QDVSFAYP-NRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQVAAV 584
Cdd:TIGR01193 477 NDVSYSYGyGSN---ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYL 553
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 585 GQEPQVFGRSLQENIAYGLTQKPTMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVL 664
Cdd:TIGR01193 554 PQEPYIFSGSILENLLLGAKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVL 633
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2468698279 665 ILDDATSALDANSQLQ-VEQLLYespeLYSRSVLLITQHLSLVEQADHILFLEGGTIREGGTHQQLMEKKGCYWAMVQA 742
Cdd:TIGR01193 634 ILDESTSNLDTITEKKiVNNLLN----LQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLIHN 708
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
233-741 4.78e-59

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


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 210.34  E-value: 4.78e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 233 ILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQNQTGNITSRVTEDTSTLSDslsenlslfLWYLV- 311
Cdd:PRK10790   73 GLQLLAAGLHYAQSLLFNRAAVGVVQQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRD---------LYVTVv 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 312 ----RGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEV----QVRESLAKSSQVAIEALSAMPTVRSFANE 383
Cdd:PRK10790  144 atvlRSAALIGAMLVAMFSLDWRMALVAIMIFPAVLVVMVIYQRYSTpivrRVRAYLADINDGFNEVINGMSVIQQFRQQ 223
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 384 egeaQKFREKLQEIKTLNqkeavaYAVNSWTTSISGMLLK-----------VGILYIGGqLVTSGAVSSGNLVTFVLYQM 452
Cdd:PRK10790  224 ----ARFGERMGEASRSH------YMARMQTLRLDGFLLRpllslfsalilCGLLMLFG-FSASGTIEVGVLYAFISYLG 292
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 453 QFTQAVEVLLSIYPRVQKAVGSSEKIFEYLDRtPRCPPSGLLTPLHlEGLVQFQDVSFAYpnRPDVLVLQGLTFTLRPGE 532
Cdd:PRK10790  293 RLNEPLIELTTQQSMLQQAVVAGERVFELMDG-PRQQYGNDDRPLQ-SGRIDIDNVSFAY--RDDNLVLQNINLSVPSRG 368
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 533 VTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQENIAYGltQKPTMEEI 612
Cdd:PRK10790  369 FVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLG--RDISEEQV 446
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 613 TAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLyesPELY 692
Cdd:PRK10790  447 WQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQAL---AAVR 523
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|
gi 2468698279 693 SRSVLLITQH-LSLVEQADHILFLEGGTIREGGTHQQLMEKKGCYWAMVQ 741
Cdd:PRK10790  524 EHTTLVVIAHrLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQ 573
ABC_membrane pfam00664
ABC transporter transmembrane region; This family represents a unit of six transmembrane ...
200-458 2.04e-58

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: 395537 [Multi-domain]  Cd Length: 274  Bit Score: 199.41  E-value: 2.04e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 200 GEMAIPFFTGRLTDWILQDGSADTF--TRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQ 277
Cdd:pfam00664  14 ISPAFPLVLGRILDVLLPDGDPETQalNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLFKKILRQPMSFFD 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 278 QNQTGNITSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEVQVR 357
Cdd:pfam00664  94 TNSVGELLSRLTNDTSKIRDGLGEKLGLLFQALATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVFAKILRKLSRKEQ 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 358 ESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSG 437
Cdd:pfam00664 174 KAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYALALWFGAYLVISG 253
                         250       260
                  ....*....|....*....|.
gi 2468698279 438 AVSSGNLVTFVLYQMQFTQAV 458
Cdd:pfam00664 254 ELSVGDLVAFLSLFAQLFGPL 274
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
471-715 9.90e-54

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: 194.04  E-value: 9.90e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 471 AVGSSEKIFEYLDRTPR-CPPSGLLTPLHLEGLVqFQDVSFAYPNRPDVLvlQGLTFTLRPGEVTALVGPNGSGKSTVAA 549
Cdd:TIGR02857 290 GVAAAEALFAVLDAAPRpLAGKAPVTAAPASSLE-FSGVSVAYPGRRPAL--RPVSFTVPPGERVALVGPSGAGKSTLLN 366
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 550 LLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQENIAYGlTQKPTMEEITAAAVKSGAHSFISGLP 629
Cdd:TIGR02857 367 LLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLA-RPDASDAEIREALERAGLDEFVAALP 445
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 630 QGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSqlqvEQLLYESPELYS--RSVLLITQHLSLVE 707
Cdd:TIGR02857 446 QGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAET----EAEVLEALRALAqgRTVLLVTHRLALAA 521

                  ....*...
gi 2468698279 708 QADHILFL 715
Cdd:TIGR02857 522 LADRIVVL 529
type_I_sec_PrtD TIGR01842
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ...
420-732 4.44e-52

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


Pssm-ID: 200134 [Multi-domain]  Cd Length: 544  Bit Score: 189.87  E-value: 4.44e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 420 MLLKVGILYIGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKIFEYLDRTP-RCPPSGLLTPlh 498
Cdd:TIGR01842 236 IVLQSLVLGLGAYLAIDGEITPGMMIAGSILVGRALAPIDGAIGGWKQFSGARQAYKRLNELLANYPsRDPAMPLPEP-- 313
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 499 lEGLVQFQDVSFAYPNrPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLH 578
Cdd:TIGR01842 314 -EGHLSVENVTIVPPG-GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFG 391
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 579 RQVAAVGQEPQVFGRSLQENIAYgLTQKPTMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAVALARALI 658
Cdd:TIGR01842 392 KHIGYLPQDVELFPGTVAENIAR-FGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALY 470
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2468698279 659 RKPCVLILDDATSALDAnsqlQVEQLLYE---SPELYSRSVLLITQHLSLVEQADHILFLEGGTIREGGTHQQLMEK 732
Cdd:TIGR01842 471 GDPKLVVLDEPNSNLDE----EGEQALANaikALKARGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
270-739 4.56e-51

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


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 187.61  E-value: 4.56e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 270 RQETEFFQQNQTGNITSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIM-LWGSVSLTMVTLVTLPLLFLLPKKVGKw 348
Cdd:PRK10789   81 RQHPEFYLRHRTGDLMARATNDVDRVVFAAGEGVLTLVDSLVMGCAVLIVMsTQISWQLTLLALLPMPVMAIMIKRYGD- 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 349 yqllevQVRESLaKSSQVAI--------EALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSIS-G 419
Cdd:PRK10789  160 ------QLHERF-KLAQAAFsslndrtqESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARIDARFDPTIYIAiG 232
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 420 M--LLKVGilyiGGQ-LVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKIFEYLDRTPRCPpSGLLTP 496
Cdd:PRK10789  233 ManLLAIG----GGSwMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRIRAMLAEAPVVK-DGSEPV 307
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 497 LHLEGLVQFQDVSFAYPNRpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRY 576
Cdd:PRK10789  308 PEGRGELDVNIRQFTYPQT-DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDS 386
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 577 LHRQVAAVGQEPQVFGRSLQENIAYGltqKP--TMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAVALA 654
Cdd:PRK10789  387 WRSRLAVVSQTPFLFSDTVANNIALG---RPdaTQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIA 463
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 655 RALIRKPCVLILDDATSALDANSQLQVEQLLYESPElySRSVLLITQHLSLVEQADHILFLEGGTIREGGTHQQLMEKKG 734
Cdd:PRK10789  464 RALLLNAEILILDDALSAVDGRTEHQILHNLRQWGE--GRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSG 541

                  ....*
gi 2468698279 735 CYWAM 739
Cdd:PRK10789  542 WYRDM 546
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
385-741 4.07e-49

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 181.95  E-value: 4.07e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 385 GEAQKFREKL--QEIKTLNQKEAVAyavnswttSISGM----------LLKVGILYIGGQLVTSGAVSSGNLVTFVLYQM 452
Cdd:PRK11160  217 GAEDRYRQQLeqTEQQWLAAQRRQA--------NLTGLsqalmilangLTVVLMLWLAAGGVGGNAQPGALIALFVFAAL 288
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 453 QftqAVEVLLSI---YPRVQKAVGSSEKIFEYLDRTP--RCPPSGLLTPLHleGLVQFQDVSFAYPNRPDvLVLQGLTFT 527
Cdd:PRK11160  289 A---AFEALMPVagaFQHLGQVIASARRINEITEQKPevTFPTTSTAAADQ--VSLTLNNVSFTYPDQPQ-PVLKGLSLQ 362
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 528 LRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQENIAYGLTQKp 607
Cdd:PRK11160  363 IKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNA- 441
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 608 TMEEITAAAVKSGAHSFISGlPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYE 687
Cdd:PRK11160  442 SDEALIEVLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAE 520
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2468698279 688 SPElySRSVLLITQHLSLVEQADHILFLEGGTIREGGTHQQLMEKKGCYWAMVQ 741
Cdd:PRK11160  521 HAQ--NKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQLKQ 572
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
420-732 1.74e-47

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


Pssm-ID: 226969 [Multi-domain]  Cd Length: 580  Bit Score: 177.47  E-value: 1.74e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 420 MLLKVGILYIGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKIFEYLDRTP-RCPPSGLLTPlh 498
Cdd:COG4618   254 MALQSAVLGLGAWLVIKGEITPGMMIAGSILSGRALAPIDLAIANWKQFVAARQSYKRLNELLAELPaAAERMPLPAP-- 331
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 499 lEGLVQFQDVSFAYPNRPDVlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLH 578
Cdd:COG4618   332 -QGALSVERLTAAPPGQKKP-ILKGISFALQAGEALGIIGPSGSGKSTLARLLVGIWPPTSGSVRLDGADLRQWDREQLG 409
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 579 RQVAAVGQEPQVFGRSLQENIAYgLTQKPTMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAVALARALI 658
Cdd:COG4618   410 RHIGYLPQDVELFDGTIAENIAR-FGEEADPEKVIEAARLAGVHELILRLPQGYDTRIGEGGATLSGGQRQRIALARALY 488
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2468698279 659 RKPCVLILDDATSALDANSqlqvEQLLYES-PELYSR--SVLLITQHLSLVEQADHILFLEGGTIREGGTHQQLMEK 732
Cdd:COG4618   489 GDPFLVVLDEPNSNLDSEG----EAALAAAiLAAKARggTVVVIAHRPSALASVDKILVLQDGRIAAFGPREEVLAK 561
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
258-703 1.48e-46

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: 173.70  E-value: 1.48e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 258 SHLQGEVFGAVLRQETEFFQQNQTGNITSRVTEDTSTLSD---------------SLSENLSLFLWYLVRGLCLLGIMLW 322
Cdd:TIGR02868  86 GALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDlyvrvivpagvalvvGAAAVAAIAVLSVPAALILAAGLLL 165
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 323 GSVSLTMVTLvtlpllfllpkKVGKWYQLLEVQVRESLAkssQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQ 402
Cdd:TIGR02868 166 AGFVAPLVSL-----------RAARAAEQALARLRGELA---AQLTDALDGAAELVASGALPAALAQVEEADRELTRAER 231
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 403 KEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKIFEYL 482
Cdd:TIGR02868 232 RAAAATALGAALTLLAAGLAVLGALWAGGPAVADGRLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAAERIVEVL 311
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 483 DRTPRCP----PSGLLTPLHLEGLVqFQDVSFAYPNRPDVLvlQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPT 558
Cdd:TIGR02868 312 DAAGPVAegsaPAAGAVGLGKPTLE-LRDLSAGYPGAPPVL--DGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPL 388
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 559 EGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQENIAYGltqKP--TMEEITAAAVKSGAHSFISGLPQGYDTEV 636
Cdd:TIGR02868 389 QGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLA---RPdaTDEELWAALERVGLADWLRALPDGLDTVL 465
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2468698279 637 GEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPElySRSVLLITQHL 703
Cdd:TIGR02868 466 GEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALS--GRTVVLITHHL 530
ABC_6TM_TAP2 cd18590
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ...
200-478 1.97e-46

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: 167.13  E-value: 1.97e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 200 GEMAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQN 279
Cdd:cd18590    11 CETFIPYYTGRVIDILGGEYQHNAFTSAIGLMCLFSLGSSLSAGLRGGLFMCTLSRLNLRLRHQLFSSLVQQDIGFFEKT 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 280 QTGNITSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEVQVRES 359
Cdd:cd18590    91 KTGDLTSRLSTDTTLMSRSVALNANVLLRSLVKTLGMLGFMLSLSWQLTLLTLIEMPLTAIAQKVYNTYHQKLSQAVQDS 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 360 LAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSGAV 439
Cdd:cd18590   171 IAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTVRAVYLLVRRVLQLGVQVLMLYCGRQLIQSGHL 250
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 2468698279 440 SSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18590   251 TTGSLVSFILYQKNLGSYVRTLVYIYGDMLSNVGAAAKV 289
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
469-739 9.16e-46

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 172.72  E-value: 9.16e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 469 QKAVGSSEKIFEYLDrTPRCPPSGLLTPLHLEGLVQF--QDVSfaypnrpdVLVLQG------LTFTLRPGEVTALVGPN 540
Cdd:PRK11174  315 AQAVGAAESLVTFLE-TPLAHPQQGEKELASNDPVTIeaEDLE--------ILSPDGktlagpLNFTLPAGQRIALVGPS 385
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 541 GSGKST-VAALLQNLyqPTEGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQENIAYGltqKPTM--EEITAAAV 617
Cdd:PRK11174  386 GAGKTSlLNALLGFL--PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLG---NPDAsdEQLQQALE 460
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 618 KSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPElySRSVL 697
Cdd:PRK11174  461 NAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASR--RQTTL 538
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 2468698279 698 LITQHLSLVEQADHILFLEGGTIREGGTHQQLMEKKGCYWAM 739
Cdd:PRK11174  539 MVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATL 580
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
521-671 2.20e-45

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 as in CFTR, or belong in different polypeptide chains.


Pssm-ID: 394964 [Multi-domain]  Cd Length: 150  Bit Score: 158.97  E-value: 2.20e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 521 LQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGR-SLQENI 599
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2468698279 600 AYGLtqkpTMEEITAAAVKSGAHSFISGLPQGY--DTEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATS 671
Cdd:pfam00005  81 RLGL----LLKGLSKREKDARAEEALEKLGLGDlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
501-725 4.70e-45

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: 160.74  E-value: 4.70e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 501 GLVQFQDVSFAYpnRPD-VLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHR 579
Cdd:cd03244     1 GDIEFKNVSLRY--RPNlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 580 QVAAVGQEPQVFGRSLQENIAygltqkP----TMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAVALAR 655
Cdd:cd03244    79 RISIIPQDPVLFSGTIRSNLD------PfgeySDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLAR 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 656 ALIRKPCVLILDDATSALDANSQLQVEQLLYEspELYSRSVLLITQHLSLVEQADHILFLEGGTIREGGT 725
Cdd:cd03244   153 ALLRKSKILVLDEATASVDPETDALIQKTIRE--AFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
ABC_6TM_ABCB10_like cd18573
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ...
202-478 2.55e-43

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: 158.45  E-value: 2.55e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 202 MAIPFFTGRLTDWILQ-DGSADTFTRNLT-----LMSILTIASA-------VLEFVGDGIYNNtmghvhshLQGEVFGAV 268
Cdd:cd18573    13 MSVPFAIGKLIDVASKeSGDIEIFGLSLKtfalaLLGVFVVGAAanfgrvyLLRIAGERIVAR--------LRKRLFKSI 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 269 LRQETEFFQQNQTGNITSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKW 348
Cdd:cd18573    85 LRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRY 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 349 YQLLEVQVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILY 428
Cdd:cd18573   165 VRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLLSVLY 244
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 2468698279 429 IGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18573   245 YGGSLVASGELTVGDLTSFLMYAVYVGSSVSGLSSFYSELMKGLGASSRL 294
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
502-722 5.24e-43

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


Pssm-ID: 213224 [Multi-domain]  Cd Length: 228  Bit Score: 155.36  E-value: 5.24e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYPNRPDVL-VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGK---PLPQYEHRYL 577
Cdd:cd03257     1 LLEVKNLSVSFPTGGGSVkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKdllKLSRRLRKIR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 578 HRQVAAVGQEPQ-----VF--GRSLQENI-AYGLTQKPTMEEITAAAVKSG---AHSFISGLPQgydtevgeagsQLSGG 646
Cdd:cd03257    81 RKEIQMVFQDPMsslnpRMtiGEQIAEPLrIHGKLSKKEARKEAVLLLLVGvglPEEVLNRYPH-----------ELSGG 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2468698279 647 QRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQ-ADHILFLEGGTIRE 722
Cdd:cd03257   150 QRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKiADRVAVMYAGKIVE 226
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
233-741 1.38e-42

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 167.13  E-value: 1.38e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279  233 ILTIASAVleFVGDGI---YNNTMGH-VHSHLQGEVFGAVLRQETEFFQQ--NQTGNITSRVTEDTSTLSDSLSENLSLF 306
Cdd:PTZ00265   872 ILVIAIAM--FISETLknyYNNVIGEkVEKTMKRRLFENILYQEISFFDQdkHAPGLLSAHINRDVHLLKTGLVNNIVIF 949
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279  307 LWYLVRGL---------C-LLGIMLWGSVSLTM----VTLVTLPLLFLLPKKVGKWYQLLEVQVRESLAKSSQVAI-EAL 371
Cdd:PTZ00265   950 THFIVLFLvsmvmsfyfCpIVAAVLTGTYFIFMrvfaIRARLTANKDVEKKEINQPGTVFAYNSDDEIFKDPSFLIqEAF 1029
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279  372 SAMPTVRSFANEE------GEAQKFREKLQEIKTLnqkeavayaVNS--WTTSISGMLLKVGILY-IGGQLVTSGAVSSG 442
Cdd:PTZ00265  1030 YNMNTVIIYGLEDyfcnliEKAIDYSNKGQKRKTL---------VNSmlWGFSQSAQLFINSFAYwFGSFLIRRGTILVD 1100
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279  443 NLVTfVLYQMQFTQAVE-VLLSIYPRVQKAVGSSEKIFEYLDRTP----------RCPPSGLLtplhlEGLVQFQDVSFA 511
Cdd:PTZ00265  1101 DFMK-SLFTFLFTGSYAgKLMSLKGDSENAKLSFEKYYPLIIRKSnidvrdnggiRIKNKNDI-----KGKIEIMDVNFR 1174
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279  512 YPNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQ----------------------------------- 556
Cdd:PTZ00265  1175 YISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqdyqgdeeqnvgmkn 1254
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279  557 -------------------PTEGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQENIAYGlTQKPTMEEITAAAV 617
Cdd:PTZ00265  1255 vnefsltkeggsgedstvfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFG-KEDATREDVKRACK 1333
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279  618 KSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVL 697
Cdd:PTZ00265  1334 FAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTII 1413
                          570       580       590       600       610
                   ....*....|....*....|....*....|....*....|....*....|
gi 2468698279  698 LITQHLSLVEQADHILFLE-----GGTIREGGTHQQLME-KKGCYWAMVQ 741
Cdd:PTZ00265  1414 TIAHRIASIKRSDKIVVFNnpdrtGSFVQAHGTHEELLSvQDGVYKKYVK 1463
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
503-719 9.02e-41

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: 148.39  E-value: 9.02e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPNRPDV--LVLQGLTFTLRPGEVTALVGPNGSGKSTV-AALLQNLyQPTEGQLlldgkplpqyehrYLHR 579
Cdd:cd03250     1 ISVEDASFTWDSGEQEtsFTLKDINLEVPKGELVAIVGPVGSGKSSLlSALLGEL-EKLSGSV-------------SVPG 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 580 QVAAVGQEPQVFGRSLQENIAYGltqKPTMEE-----ITAAAVKSGahsfISGLPQGYDTEVGEAGSQLSGGQRQAVALA 654
Cdd:cd03250    67 SIAYVSQEPWIQNGTIRENILFG---KPFDEEryekvIKACALEPD----LEILPDGDLTEIGEKGINLSGGQKQRISLA 139
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2468698279 655 RALIRKPCVLILDDATSALDAnsqlQVEQLLYES----PELYSRSVLLITQHLSLVEQADHILFLEGGT 719
Cdd:cd03250   140 RAVYSDADIYLLDDPLSAVDA----HVGRHIFENcilgLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
504-719 2.36e-40

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: 147.23  E-value: 2.36e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 504 QFQDVSFAYPNRpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQVAA 583
Cdd:cd03225     1 ELKNLSFSYPDG-ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 584 VGQEP--QVFGRSLQENIAYGLTQ----KPTMEEITAAAVKsgahsfisglpqgydtEVGEAG------SQLSGGQRQAV 651
Cdd:cd03225    80 VFQNPddQFFGPTVEEEVAFGLENlglpEEEIEERVEEALE----------------LVGLEGlrdrspFTLSGGQKQRV 143
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2468698279 652 ALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELySRSVLLITQHLSLV-EQADHILFLEGGT 719
Cdd:cd03225   144 AIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLlELADRVIVLEDGK 211
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
502-732 6.08e-40

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


Pssm-ID: 224054 [Multi-domain]  Cd Length: 293  Bit Score: 148.99  E-value: 6.08e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYPNrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQyEHRYLHRQV 581
Cdd:COG1131     4 VIEVRNLTKKYGG--DKTALDGVSFEVEPGEIFGLLGPNGAGKTTLLKILAGLLKPTSGEILVLGYDVVK-EPAKVRRRI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 582 AAVGQEPQVFGR-SLQENI-----AYGLTQKPTMEEITAAAvksgahsFISGLPQGYDTEVgeagSQLSGGQRQAVALAR 655
Cdd:COG1131    81 GYVPQEPSLYPElTVRENLeffarLYGLSKEEAEERIEELL-------ELFGLEDKANKKV----RTLSGGMKQRLSIAL 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2468698279 656 ALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQ-ADHILFLEGGTIREGGTHQQLMEK 732
Cdd:COG1131   150 ALLHDPELLILDEPTSGLDPESRREIWELLRELAKEGGVTILLSTHILEEAEElCDRVIILNDGKIIAEGTPEELKEK 227
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
502-729 9.43e-40

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


Pssm-ID: 224045 [Multi-domain]  Cd Length: 258  Bit Score: 147.32  E-value: 9.43e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQV 581
Cdd:COG1120     2 MLEVENLSFGYGGKP---ILDDLSFSIPKGEITGILGPNGSGKSTLLKCLAGLLKPKSGEVLLDGKDIASLSPKELAKKL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 582 AAVGQEPQV-FGRSLQENIAYGLTQKPTM---------EEITAAAVKSGAHSFIsglpqgyDTEVGEagsqLSGGQRQAV 651
Cdd:COG1120    79 AYVPQSPSApFGLTVYELVLLGRYPHLGLfgrpskedeEIVEEALELLGLEHLA-------DRPVDE----LSGGERQRV 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 652 ALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQ-ADHILFLEGGTI-REGGTHQQL 729
Cdd:COG1120   148 LIARALAQETPILLLDEPTSHLDIAHQIEVLELLRDLNREKGLTVVMVLHDLNLAARyADHLILLKDGKIvAQGTPEEVL 227
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
502-733 1.84e-39

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


Pssm-ID: 224047 [Multi-domain]  Cd Length: 235  Bit Score: 145.48  E-value: 1.84e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYPNRpdVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPL-PQYEHRYLHRQ 580
Cdd:COG1122     3 MIEAENLSFRYPGR--KAALKDVSLEIEKGERVLLIGPNGSGKSTLLKLLNGLLKPTSGEVLVDGLDTsSEKSLLELRQK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 581 VAAVGQEP--QVFGRSLQENIAYGLTQKPTMEEITAAAVKSGAHSFisGLPQGYDTEVgeagSQLSGGQRQAVALARALI 658
Cdd:COG1122    81 VGLVFQNPddQLFGPTVEDEVAFGLENLGLPREEIEERVAEALELV--GLEELLDRPP----FNLSGGQKQRVAIAGVLA 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2468698279 659 RKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQ-ADHILFLEGGTIREGGTHQQLMEKK 733
Cdd:COG1122   155 MGPEILLLDEPTAGLDPKGRRELLELLKKLKEEGGKTIIIVTHDLELVLEyADRVVVLDDGKILADGDPAEIFNDA 230
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
503-722 1.26e-38

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: 142.61  E-value: 1.26e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPNR-PDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQyehryLHRQV 581
Cdd:cd03293     1 LEVRNVSKTYGGGgGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG-----PGPDR 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 582 AAVGQEPQVFG-RSLQENIAYGLtqkpTMEEITAAAVKSGAHSFISglpqgydtEVGEAG------SQLSGGQRQAVALA 654
Cdd:cd03293    76 GYVFQQDALLPwLTVLDNVALGL----ELQGVPKAEARERAEELLE--------LVGLSGfenaypHQLSGGMRQRVALA 143
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2468698279 655 RALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITqHlSLVEQ---ADHILFLEG--GTIRE 722
Cdd:cd03293   144 RALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVT-H-DIDEAvflADRVVVLSArpGRIVA 214
ABC_6TM_exporters cd07346
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ...
201-478 1.70e-38

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: 144.62  E-value: 1.70e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 201 EMAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQNQ 280
Cdd:cd07346    15 GLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQRLSLSFFDRNR 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 281 TGNITSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEVQVRESL 360
Cdd:cd07346    95 TGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRRRIRKASREVRESL 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 361 AKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSGAVS 440
Cdd:cd07346   175 AELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALVLLYGGYLVLQGSLT 254
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 2468698279 441 SGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd07346   255 IGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
503-724 2.06e-38

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: 140.53  E-value: 2.06e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPNRpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRyLHRQVA 582
Cdd:cd03247     1 LSINNVSFSYPEQ-EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-LSSLIS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 583 AVGQEPQVFGRSLQENIaygltqkptmeeitaaavksgahsfisglpqgydtevgeaGSQLSGGQRQAVALARALIRKPC 662
Cdd:cd03247    79 VLNQRPYLFDTTLRNNL----------------------------------------GRRFSGGERQRLALARILLQDAP 118
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2468698279 663 VLILDDATSALDANSQLQVEQLLYEspELYSRSVLLITQHLSLVEQADHILFLEGGTIREGG 724
Cdd:cd03247   119 IVLLDEPTVGLDPITERQLLSLIFE--VLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
506-720 2.09e-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: 2.09e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 506 QDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQVAAVg 585
Cdd:cd03214     3 ENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYV- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 586 qePQVfgrslqeniaygltqkptMEEITAAAVksgAHSFIsglpqgydtevgeagSQLSGGQRQAVALARALIRKPCVLI 665
Cdd:cd03214    79 --PQA------------------LELLGLAHL---ADRPF---------------NELSGGERQRVLLARALAQEPPILL 120
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2468698279 666 LDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQ-ADHILFLEGGTI 720
Cdd:cd03214   121 LDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARyADRVILLKDGRI 176
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
504-720 1.90e-37

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: 137.73  E-value: 1.90e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 504 QFQDVSFAYPNRpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQVAA 583
Cdd:cd03246     2 EVENVSFRYPGA-EPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 584 VGQEPQVFGRSLQENIaygltqkptmeeitaaavksgahsfisglpqgydtevgeagsqLSGGQRQAVALARALIRKPCV 663
Cdd:cd03246    81 LPQDDELFSGSIAENI-------------------------------------------LSGGQRQRLGLARALYGNPRI 117
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 664 LILDDATSALDansqLQVEQLLYE---SPELYSRSVLLITQHLSLVEQADHILFLEGGTI 720
Cdd:cd03246   118 LVLDEPNSHLD----VEGERALNQaiaALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
PLN03232 PLN03232
ABC transporter C family member; Provisional
255-746 2.03e-37

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 151.28  E-value: 2.03e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279  255 HVHSHLQGEVFGAVLRQETEFFQQNQTGNITSRVTEDTSTLSDSLSENLSLF---LWYLVRGLCLLG----IMLWGSVSL 327
Cdd:PLN03232   980 HAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFmnqLWQLLSTFALIGtvstISLWAIMPL 1059
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279  328 TMVTLVTLPllfllpkkvgkWYQLLEVQVR--ESLAKSSQVAI--EALSAMPTVRSFaneegeaqKFREKLQEIKTLNQK 403
Cdd:PLN03232  1060 LILFYAAYL-----------YYQSTSREVRrlDSVTRSPIYAQfgEALNGLSSIRAY--------KAYDRMAKINGKSMD 1120
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279  404 EAVAYAV-----NSWTT----SISGMLL----KVGILYIGGQLVTSGAVSSGNLVtfVLYQMQFTQAVEVLLSIYPRVQK 470
Cdd:PLN03232  1121 NNIRFTLantssNRWLTirleTLGGVMIwltaTFAVLRNGNAENQAGFASTMGLL--LSYTLNITTLLSGVLRQASKAEN 1198
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279  471 AVGSSEKIFEYLDRTPRC--------PPSGLltplHLEGLVQFQDVSFAYpnRPDVL-VLQGLTFTLRPGEVTALVGPNG 541
Cdd:PLN03232  1199 SLNSVERVGNYIDLPSEAtaiiennrPVSGW----PSRGSIKFEDVHLRY--RPGLPpVLHGLSFFVSPSEKVGVVGRTG 1272
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279  542 SGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQENIaygltqKPTMEEITA----AAV 617
Cdd:PLN03232  1273 AGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNI------DPFSEHNDAdlweALE 1346
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279  618 KSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYEspELYSRSVL 697
Cdd:PLN03232  1347 RAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIRE--EFKSCTML 1424
                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2468698279  698 LITQHLSLVEQADHILFLEGGTIREGGTHQQLMEKKG-CYWAMVQA--PADA 746
Cdd:PLN03232  1425 VIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTsAFFRMVHStgPANA 1476
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
503-729 5.51e-37

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: 138.47  E-value: 5.51e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPnrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLY-----QPTEGQLLLDGKPL--PQYEHR 575
Cdd:cd03260     1 IELRDLNVYYG---DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIydLDVDVL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 576 YLHRQVAAVGQEPQVFGRSLQENIAYGLT-----QKPTMEEITAAAVKsgahsfISGLPQgydtEVGE--AGSQLSGGQR 648
Cdd:cd03260    78 ELRRRVGMVFQKPNPFPGSIYDNVAYGLRlhgikLKEELDERVEEALR------KAALWD----EVKDrlHALGLSGGQQ 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 649 QAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYsrSVLLITQHLslvEQA----DHILFLEGGTIREGG 724
Cdd:cd03260   148 QRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHNM---QQAarvaDRTAFLLNGRLVEFG 222

                  ....*
gi 2468698279 725 THQQL 729
Cdd:cd03260   223 PTEQI 227
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
504-719 6.59e-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: 6.59e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 504 QFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQVAA 583
Cdd:cd00267     1 EIENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 584 VgqepqvfgrslqeniaygltqkptmeeitaaavksgahsfisglpqgydtevgeagSQLSGGQRQAVALARALIRKPCV 663
Cdd:cd00267    78 V--------------------------------------------------------PQLSGGQRQRVALARALLLNPDL 101
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2468698279 664 LILDDATSALDANSQLQVEQLLYESPELySRSVLLITQHLSLVEQA-DHILFLEGGT 719
Cdd:cd00267   102 LLLDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAaDRVIVLKDGK 157
ABC_6TM_AtABCB27_like cd18780
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ...
202-478 1.14e-36

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: 139.69  E-value: 1.14e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 202 MAIPFFTGRLTDWILQDGSADTFT-RNLTLMSILTIasaVLEFVGDGIYN-------NTMGH-VHSHLQGEVFGAVLRQE 272
Cdd:cd18780    13 LALPYFFGQVIDAVTNHSGSGGEEaLRALNQAVLIL---LGVVLIGSIATflrswlfTLAGErVVARLRKRLFSAIIAQE 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 273 TEFFQQNQTGNITSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLL 352
Cdd:cd18780    90 IAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAVIYGKYVRKL 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 353 EVQVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQ 432
Cdd:cd18780   170 SKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQLAIVLVLWYGGR 249
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 2468698279 433 LVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18780   250 LVIDGELTTGLLTSFLLYTLTVAMSFAFLSSLYGDFMQAVGASVRV 295
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
369-740 1.41e-36

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 148.64  E-value: 1.41e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279  369 EALSAMPTVRSFANEEGEAQKFR--EKLQEIKTL--NQKEAVAYAVnswttsISGMLL---KVGILYiGGQLVTSGAVSS 441
Cdd:PTZ00265   241 EALVGIRTVVSYCGEKTILKKFNlsEKLYSKYILkaNFMESLHIGM------INGFILasyAFGFWY-GTRIIISDLSNQ 313
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279  442 --------GNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKIFEYLDRTPRCPPSGLLTPLHLEGLVQFQDVSFAYP 513
Cdd:PTZ00265   314 qpnndfhgGSVISILLGVLISMFMLTIILPNITEYMKSLEATNSLYEIINRKPLVENNDDGKKLKDIKKIQFKNVRFHYD 393
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279  514 NRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLL-DGKPLPQYEHRYLHRQVAAVGQEPQVFG 592
Cdd:PTZ00265   394 TRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFS 473
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279  593 RSLQENIAYGLTQKPTME--------------------------------------------------------EITAAA 616
Cdd:PTZ00265   474 NSIKNNIKYSLYSLKDLEalsnyynedgndsqenknkrnscrakcagdlndmsnttdsneliemrknyqtikdsEVVDVS 553
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279  617 VKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSV 696
Cdd:PTZ00265   554 KKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRIT 633
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279  697 LLITQHLSLVEQADHILFL-----------------------------------------------EGGTIREGGTHQQL 729
Cdd:PTZ00265   634 IIIAHRLSTIRYANTIFVLsnrergstvdvdiigedptkdnkennnknnkddnnnnnnnnnnkinnAGSYIIEQGTHDAL 713
                          490
                   ....*....|..
gi 2468698279  730 ME-KKGCYWAMV 740
Cdd:PTZ00265   714 MKnKNGIYYTMI 725
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
502-731 1.58e-36

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


Pssm-ID: 224049 [Multi-domain]  Cd Length: 252  Bit Score: 137.78  E-value: 1.58e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYPNRPDVL-VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEH-RYLHR 579
Cdd:COG1124     3 LLSVRNLSIVYGGGKFAFhALNNVSLEIERGETLGIVGESGSGKSTLARLLAGLEKPSSGSILLDGKPLAPKKRaKAFYR 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 580 QVAAVGQEP-------QVFGRSLQENIAYGLTQKPTMEEITAAavksgaHSFisGLPQGYDTEvgeAGSQLSGGQRQAVA 652
Cdd:COG1124    83 PVQMVFQDPysslnprRTVGRILSEPLRPHGLSKSQQRIAELL------DQV--GLPPSFLDR---RPHELSGGQRQRIA 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 653 LARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQ-ADHILFLEGGTIREGGTHQQLME 731
Cdd:COG1124   152 IARALIPEPKLLILDEPTSALDVSVQAQILNLLLELKKERGLTYLFISHDLALVEHmCDRIAVMDNGQIVEIGPTEELLS 231
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
268-741 3.97e-36

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: 147.01  E-value: 3.97e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279  268 VLRQETEFFQQNQTGNITSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLlpkkVGK 347
Cdd:TIGR00957 1048 KLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIAAVIIPPLGLLYFF----VQR 1123
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279  348 WYQLLEVQVR--ESLAKSSQVA--IEALSAMPTVRSFANEEGEAQKFREKLQEiktlNQKEAVAYAV-NSWttsisgmlL 422
Cdd:TIGR00957 1124 FYVASSRQLKrlESVSRSPVYShfNETLLGVSVIRAFEEQERFIHQSDLKVDE----NQKAYYPSIVaNRW--------L 1191
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279  423 KVGILYIGGQLVTSGAV---------SSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKIFEYLDRTPRCP---- 489
Cdd:TIGR00957 1192 AVRLECVGNCIVLFAALfavisrhslSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPwqiq 1271
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279  490 ----PSGLLTplhlEGLVQFQDVSFAYpnRPDV-LVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLL 564
Cdd:TIGR00957 1272 etapPSGWPP----RGRVEFRNYCLRY--REDLdLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIII 1345
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279  565 DGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQENI-AYGltqKPTMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQL 643
Cdd:TIGR00957 1346 DGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLdPFS---QYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENL 1422
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279  644 SGGQRQAVALARALIRKPCVLILDDATSALDansqLQVEQLLYES--PELYSRSVLLITQHLSLVEQADHILFLEGGTIR 721
Cdd:TIGR00957 1423 SVGQRQLVCLARALLRKTKILVLDEATAAVD----LETDNLIQSTirTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVA 1498
                          490       500
                   ....*....|....*....|
gi 2468698279  722 EGGTHQQLMEKKGCYWAMVQ 741
Cdd:TIGR00957 1499 EFGAPSNLLQQRGIFYSMAK 1518
ABC_6TM_bac_exporter_ABCB8_10_like cd18576
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ...
202-478 9.62e-36

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: 136.84  E-value: 9.62e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 202 MAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQNQT 281
Cdd:cd18576    13 LVFPLLAGQLIDAALGGGDTASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQRLPLSFFHERRV 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 282 GNITSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEVQVRESLA 361
Cdd:cd18576    93 GELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFGRRIRKLSKKVQDELA 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 362 KSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSGAVSS 441
Cdd:cd18576   173 EANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAIVAVLWYGGRLVLAGELTA 252
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 2468698279 442 GNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18576   253 GDLVAFLLYTLFIAGSIGSLADLYGQLQKALGASERV 289
ECF_ATPase_1 TIGR04520
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
503-733 8.92e-35

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: 133.32  E-value: 8.92e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPNRpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDG-KPLPQYEHRYLHRQV 581
Cdd:TIGR04520   1 IEVENVSFSYPES-EKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGlDTLDEENLWEIRKKV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 582 AAVGQEP--QVFGRSLQENIAYGLTQK----PTMEEITAAAVKS-GAHSFISGLPQgydtevgeagsQLSGGQRQAVALA 654
Cdd:TIGR04520  80 GMVFQNPdnQFVGATVEDDVAFGLENLgvprEEMRKRVDEALKLvGMEDFRDREPH-----------LLSGGQKQRVAIA 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2468698279 655 RALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQADHILFLEGGTIREGGTHQQLMEKK 733
Cdd:TIGR04520 149 GVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPREIFSQV 227
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
503-720 1.01e-34

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: 129.83  E-value: 1.01e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLhRQVA 582
Cdd:cd03230     1 IEVRNLSKRYGKKT---ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVK-RRIG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 583 AVGQEPQVFGR-SLQENIaygltqkptmeeitaaavksgahsfisglpqgydtevgeagsQLSGGQRQAVALARALIRKP 661
Cdd:cd03230    77 YLPEEPSLYENlTVRENL------------------------------------------KLSGGMKQRLALAQALLHDP 114
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2468698279 662 CVLILDDATSALDANSQLQVEQLLYEspelYS---RSVLLITQHLSLVEQ-ADHILFLEGGTI 720
Cdd:cd03230   115 ELLILDEPTSGLDPESRREFWELLRE----LKkegKTILLSSHILEEAERlCDRVAILNNGRI 173
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
484-731 1.60e-34

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


Pssm-ID: 224048 [Multi-domain]  Cd Length: 539  Bit Score: 138.86  E-value: 1.60e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 484 RTPRCPPSGLLTPLHLEGLVQFQDVSFAYPNRPD--------VLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLY 555
Cdd:COG1123   262 GDEKIIRLPRRGPLRAEPLLSVRNLSKRYGSRKGlfvrergeVKAVDDVSFDLREGETLGLVGESGSGKSTLARILAGLL 341
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 556 QPTEGQLLLDGKPLPQYEHRY--LHRQVAAVGQEPQVF---GRSLQENIA-----YGLTQKPTMEEITAAAVKsgahsfI 625
Cdd:COG1123   342 PPSSGSIIFDGQDLDLTGGELrrLRRRIQMVFQDPYSSlnpRMTVGDILAeplriHGGGSGAERRARVAELLE------L 415
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 626 SGLPQGYdtevgeAGS---QLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQH 702
Cdd:COG1123   416 VGLPPEF------LDRyphELSGGQRQRVAIARALALEPKLLILDEPVSALDVSVQAQVLNLLKDLQEELGLTYLFISHD 489
                         250       260       270
                  ....*....|....*....|....*....|
gi 2468698279 703 LSLVEQ-ADHILFLEGGTIREGGTHQQLME 731
Cdd:COG1123   490 LAVVRYiADRVAVMYDGRIVEEGPTEKVFE 519
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
502-725 3.08e-34

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


Pssm-ID: 224058 [Multi-domain]  Cd Length: 339  Bit Score: 133.91  E-value: 3.08e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYPNR--PDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGK---PLPQYEHRY 576
Cdd:COG1135     1 MIELENVSKTFGQTgtGTVTALDDVSLEIPKGEIFGIIGYSGAGKSTLLRLINLLERPTSGSVFVDGQdltALSEAELRQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 577 LHRQVAAVGQEPQVFG-RSLQENIAYGL-TQKPTMEEItAAAVKSGAHsfISGLPqgydtevGEAG---SQLSGGQRQAV 651
Cdd:COG1135    81 LRQKIGMIFQHFNLLSsRTVFENVAFPLeLAGVPKAEI-KQRVAELLE--LVGLS-------DKADrypAQLSGGQKQRV 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2468698279 652 ALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQ-ADHILFLEGGTIREGGT 725
Cdd:COG1135   151 AIARALANNPKILLCDEATSALDPETTQSILELLKDINRELGLTIVLITHEMEVVKRiCDRVAVLDQGRLVEEGT 225
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
503-720 9.75e-34

ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and cell division protein; 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. An FtsE null mutants showed filamentous growth and appeared viable on high salt medium only, indicating a role for FtsE in cell division and/or salt transport. 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: 128.76  E-value: 9.75e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPNRPD-VLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHR----YL 577
Cdd:cd03255     1 IELKNLSKTYGGGGEkVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKelaaFR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 578 HRQVAAVGQEPQVFGR-SLQENIAYGL----TQKPTMEEITAAAVKSgahsfiSGLPQGYDTEVgeagSQLSGGQRQAVA 652
Cdd:cd03255    81 RRHIGFVFQSFNLLPDlTALENVELPLllagVPKKERRERAEELLER------VGLGDRLNHYP----SELSGGQQQRVA 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2468698279 653 LARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQADHILFLEGGTI 720
Cdd:cd03255   151 IARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase components [Amino acid transport ...
501-725 1.87e-33

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


Pssm-ID: 226361 [Multi-domain]  Cd Length: 352  Bit Score: 132.02  E-value: 1.87e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 501 GLVQFQDVSFAYPnrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKP---LPQYEhryl 577
Cdd:COG3842     4 PALEIRNVSKSFG---DFTAVDDISLDIKKGEFVTLLGPSGCGKTTLLRMIAGFEQPSSGEILLDGEDitdVPPEK---- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 578 hRQVAAVGQEPQVFG-RSLQENIAYGL--TQKPTMEEITAAAVKsgAHSFIsGLPQGYDTEVgeagSQLSGGQRQAVALA 654
Cdd:COG3842    77 -RPIGMVFQSYALFPhMTVEENVAFGLkvRKKLKKAEIKARVEE--ALELV-GLEGFADRKP----HQLSGGQQQRVALA 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 655 RALIRKPCVLILDDATSALDAN--SQLQVEQLlyespELYSR---SVLLITQH----LSLveqADHILFLEGGTIREGGT 725
Cdd:COG3842   149 RALVPEPKVLLLDEPLSALDAKlrEQMRKELK-----ELQRElgiTFVYVTHDqeeaLAM---SDRIAVMNDGRIEQVGT 220
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
502-722 6.36e-33

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


Pssm-ID: 224041 [Multi-domain]  Cd Length: 248  Bit Score: 127.29  E-value: 6.36e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYehrylHRQV 581
Cdd:COG1116     3 LLEIEGVSKSFGGVE---VLEDINLSVEKGEFVAILGPSGCGKSTLLRLIAGLEKPTSGEVLLDGRPVTGP-----GPDI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 582 AAVGQEPQVFG-RSLQENIAYGLTQ----KPTMEEITAAAVKsgahsfisglpqgydtEVGEAG------SQLSGGQRQA 650
Cdd:COG1116    75 GYVFQEDALLPwLTVLDNVALGLELrgksKAEARERAKELLE----------------LVGLAGfedkypHQLSGGMRQR 138
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2468698279 651 VALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITqHlSLVEQ---ADHILFLEG--GTIRE 722
Cdd:COG1116   139 VAIARALATRPKLLLLDEPFGALDALTREELQDELLRLWEETRKTVLLVT-H-DVDEAvylADRVVVLSNrpGRIGE 213
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
503-720 1.50e-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: 125.32  E-value: 1.50e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPnrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKP---LPQYEhrylhR 579
Cdd:cd03259     1 LELKGLSKTYG---SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDvtgVPPER-----R 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 580 QVAAVGQEPQVF-GRSLQENIAYGLTQKPTMEEITAAAVKSGAHSF-ISGLPQGYDtevgeagSQLSGGQRQAVALARAL 657
Cdd:cd03259    73 NIGMVFQDYALFpHLTVAENIAFGLKLRGVPKAEIRARVRELLELVgLEGLLNRYP-------HELSGGQQQRVALARAL 145
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2468698279 658 IRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLS-LVEQADHILFLEGGTI 720
Cdd:cd03259   146 AREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEeALALADRIAVMNEGRI 209
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
502-722 1.64e-32

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


Pssm-ID: 224059 [Multi-domain]  Cd Length: 226  Bit Score: 125.31  E-value: 1.64e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYPNRP-DVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLH-- 578
Cdd:COG1136     1 MIELKNVSKIYGLGGeKVEALKDVNLEIEAGEFVAIVGPSGSGKSTLLNLLGGLDKPTSGEVLINGKDLTKLSEKELAkl 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 579 -RQvaAVGQEPQVFG----RSLQENIAYGLT-----QKPTMEEITAAAVKSG-AHSFISGLPqgydtevgeagSQLSGGQ 647
Cdd:COG1136    81 rRK--KIGFVFQNFNllpdLTVLENVELPLLiagksAGRRKRAAEELLEVLGlEDRLLKKKP-----------SELSGGQ 147
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2468698279 648 RQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQADHILFLEGGTIRE 722
Cdd:COG1136   148 QQRVAIARALINNPKIILADEPTGNLDSKTAKEVLELLRELNKERGKTIIMVTHDPELAKYADRVIELKDGKIEE 222
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
503-719 2.92e-32

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: 123.07  E-value: 2.92e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPnrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYE--HRYLHRQ 580
Cdd:cd03229     1 LELKNVSKRYG---QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 581 VAAVGQEPQVF-GRSLQENIAYGltqkptmeeitaaavksgahsfisglpqgydtevgeagsqLSGGQRQAVALARALIR 659
Cdd:cd03229    78 IGMVFQDFALFpHLTVLENIALG----------------------------------------LSGGQQQRVALARALAM 117
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2468698279 660 KPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQ-ADHILFLEGGT 719
Cdd:cd03229   118 DPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
500-731 5.60e-32

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 125.51  E-value: 5.60e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 500 EGLVQFQDVSFAYPNRPDvLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHR 579
Cdd:PRK13635    3 EEIIRVEHISFRYPDAAT-YALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 580 QVAAVGQEP--QVFGRSLQENIAYGLTQ----KPTMEEITAAAVKS-GAHSFISGLPqgydtevgeagSQLSGGQRQAVA 652
Cdd:PRK13635   82 QVGMVFQNPdnQFVGATVQDDVAFGLENigvpREEMVERVDQALRQvGMEDFLNREP-----------HRLSGGQKQRVA 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2468698279 653 LARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQADHILFLEGGTIREGGTHQQLME 731
Cdd:PRK13635  151 IAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFK 229
MalK COG3839
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
503-732 6.56e-32

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


Pssm-ID: 226359 [Multi-domain]  Cd Length: 338  Bit Score: 126.99  E-value: 6.56e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPNrpdVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPL----PQyehrylH 578
Cdd:COG3839     4 LELKNVRKSFGS---FEVLKDVNLDIEDGEFVVLLGPSGCGKSTLLRMIAGLEEPTSGEILIDGRDVtdlpPE------K 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 579 RQVAAVGQEPQVFGR-SLQENIAYGLTQKPTMEEITAAAVK-----SGAHSFISGLPqgydtevgeagSQLSGGQRQAVA 652
Cdd:COG3839    75 RGIAMVFQNYALYPHmTVYENIAFGLKLRGVPKAEIDKRVKevaklLGLEHLLNRKP-----------LQLSGGQRQRVA 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 653 LARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQhlSLVEQ---ADHILFLEGGTIREGGTHQQL 729
Cdd:COG3839   144 LARALVRKPKVFLLDEPLSNLDAKLRVLMRSEIKKLHERLGTTTIYVTH--DQVEAmtlADRIVVMNDGRIQQVGTPLEL 221

                  ...
gi 2468698279 730 MEK 732
Cdd:COG3839   222 YER 224
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
502-727 9.40e-32

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


Pssm-ID: 224046 [Multi-domain]  Cd Length: 254  Bit Score: 124.26  E-value: 9.40e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQyeHRYLHRqv 581
Cdd:COG1121     4 MIEVENLTVSYGNRP---VLEDISLSVEKGEITALIGPNGAGKSTLLKAILGLLKPSSGEIKIFGKPVRK--RRKRLR-- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 582 aaVGQEPQvfgrslQENIAYGLtqkP-TMEEItaaaVKSGAHS---FISGLPQGYDTEVGEA----G---------SQLS 644
Cdd:COG1121    77 --IGYVPQ------KSSVDRSF---PiTVKDV----VLLGRYGkkgWFRRLNKKDKEKVDEAlervGmedlrdrqiGELS 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 645 GGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPElYSRSVLLITQHLSLVEQ-ADHILFLEGGTIREG 723
Cdd:COG1121   142 GGQKQRVLLARALAQNPDLLLLDEPFTGVDVAGQKEIYDLLKELRQ-EGKTVLMVTHDLGLVMAyFDRVICLNRHLIASG 220

                  ....
gi 2468698279 724 GTHQ 727
Cdd:COG1121   221 PPEE 224
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
516-732 9.90e-32

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


Pssm-ID: 224043 [Multi-domain]  Cd Length: 345  Bit Score: 126.70  E-value: 9.90e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 516 PDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLH-RQVAAVGQEPQVFGR- 593
Cdd:COG1118    13 GAFGALDDISLDIKSGELVALLGPSGAGKSTLLRIIAGLETPDAGRIRLNGRVLFDVSNLAVRdRKVGFVFQHYALFPHm 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 594 SLQENIAYGLTQKPTMEEitAAAVKSGAHSFI-----SGLPQGYDtevgeagSQLSGGQRQAVALARALIRKPCVLILDD 668
Cdd:COG1118    93 TVADNIAFGLKVRKERPS--EAEIRARVEELLrlvqlEGLADRYP-------AQLSGGQRQRVALARALAVEPKVLLLDE 163
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2468698279 669 ATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLV-EQADHILFLEGGTIREGGTHQQLMEK 732
Cdd:COG1118   164 PFGALDAKVRKELRRWLRKLHDRLGVTTVFVTHDQEEAlELADRVVVLNQGRIEQVGPPDEVYDH 228
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
503-723 7.33e-31

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 122.02  E-value: 7.33e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPNRpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQVA 582
Cdd:PRK13632    8 IKVENVSFSYPNS-ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 583 AVGQEP--QVFGRSLQENIAYGLTQK----PTMEE-ITAAAVKSGAHSFISGLPQgydtevgeagsQLSGGQRQAVALAR 655
Cdd:PRK13632   87 IIFQNPdnQFIGATVEDDIAFGLENKkvppKKMKDiIDDLAKKVGMEDYLDKEPQ-----------NLSGGQKQRVAIAS 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2468698279 656 ALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQADHIL-FLEGGTIREG 723
Cdd:PRK13632  156 VLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIvFSEGKLIAQG 224
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
502-725 7.35e-31

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: 121.15  E-value: 7.35e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYPNRP-DVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKP---LPQYEHRYL 577
Cdd:cd03258     1 MIELKNVSKVFGDTGgKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDltlLSGKELRKA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 578 HRQVAAVGQEPQVF-GRSLQENIAYGLTqkptmeeitaaavksgahsfISGLPQGYDTE--------VGEAG------SQ 642
Cdd:cd03258    81 RRRIGMIFQHFNLLsSRTVFENVALPLE--------------------IAGVPKAEIEErvlellelVGLEDkadaypAQ 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 643 LSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQ-ADHILFLEGGTIR 721
Cdd:cd03258   141 LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVV 220

                  ....
gi 2468698279 722 EGGT 725
Cdd:cd03258   221 EEGT 224
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
503-729 2.00e-30

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


Pssm-ID: 213228 [Multi-domain]  Cd Length: 235  Bit Score: 119.91  E-value: 2.00e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLP---QYEHRYLHR 579
Cdd:cd03261     1 IELRGLTKSFGGRT---VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISglsEAELYRLRR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 580 QVAAVGQEPQVFGR-SLQENIAYGLTQKPTM--EEITA------AAVksgahsfisGLPQGYDTEVGEagsqLSGGQRQA 650
Cdd:cd03261    78 RMGMLFQSGALFDSlTVFENVAFPLREHTRLseEEIREivleklEAV---------GLRGAEDLYPAE----LSGGMKKR 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 651 VALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHL-SLVEQADHILFLEGGTIREGGTHQQL 729
Cdd:cd03261   145 VALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLdTAFAIADRIAVLYDGKIVAEGTPEEL 224
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
503-732 2.73e-30

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


Pssm-ID: 213263 [Multi-domain]  Cd Length: 239  Bit Score: 119.75  E-value: 2.73e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRylHRQVA 582
Cdd:cd03296     3 IEVRNVSKRFGDFV---ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 583 AVGQEPQVFGR-SLQENIAYGLTQKPTMEEITAAAVKSGAHSFI-----SGLPQGYDtevgeagSQLSGGQRQAVALARA 656
Cdd:cd03296    78 FVFQHYALFRHmTVFDNVAFGLRVKPRSERPPEAEIRAKVHELLklvqlDWLADRYP-------AQLSGGQRQRVALARA 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2468698279 657 LIRKPCVLILDDATSALDANSQLQVEQLLYE-SPELYSRSVLLITQHLSLVEQADHILFLEGGTIREGGTHQQLMEK 732
Cdd:cd03296   151 LAVEPKVLLLDEPFGALDAKVRKELRRWLRRlHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDH 227
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
502-729 2.85e-30

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


Pssm-ID: 224051 [Multi-domain]  Cd Length: 240  Bit Score: 119.53  E-value: 2.85e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYPnrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEH-RYLHRQ 580
Cdd:COG1126     2 MIEIKNLSKSFG---DKEVLKGISLSVEKGEVVVIIGPSGSGKSTLLRCLNGLEEPDSGSITVDGEDVGDKKDiLKLRRK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 581 VAAVGQEPQVFG-RSLQENIAYGL--TQKPTMEEITAAAVK--------SGAHSFisglPqgydtevgeagSQLSGGQRQ 649
Cdd:COG1126    79 VGMVFQQFNLFPhLTVLENVTLAPvkVKKLSKAEAREKALEllekvglaDKADAY----P-----------AQLSGGQQQ 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 650 AVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELySRSVLLITQHLSLVEQ-ADHILFLEGGTIREGGTHQQ 728
Cdd:COG1126   144 RVAIARALAMDPKVMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMIIVTHEMGFAREvADRVIFMDQGKIIEEGPPEE 222

                  .
gi 2468698279 729 L 729
Cdd:COG1126   223 F 223
FtsE COG2884
ABC-type ATPase involved in cell division [Cell cycle control, cell division, chromosome ...
502-727 3.43e-30

ABC-type ATPase involved in cell division [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 225438 [Multi-domain]  Cd Length: 223  Bit Score: 118.86  E-value: 3.43e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYPNRPdvLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHR---YLH 578
Cdd:COG2884     1 MIRFENVSKAYPGGR--EALRDVSFHIPKGEFVFLTGPSGAGKSTLLKLIYGEERPTRGKILVNGHDLSRLKGReipFLR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 579 RQVAAVGQEPQVF-GRSLQENIAYGL---------TQKPTMEEITAAAVKSGAHSFisglPqgydtevgeagSQLSGGQR 648
Cdd:COG2884    79 RQIGVVFQDFRLLpDRTVYENVALPLrvigkppreIRRRVSEVLDLVGLKHKARAL----P-----------SQLSGGEQ 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 649 QAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELySRSVLLITQHLSLVEQADH-ILFLEGGTIREGGTHQ 727
Cdd:COG2884   144 QRVAIARAIVNQPAVLLADEPTGNLDPDLSWEIMRLFEEINRL-GTTVLMATHDLELVNRMRHrVLALEDGRLVRDESRG 222
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
504-723 1.03e-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: 116.86  E-value: 1.03e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 504 QFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLpqyehRYLHRQVAA 583
Cdd:cd03235     1 EVEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPL-----EKERKRIGY 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 584 VGQEPQV---FGRSLQENIAYGLTQKPTMEEITAAAVKSGAHSFIsglpqgydTEVGEAG------SQLSGGQRQAVALA 654
Cdd:cd03235    73 VPQRRSIdrdFPISVRDVVLMGLYGHKGLFRRLSKADKAKVDEAL--------ERVGLSEladrqiGELSGGQQQRVLLA 144
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 655 RALIRKPCVLILDDATSALDANSQLQVEQLLYESPELySRSVLLITQHLSLVEQ-ADHILFLEGGTIREG 723
Cdd:cd03235   145 RALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEyFDRVLLLNRTVVASG 213
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
507-720 1.26e-29

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: 116.59  E-value: 1.26e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 507 DVSFAYpnRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRylhRQVAAVGQ 586
Cdd:cd03226     4 NISFSY--KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERR---KSIGYVMQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 587 EP--QVFGRSLQENIAYGLTQKPTMEEITAAAVKS-GAHSFISGLPQgydtevgeagsQLSGGQRQAVALARALIRKPCV 663
Cdd:cd03226    79 DVdyQLFTDSVREELLLGLKELDAGNEQAETVLKDlDLYALKERHPL-----------SLSGGQKQRLAIAAALLSGKDL 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2468698279 664 LILDDATSALDANSQLQVEQLLYESPELySRSVLLITQHLSLV-EQADHILFLEGGTI 720
Cdd:cd03226   148 LIFDEPTSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLaKVCDRVLLLANGAI 204
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
502-685 2.25e-29

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


Pssm-ID: 224053 [Multi-domain]  Cd Length: 500  Bit Score: 122.62  E-value: 2.25e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYPnrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHR-YLHRQ 580
Cdd:COG1129     8 LLELRGISKSFG---GVKALDGVSLTVRPGEVHALLGENGAGKSTLMKILSGVYPPDSGEILIDGKPVAFSSPRdALAAG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 581 VAAVGQEPQVFGR-SLQENI--------AYGLTQKPTMEEITAAAVKSgahsfiSGLPQGYDTEVGEagsqLSGGQRQAV 651
Cdd:COG1129    85 IATVHQELSLVPNlSVAENIflgreptrRFGLIDRKAMRRRARELLAR------LGLDIDPDTLVGD----LSIAQRQMV 154
                         170       180       190
                  ....*....|....*....|....*....|....
gi 2468698279 652 ALARALIRKPCVLILDDATSALDANsqlQVEQLL 685
Cdd:COG1129   155 EIARALSFDARVLILDEPTAALTVK---ETERLF 185
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
508-732 3.30e-29

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


Pssm-ID: 224048 [Multi-domain]  Cd Length: 539  Bit Score: 122.68  E-value: 3.30e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 508 VSFAYPNRPdVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNL----YQPTEGQLLLDGKP---LPQYEHRYLH-R 579
Cdd:COG1123    13 VEFATDGGR-VPAVRDVSFEVEPGEILGIVGESGSGKSTLALALMGLlpegGRITSGEVILDGRDllgLSEREMRKLRgK 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 580 QVAAVGQEP-------QVFGRSLQEniAYGLTQKPTMEEITAAAVKSGAhsfISGLPQgyDTEVGEAGSQLSGGQRQAVA 652
Cdd:COG1123    92 RIAMIFQDPmtslnpvMTIGDQIRE--ALRLHGKGSRAEARKRAVELLE---QVGLPD--PERRDRYPHQLSGGMRQRVM 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 653 LARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQ-ADHILFLEGGTIREGGTHQQLME 731
Cdd:COG1123   165 IAMALALKPKLLIADEPTTALDVTTQAQILDLLKDLQRELGMAVLFITHDLGVVAElADRVVVMYKGEIVETGPTEEILS 244

                  .
gi 2468698279 732 K 732
Cdd:COG1123   245 N 245
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
503-732 4.47e-29

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


Pssm-ID: 224042 [Multi-domain]  Cd Length: 253  Bit Score: 116.49  E-value: 4.47e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPnrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTvaaLLQNL--------YQPTEGQLLLDGKPLpqYEH 574
Cdd:COG1117     8 IEVRDLNLYYG---DKHALKDINLDIPKNKVTALIGPSGCGKST---LLRCLnrmndlipGARVEGEVLLDGKNI--YDP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 575 RY----LHRQVAAVGQEPQVFGRSLQENIAYGL----TQKPTMEEITAAAVKSGAhsfisgLpqgYDtEV----GEAGSQ 642
Cdd:COG1117    80 KVdvveLRRRVGMVFQKPNPFPMSIYDNVAYGLrlhgIKDKELDEIVESSLKKAA------L---WD-EVkdrlHKSALG 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 643 LSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYsrSVLLITQHLslvEQA----DHILFLEGG 718
Cdd:COG1117   150 LSGGQQQRLCIARALAVKPEVLLMDEPTSALDPISTLKIEELITELKKKY--TIVIVTHNM---QQAarvsDYTAFFYLG 224
                         250
                  ....*....|....
gi 2468698279 719 TIREGGTHQQLMEK 732
Cdd:COG1117   225 ELVEFGPTDKIFTN 238
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
500-732 7.23e-29

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 116.39  E-value: 7.23e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 500 EGLVQFQDVSFAYpNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHR 579
Cdd:PRK13648    5 NSIIVFKNVSFQY-QSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRK 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 580 QVAAVGQEP--QVFGRSLQENIAYGLTQK--PT--MEEITAAAVKS-GAHSFISGLPQGydtevgeagsqLSGGQRQAVA 652
Cdd:PRK13648   84 HIGIVFQNPdnQFVGSIVKYDVAFGLENHavPYdeMHRRVSEALKQvDMLERADYEPNA-----------LSGGQKQRVA 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 653 LARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQADHILFLEGGTIREGGTHQQLMEK 732
Cdd:PRK13648  153 IAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDH 232
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
503-730 1.72e-28

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: 114.32  E-value: 1.72e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPNRPDVLvlQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQVA 582
Cdd:cd03295     1 IEFENVTKRYGGGKKAV--NNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 583 AVGQEPQVF-GRSLQENIAYgltqKPTMEEITAAAVKSGAHSFIS--GL-PQGYdteVGEAGSQLSGGQRQAVALARALI 658
Cdd:cd03295    79 YVIQQIGLFpHMTVEENIAL----VPKLLKWPKEKIRERADELLAlvGLdPAEF---ADRYPHELSGGQQQRVGVARALA 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2468698279 659 RKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHL-SLVEQADHILFLEGGTIREGGTHQQLM 730
Cdd:cd03295   152 ADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEIL 224
cbiO PRK13640
energy-coupling factor transporter ATPase;
503-732 2.88e-28

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 114.90  E-value: 2.88e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPNRPdVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQP---TEGQLLLDGKPLPQYEHRYLHR 579
Cdd:PRK13640    6 VEFKHVSFTYPDSK-KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWDIRE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 580 QVAAVGQEP--QVFGRSLQENIAYGLTQK----PTMEEITAAAVKS-GAHSFISGLPQgydtevgeagsQLSGGQRQAVA 652
Cdd:PRK13640   85 KVGIVFQNPdnQFVGATVGDDVAFGLENRavprPEMIKIVRDVLADvGMLDYIDSEPA-----------NLSGGQKQRVA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 653 LARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQADHILFLEGGTIREGGTHQQLMEK 732
Cdd:PRK13640  154 IAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSK 233
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
500-729 4.46e-28

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


Pssm-ID: 226967 [Multi-domain]  Cd Length: 268  Bit Score: 113.85  E-value: 4.46e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 500 EGLVQFQDVSFAYPNR------PDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQY- 572
Cdd:COG4608     2 EPLLEVKNLKKYFPVGkgfgkkRYVKAVDGVSFSIKEGETLGLVGESGCGKSTLGRLILGLEEPTSGEILFEGKDITKLs 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 573 ---EHRYLHRQVAAVGQEPQVFGRslqeniaygltqkptmeeitaaavksgahsfisglpqgYDtevgeagSQLSGGQRQ 649
Cdd:COG4608    82 keeRRERVLELLEKVGLPEEFLYR--------------------------------------YP-------HELSGGQRQ 116
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 650 AVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQ-ADHILFLEGGTIREGGTHQQ 728
Cdd:COG4608   117 RIGIARALALNPKLIVADEPVSALDVSVQAQILNLLKDLQEELGLTYLFISHDLSVVRYiSDRIAVMYLGKIVEIGPTEE 196

                  .
gi 2468698279 729 L 729
Cdd:COG4608   197 V 197
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
503-732 4.91e-28

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: 112.72  E-value: 4.91e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPnrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKP---LPQYEhrylhR 579
Cdd:cd03300     1 IELENVSKFYG---GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDitnLPPHK-----R 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 580 QVAAVGQEPQVFGR-SLQENIAYGLTQKPTMEEITAAAVKSGAHSF-ISGLPQGYDtevgeagSQLSGGQRQAVALARAL 657
Cdd:cd03300    73 PVNTVFQNYALFPHlTVFENIAFGLRLKKLPKAEIKERVAEALDLVqLEGYANRKP-------SQLSGGQQQRVAIARAL 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 658 IRKPCVLILDDATSALDAnsQLQvEQLLYESPELYSR---SVLLITqH-----LSLveqADHILFLEGGTIREGGTHQQL 729
Cdd:cd03300   146 VNEPKVLLLDEPLGALDL--KLR-KDMQLELKRLQKElgiTFVFVT-HdqeeaLTM---SDRIAVMNKGKIQQIGTPEEI 218

                  ...
gi 2468698279 730 MEK 732
Cdd:cd03300   219 YEE 221
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
502-725 6.04e-28

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 114.02  E-value: 6.04e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYPNrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLpQYEHRYL---H 578
Cdd:PRK13639    1 ILETRDLKYSYPD--GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLlevR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 579 RQVAAVGQEP--QVFGRSLQENIAYG-LTQKPTMEEI----TAAAVKSGAHSFISGLPQgydtevgeagsQLSGGQRQAV 651
Cdd:PRK13639   78 KTVGIVFQNPddQLFAPTVEEDVAFGpLNLGLSKEEVekrvKEALKAVGMEGFENKPPH-----------HLSGGQKKRV 146
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2468698279 652 ALARALIRKPCVLILDDATSALDANSQLQVEQLLYespELYSRSVLLI--TQHLSLVE-QADHILFLEGGTIREGGT 725
Cdd:PRK13639  147 AIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLY---DLNKEGITIIisTHDVDLVPvYADKVYVMSDGKIIKEGT 220
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component [Amino acid transport ...
502-731 9.15e-28

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


Pssm-ID: 223487 [Multi-domain]  Cd Length: 237  Bit Score: 112.18  E-value: 9.15e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYE-HRYLHRQ 580
Cdd:COG0410     3 MLEVENLSAGYGKIQ---ALRGVSLEVERGEIVALLGRNGAGKTTLLKTIMGLVRPRSGRIIFDGEDITGLPpHERARLG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 581 VAAVGQEPQVFGR-SLQENIAYGltqkptmeeitaAAVKSGAHSFISGLPQGYD------TEVGEAGSQLSGGQRQAVAL 653
Cdd:COG0410    80 IAYVPEGRRIFPRlTVEENLLLG------------AYARRDKEAQERDLEEVYElfprlkERRNQRAGTLSGGEQQMLAI 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 654 ARALIRKPCVLILDDATSALdanSQLQVEQLLYESPELYSR---SVLLITQHLSLV-EQADHILFLEGGTIREGGTHQQL 729
Cdd:COG0410   148 ARALMSRPKLLLLDEPSEGL---APKIVEEIFEAIKELRKEggmTILLVEQNARFAlEIADRGYVLENGRIVLSGTAAEL 224

                  ..
gi 2468698279 730 ME 731
Cdd:COG0410   225 LA 226
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
501-725 1.32e-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: 110.96  E-value: 1.32e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 501 GLVQFQDVSFAY-PNRPDVLvlQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHR 579
Cdd:cd03369     5 GEIEVENLSVRYaPDLPPVL--KNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 580 QVAAVGQEPQVFGRSLQENI-AYGltqKPTMEEITAAavksgahsfisglpqgydTEVGEAGSQLSGGQRQAVALARALI 658
Cdd:cd03369    83 SLTIIPQDPTLFSGTIRSNLdPFD---EYSDEEIYGA------------------LRVSEGGLNLSQGQRQLLCLARALL 141
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2468698279 659 RKPCVLILDDATSALDANSQLQVEQLLYEspELYSRSVLLITQHLSLVEQADHILFLEGGTIREGGT 725
Cdd:cd03369   142 KRPRVLVLDEATASIDYATDALIQKTIRE--EFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
520-731 1.37e-27

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: 111.37  E-value: 1.37e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYE-HRYLHRQVAAVGQEPQVFGR-SLQE 597
Cdd:cd03224    15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPpHERARAGIGYVPEGRRIFPElTVEE 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 598 NI---AYGLTQ---KPTMEEItaaavksgahsfisglpqgYD------TEVGEAGSQLSGGQRQAVALARALIRKPCVLI 665
Cdd:cd03224    95 NLllgAYARRRakrKARLERV-------------------YElfprlkERRKQLAGTLSGGEQQMLAIARALMSRPKLLL 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2468698279 666 LDDATSALdanSQLQVEQLLYESPELYSR--SVLLITQHLSLVEQ-ADHILFLEGGTIREGGTHQQLME 731
Cdd:cd03224   156 LDEPSEGL---APKIVEEIFEAIRELRDEgvTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLA 221
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
506-730 1.43e-27

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 112.17  E-value: 1.43e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 506 QDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQVAAVG 585
Cdd:PRK13548    6 RNLSVRLGGRT---LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 586 QEPQV-FGRSLQENIAYGLT-----QKPTMEEITAAAVKSGAHSFisglpqgydtevgeAGS---QLSGGQRQAVALARA 656
Cdd:PRK13548   83 QHSSLsFPFTVEEVVAMGRAphglsRAEDDALVAAALAQVDLAHL--------------AGRdypQLSGGEQQRVQLARV 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 657 LIR------KPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQ-ADHILFLEGGTIREGGTHQQL 729
Cdd:PRK13548  149 LAQlwepdgPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARyADRIVLLHQGRLVADGTPAEV 228

                  .
gi 2468698279 730 M 730
Cdd:PRK13548  229 L 229
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
503-720 1.60e-27

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: 110.70  E-value: 1.60e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQ--YEHRYLHRQ 580
Cdd:cd03262     1 IEIKNLHKSFGDFH---VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDdkKNINELRQK 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 581 VAAVGQEPQVFG-RSLQENIAYGLT--QKPTMEEITAAAV----KSGAHSFISGLPqgydtevgeagSQLSGGQRQAVAL 653
Cdd:cd03262    78 VGMVFQQFNLFPhLTVLENITLAPIkvKGMSKAEAEERALelleKVGLADKADAYP-----------AQLSGGQQQRVAI 146
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2468698279 654 ARALIRKPCVLILDDATSALD---ANSQLQVEQLLYESpelySRSVLLITQHLSLV-EQADHILFLEGGTI 720
Cdd:cd03262   147 ARALAMNPKVMLFDEPTSALDpelVGEVLDVMKDLAEE----GMTMVVVTHEMGFArEVADRVIFMDDGRI 213
cbiO PRK13642
energy-coupling factor transporter ATPase;
499-720 1.65e-27

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 112.88  E-value: 1.65e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 499 LEGLVQFQDVSFAYPNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLH 578
Cdd:PRK13642    1 MNKILEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 579 RQVAAVGQEP--QVFGRSLQENIAYGLT-----QKPTMEEITAAAVKSGAHSFISGLPqgydtevgeagSQLSGGQRQAV 651
Cdd:PRK13642   81 RKIGMVFQNPdnQFVGATVEDDVAFGMEnqgipREEMIKRVDEALLAVNMLDFKTREP-----------ARLSGGQKQRV 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2468698279 652 ALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQADHILFLEGGTI 720
Cdd:PRK13642  150 AVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEI 218
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
526-724 2.20e-27

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


Pssm-ID: 213264 [Multi-domain]  Cd Length: 214  Bit Score: 110.46  E-value: 2.20e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 526 FTLR-----PGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPL----------PQyehrylHRQVAAVGQEPQV 590
Cdd:cd03297    13 FTLKidfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdsrkkinlpPQ------QRKIGLVFQQYAL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 591 FGR-SLQENIAYGLTQKPTMEE-ITAAAVKSGAHsfISGLPQGYDtevgeagSQLSGGQRQAVALARALIRKPCVLILDD 668
Cdd:cd03297    87 FPHlNVRENLAFGLKRKRNREDrISVDELLDLLG--LDHLLNRYP-------AQLSGGEKQRVALARALAAQPELLLLDE 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2468698279 669 ATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQ-ADHILFLEGGTIREGG 724
Cdd:cd03297   158 PFSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
504-720 2.43e-27

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: 111.12  E-value: 2.43e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 504 QFQDVSFAYPNrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLH---RQ 580
Cdd:cd03256     2 EVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRqlrRQ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 581 VAAVGQEPQVFGR-SLQENIAYGltqkptmeeitaaavKSGAHSFISGLPQGYDTE-----------VGEAG------SQ 642
Cdd:cd03256    80 IGMIFQQFNLIERlSVLENVLSG---------------RLGRRSTWRSLFGLFPKEekqralaalerVGLLDkayqraDQ 144
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2468698279 643 LSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLV-EQADHILFLEGGTI 720
Cdd:cd03256   145 LSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLArEYADRIVGLKDGRI 223
PLN03130 PLN03130
ABC transporter C family member; Provisional
266-746 2.75e-27

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 119.07  E-value: 2.75e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279  266 GAVLRQETEFFQQNQTGNITSRVTEDTSTLSDSLSENLSLFL---WYLVRGLCLLGIM----LWGSVSLTMVTLVTLPll 338
Cdd:PLN03130   994 GSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNVAVFVNMFLgqiFQLLSTFVLIGIVstisLWAIMPLLVLFYGAYL-- 1071
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279  339 fllpkkvgkWYQLL--EVQVRESLAKSSQVAI--EALSAMPTVRsfaneegeAQKFREKLQEIKTLNQKEAVAYAV---- 410
Cdd:PLN03130  1072 ---------YYQSTarEVKRLDSITRSPVYAQfgEALNGLSTIR--------AYKAYDRMAEINGRSMDNNIRFTLvnms 1134
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279  411 -NSWTT----SISG-MLLKVGILYIGGQLVTSGAVSSGNLVTFVL-YQMQFTQAVEVLLSIYPRVQKAVGSSEKIFEYLD 483
Cdd:PLN03130  1135 sNRWLAirleTLGGlMIWLTASFAVMQNGRAENQAAFASTMGLLLsYALNITSLLTAVLRLASLAENSLNAVERVGTYID 1214
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279  484 RTPRCP--------PSGLLTplhlEGLVQFQDVSFAYpnRPDVL-VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNL 554
Cdd:PLN03130  1215 LPSEAPlviennrpPPGWPS----SGSIKFEDVVLRY--RPELPpVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRI 1288
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279  555 YQPTEGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQENIaygltqKPTMEEITAAAVKS--GAH--SFISGLPQ 630
Cdd:PLN03130  1289 VELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNL------DPFNEHNDADLWESleRAHlkDVIRRNSL 1362
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279  631 GYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYEspELYSRSVLLITQHLSLVEQAD 710
Cdd:PLN03130  1363 GLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIRE--EFKSCTMLIIAHRLNTIIDCD 1440
                          490       500       510
                   ....*....|....*....|....*....|....*....
gi 2468698279  711 HILFLEGGTIREGGTHQQLMEKKGCYWA-MVQA--PADA 746
Cdd:PLN03130  1441 RILVLDAGRVVEFDTPENLLSNEGSAFSkMVQStgAANA 1479
OpuBA COG1125
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ...
502-725 3.24e-27

ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 224050 [Multi-domain]  Cd Length: 309  Bit Score: 112.78  E-value: 3.24e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQV 581
Cdd:COG1125     1 MIEFENVSKRYGNKK---AVDDVNLTIEEGEFLVLIGPSGSGKTTTLKMINRLIEPTSGEILIDGEDISDLDPVELRRKI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 582 AAVGQEPQVF-GRSLQENIAYgltqKPTMEEITAAAVKSGAHSFIS--GL-PQGYdteVGEAGSQLSGGQRQAVALARAL 657
Cdd:COG1125    78 GYVIQQIGLFpHLTVAENIAT----VPKLLGWDKERIKKRADELLDlvGLdPSEY---ADRYPHELSGGQQQRVGVARAL 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2468698279 658 IRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITqH-----LSLveqADHILFLEGGTIREGGT 725
Cdd:COG1125   151 AADPPILLMDEPFGALDPITRKQLQEEIKELQKELGKTIVFVT-HdideaLKL---ADRIAVMDAGEIVQYDT 219
FetA COG4619
ABC-type iron transport system FetAB, ATPase component [Inorganic ion transport and metabolism] ...
502-700 4.74e-27

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


Pssm-ID: 226970 [Multi-domain]  Cd Length: 223  Bit Score: 109.56  E-value: 4.74e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQV 581
Cdd:COG4619     3 LLELKQVGYLAGDAK---ILNNISLSVRAGEFIAITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDVSTLKPEAYRQQV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 582 AAVGQEPQVFGRSLQENI--AYGLTQKPTMEEITAAAVKSgahsfiSGLPqgyDTEVGEAGSQLSGGQRQAVALARALIR 659
Cdd:COG4619    80 SYCAQTPALFGDTVEDNLifPWQIRNRRPDRAAALDLLAR------FALP---DSILTKNITELSGGEKQRIALIRNLQF 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2468698279 660 KPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLIT 700
Cdd:COG4619   151 MPKILLLDEITSALDESNKRNIEEMIHRYVREQNVAVLWIT 191
ABC_6TM_Pgp_ABCB1_D1_like cd18577
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ...
202-478 6.54e-27

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: 111.41  E-value: 6.54e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 202 MAIPF--FTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGDGIYNNTMGHVhSHLQG-----EVFGAVLRQETE 274
Cdd:cd18577    18 MTIVFgdLFDAFTDFGSGESSPDEFLDDVNKYALYFVYLGIGSFVLSYIQTACWTIT-GERQArrirkRYLKALLRQDIA 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 275 FFQQNQTGNITSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEV 354
Cdd:cd18577    97 WFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLPLIAIVGGIMGKLLSKYTK 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 355 QVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLV 434
Cdd:cd18577   177 KEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLFFIIFAMYALAFWYGSRLV 256
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 2468698279 435 TSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18577   257 RDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
MlaF COG1127
ABC-type transporter Mla maintaining outer membrane lipid asymmetry, ATPase component MlaF ...
502-729 7.21e-27

ABC-type transporter Mla maintaining outer membrane lipid asymmetry, ATPase component MlaF [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 224052 [Multi-domain]  Cd Length: 263  Bit Score: 110.38  E-value: 7.21e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQY--EHRYLHR 579
Cdd:COG1127     8 LIEVRGVTKSFGDRV---ILDGVDLDVPRGEILAILGGSGSGKSTLLRLILGLLRPDKGEILIDGEDIPQLseEELYEIR 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 580 -QVAAVGQEPQVFGR-SLQENIAYGLTQ-----KPTMEEITAAAVKSgahsfiSGLPqgydtevGEAG----SQLSGGQR 648
Cdd:COG1127    85 kRMGVLFQQGALFSSlTVFENVAFPLREhtklpESLIRELVLMKLEL------VGLR-------GAAAdlypSELSGGMR 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 649 QAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHL-SLVEQADHILFLEGGTIREGGTHQ 727
Cdd:COG1127   152 KRVALARAIALDPELLFLDEPTSGLDPISAGVIDELIRELNDALGLTVIMVTHDLdSLLTIADRVAVLADGKVIAEGTPE 231

                  ..
gi 2468698279 728 QL 729
Cdd:COG1127   232 EL 233
ThiQ COG3840
ABC-type thiamine transport system, ATPase component [Coenzyme transport and metabolism];
507-734 8.19e-27

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


Pssm-ID: 226360 [Multi-domain]  Cd Length: 231  Bit Score: 109.36  E-value: 8.19e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 507 DVSFAYPNRPdvlvlqgLTFTLR--PGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKP---LPQYEhrylhRQV 581
Cdd:COG3840     6 DVRFSYGHLP-------MRFDLTvpAGEIVAILGPSGAGKSTLLNLIAGFETPASGEILINGVDhtaSPPAE-----RPV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 582 AAVGQEPQVFGR-SLQENIAYGLtqKPTM-------EEITAAAVKSGAHSFISGLPqgydtevgeagSQLSGGQRQAVAL 653
Cdd:COG3840    74 SMLFQENNLFAHlTVAQNIGLGL--SPGLklnaeqrEKVEAAAAQVGLAGFLKRLP-----------GELSGGQRQRVAL 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 654 ARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQ-ADHILFLEGGTIREGGTHQQLMEK 732
Cdd:COG3840   141 ARCLVREQPILLLDEPFSALDPALRAEMLALVSQLCDERKMTLLMVTHHPEDAARiADRVVFLDNGRIAAQGSTQELLSG 220

                  ..
gi 2468698279 733 KG 734
Cdd:COG3840   221 KA 222
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
490-731 1.65e-26

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


Pssm-ID: 226641 [Multi-domain]  Cd Length: 534  Bit Score: 114.29  E-value: 1.65e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 490 PSGLLTPLHLEG--LVQFQDVSFAYPNRPDVL--------VLQGLTFTLRPGEVTALVGPNGSGKSTVA-ALLQNLyqPT 558
Cdd:COG4172   262 PSGDPPPLPEDApvLLEVEDLRVWFPIKGGFLrrtvdhlrAVDGISLTLRRGQTLGLVGESGSGKSTLGlALLRLI--PS 339
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 559 EGQLLLDGKPLPQY---EHRYLHRQVAAVGQEPqvFG-----RSLQENIAYGL---TQKPTMEEI---TAAAVKSgahsf 624
Cdd:COG4172   340 QGEIRFDGQDIDGLsrkEMRPLRRRMQVVFQDP--YGslsprMTVGQIIEEGLrvhEPKLSAAERdqrVIEALEE----- 412
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 625 iSGLPQG----YDTEvgeagsqLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLIT 700
Cdd:COG4172   413 -VGLDPAtrnrYPHE-------FSGGQRQRIAIARALILKPELILLDEPTSALDRSVQAQVLDLLRDLQQKHGLSYLFIS 484
                         250       260       270
                  ....*....|....*....|....*....|..
gi 2468698279 701 QHLSLVEQ-ADHILFLEGGTIREGGTHQQLME 731
Cdd:COG4172   485 HDLAVVRAlCHRVIVMRDGKIVEQGPTEAVFA 516
cbiO PRK13650
energy-coupling factor transporter ATPase;
499-729 2.09e-26

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 109.44  E-value: 2.09e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 499 LEGLVQFQDVSFAYPNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLH 578
Cdd:PRK13650    1 MSNIIEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 579 RQVAAVGQEP--QVFGRSLQENIAYGLTQK----PTMEEITAAAVK-SGAHSFISGLPqgydtevgeagSQLSGGQRQAV 651
Cdd:PRK13650   81 HKIGMVFQNPdnQFVGATVEDDVAFGLENKgiphEEMKERVNEALElVGMQDFKEREP-----------ARLSGGQKQRV 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2468698279 652 ALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQADHILFLEGGTIREGGTHQQL 729
Cdd:PRK13650  150 AIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
502-729 2.79e-26

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 109.12  E-value: 2.79e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYpnRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQV 581
Cdd:PRK13652    3 LIETRDLCYSY--SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 582 AAVGQEP--QVFGRSLQENIAYGLTQKPTMEEITAAAVKSGAHSFisGLPQGYDtevgEAGSQLSGGQRQAVALARALIR 659
Cdd:PRK13652   81 GLVFQNPddQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHML--GLEELRD----RVPHHLSGGEKKRVAIAGVIAM 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2468698279 660 KPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLV-EQADHILFLEGGTIREGGTHQQL 729
Cdd:PRK13652  155 EPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEI 225
ABC_6TM_MsbA_like cd18552
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ...
203-478 3.80e-26

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: 109.05  E-value: 3.80e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 203 AIPFFTGRLTDWILQDGSADTftrnLTLMSILTIASAVLEFVGDGIYNNTMGHVHSH----LQGEVFGAVLRQETEFFQQ 278
Cdd:cd18552    17 ALAWLLKPLLDDIFVEKDLEA----LLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRvvrdLRNDLFDKLLRLPLSFFDR 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 279 NQTGNITSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEVQVRE 358
Cdd:cd18552    93 NSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPIRRIGKRLRKISRRSQE 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 359 SLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSGA 438
Cdd:cd18552   173 SMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELLGAIAIALVLWYGGYQVISGE 252
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 2468698279 439 VSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18552   253 LTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAAAERI 292
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
503-675 5.46e-26

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: 106.18  E-value: 5.46e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPNrpdVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGK---PLPQYEhrylhR 579
Cdd:cd03301     1 VELENVTKRFGN---VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRdvtDLPPKD-----R 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 580 QVAAVGQEPQVFGR-SLQENIAYGLTQKPTMEEITAAAVKSGAHSF-ISGLPQGYDtevgeagSQLSGGQRQAVALARAL 657
Cdd:cd03301    73 DIAMVFQNYALYPHmTVYDNIAFGLKLRKVPKDEIDERVREVAELLqIEHLLDRKP-------KQLSGGQRQRVALGRAI 145
                         170
                  ....*....|....*...
gi 2468698279 658 IRKPCVLILDDATSALDA 675
Cdd:cd03301   146 VREPKVFLMDEPLSNLDA 163
PLN03130 PLN03130
ABC transporter C family member; Provisional
369-734 9.42e-26

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 114.06  E-value: 9.42e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279  369 EALSAMPTVRSFANEegeaQKFREKLQEIK----TLNQKEAVAYAVNSWTTSISGMLLKV---GIL-YIGGQLVTSGAVS 440
Cdd:PLN03130   484 EVLAAMDTVKCYAWE----NSFQSKVQTVRddelSWFRKAQLLSAFNSFILNSIPVLVTVvsfGVFtLLGGDLTPARAFT 559
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279  441 SGNL---VTFVLYQMQ--FTQAVEVLLSIyPRVQKAVGSSEKIFeyldrtprcppsgLLTPLHLEGL--VQFQDVSFAYP 513
Cdd:PLN03130   560 SLSLfavLRFPLFMLPnlITQAVNANVSL-KRLEELLLAEERVL-------------LPNPPLEPGLpaISIKNGYFSWD 625
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279  514 NRPDVLVLQGLTFTLRPGEVTALVGPNGSGK-STVAALLQNLYQPTEGQLLLDGKplpqyehrylhrqVAAVGQEPQVFG 592
Cdd:PLN03130   626 SKAERPTLSNINLDVPVGSLVAIVGSTGEGKtSLISAMLGELPPRSDASVVIRGT-------------VAYVPQVSWIFN 692
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279  593 RSLQENIAYGLTQKPTMEEiTAAAVKSGAHSfISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATSA 672
Cdd:PLN03130   693 ATVRDNILFGSPFDPERYE-RAIDVTALQHD-LDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSA 770
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2468698279  673 LDANSQLQV-EQLLYEspELYSRSVLLITQHLSLVEQADHILFLEGGTIREGGTH----------QQLMEKKG 734
Cdd:PLN03130   771 LDAHVGRQVfDKCIKD--ELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYeelsnngplfQKLMENAG 841
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
502-722 9.43e-26

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 105.95  E-value: 9.43e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQV 581
Cdd:PRK10247    7 LLQLQNVGYLAGDAK---ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 582 AAVGQEPQVFGRSLQENIAYGLT---QKPTMEEITAAAVKsgahsFisGLPqgyDTEVGEAGSQLSGGQRQAVALARALI 658
Cdd:PRK10247   84 SYCAQTPTLFGDTVYDNLIFPWQirnQQPDPAIFLDDLER-----F--ALP---DTILTKNIAELSGGEKQRISLIRNLQ 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2468698279 659 RKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQADHILFLE--GGTIRE 722
Cdd:PRK10247  154 FMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITLQphAGEMQE 219
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
502-722 1.63e-25

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 106.69  E-value: 1.63e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYPN------RPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQY--- 572
Cdd:PRK10419    3 LLNVSGLSHHYAHgglsgkHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLnra 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 573 EHRYLHRQVAAVGQEP-------QVFGRSLQENIAYGLTQKPTMEEITAAAVKSG---AHSFISGLPQgydtevgeagsQ 642
Cdd:PRK10419   83 QRKAFRRDIQMVFQDSisavnprKTVREIIREPLRHLLSLDKAERLARASEMLRAvdlDDSVLDKRPP-----------Q 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 643 LSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQ-ADHILFLEGGTIR 721
Cdd:PRK10419  152 LSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERfCQRVMVMDNGQIV 231

                  .
gi 2468698279 722 E 722
Cdd:PRK10419  232 E 232
ABC_6TM_LmrA_like cd18551
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ...
203-478 1.65e-25

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


Pssm-ID: 349995 [Multi-domain]  Cd Length: 289  Bit Score: 107.13  E-value: 1.65e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 203 AIPFFTGRLTDWILQDGSAdtfTRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQNQTG 282
Cdd:cd18551    17 AQPLLVKNLIDALSAGGSS---GGLLALLVALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWRRLLRLPVSFFDRRRSG 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 283 NITSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEVQVRESLAK 362
Cdd:cd18551    94 DLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILPLGRRIRKASKRAQDALGE 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 363 SSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSGAVSSG 442
Cdd:cd18551   174 LSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQLALLVVLGVGGARVASGALTVG 253
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 2468698279 443 NLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18551   254 TLVAFLLYLFQLITPLSQLSSFFTQLQKALGALERI 289
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
516-720 2.00e-25

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: 102.89  E-value: 2.00e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 516 PDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPqyehrylhrqvaavgqepqvfGRSL 595
Cdd:cd03216    11 GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVS---------------------FASP 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 596 QENIAYGLtqkptmeeitaAAVksgahsfisglpqgydtevgeagSQLSGGQRQAVALARALIRKPCVLILDDATSALDA 675
Cdd:cd03216    70 RDARRAGI-----------AMV-----------------------YQLSVGERQMVEIARALARNARLLILDEPTAALTP 115
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2468698279 676 NsqlQVEQLLYESPELYSR--SVLLITQHLSLVEQ-ADHILFLEGGTI 720
Cdd:cd03216   116 A---EVERLFKVIRRLRAQgvAVIFISHRLDEVFEiADRVTVLRDGRV 160
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
502-725 2.03e-25

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


Pssm-ID: 223521 [Multi-domain]  Cd Length: 316  Bit Score: 107.66  E-value: 2.03e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYPNRP-DVLVLQGLTFTLRPGEVTALVGPNGSGKSTVA-ALLQNLYQP----TEGQLLLDGKPL----PQ 571
Cdd:COG0444     1 LLEVKNLSVSFPTDAgVVKAVDGVSFELKKGEILGIVGESGSGKSVLAkAIMGLLPKPnariVGGEILFDGKDLlslsEK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 572 YEHRYLHRQVAAVGQEPQvfgRSLqeNIAYgltqkpTMEEITAAAVKsgAHSFISGLPQGYDT------EVG--EAGS-- 641
Cdd:COG0444    81 ELRKIRGKEIAMIFQDPM---TSL--NPVM------TIGDQIAEVLR--LHGKGLSKKEAKERaielleLVGipDPERrl 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 642 -----QLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQ-ADHILFL 715
Cdd:COG0444   148 ksyphELSGGMRQRVMIAMALALNPKLLIADEPTTALDVTVQAQILDLLKELQREKGTALILITHDLGVVAEiADRVAVM 227
                         250
                  ....*....|
gi 2468698279 716 EGGTIREGGT 725
Cdd:COG0444   228 YAGRIVEEGP 237
ABC_6TM_YknU_like cd18542
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ...
202-478 2.27e-25

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


Pssm-ID: 349986 [Multi-domain]  Cd Length: 292  Bit Score: 106.75  E-value: 2.27e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 202 MAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGdGIYNNTMGH-VHSHLQGEVFGAVLRQETEFFQQNQ 280
Cdd:cd18542    16 LLIPLLIRRIIDSVIGGGLRELLWLLALLILGVALLRGVFRYLQ-GYLAEKASQkVAYDLRNDLYDHLQRLSFSFHDKAR 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 281 TGNITSRVTEDTSTLSDSLSENLSLflwyLVRGLCLLG----IMLWGSVSLTMVTLVT----LPLLFLLPKKVGKWYQll 352
Cdd:cd18542    95 TGDLMSRCTSDVDTIRRFLAFGLVE----LVRAVLLFIgaliIMFSINWKLTLISLAIipfiALFSYVFFKKVRPAFE-- 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 353 evQVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVN-SWTTSISGMLLkVGILYIGG 431
Cdd:cd18542   169 --EIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYwPLMDFLSGLQI-VLVLWVGG 245
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 2468698279 432 QLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18542   246 YLVINGEITLGELVAFISYLWMLIWPVRQLGRLINDMSRASASAERI 292
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component [Amino acid transport ...
518-720 2.58e-25

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


Pssm-ID: 223488 [Multi-domain]  Cd Length: 250  Bit Score: 105.35  E-value: 2.58e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 518 VLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYE-HRYLHRQVAAVGQEPQVF----- 591
Cdd:COG0411    17 LTAVNDVSLEVRPGEIVGLIGPNGAGKTTLFNLITGFYKPSSGTVIFRGRDITGLPpHRIARLGIARTFQITRLFpgltv 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 592 ------GRSLQENIAYGLTQKPTMEEITAAAVKsgAHSFIS--GLPQGYDTEVGEagsqLSGGQRQAVALARALIRKPCV 663
Cdd:COG0411    97 lenvavGAHARLGLSGLLGRPRARKEEREARER--ARELLEfvGLGELADRPAGN----LSYGQQRRLEIARALATQPKL 170
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2468698279 664 LILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQ-ADHILFLEGGTI 720
Cdd:COG0411   171 LLLDEPAAGLNPEETEELAELIRELRDRGGVTILLIEHDMKLVMGlADRIVVLNYGEV 228
SapF COG4167
ABC-type antimicrobial peptide transport system, ATPase component [Defense mechanisms];
499-729 2.99e-25

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


Pssm-ID: 226637 [Multi-domain]  Cd Length: 267  Bit Score: 105.67  E-value: 2.99e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 499 LEGLVQFQDVSFAYPNRPDVL------VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQY 572
Cdd:COG4167     1 IETLLEVRNLSKTFRYRTGLFrrqtveAVKPVSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGEILINDHPLHFG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 573 EHRYLHRQVAAVGQEP-------QVFGRSLQE--NIAYGLTQKPTMEEI--TAAAVksgahsfisGLpqgYDTEVGEAGS 641
Cdd:COG4167    81 DYSFRSKRIRMIFQDPntslnprLRIGQILDFplRLNTDLEPEQRRKQIfeTLRMV---------GL---LPDHANYYPH 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 642 QLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQ-ADHILFL-EGGT 719
Cdd:COG4167   149 MLAPGQKQRVALARALILRPKIIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHIGMIKHiSDQVLVMhEGEV 228
                         250
                  ....*....|
gi 2468698279 720 IREGGTHQQL 729
Cdd:COG4167   229 VERGSTADVL 238
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
515-736 4.50e-25

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: 111.96  E-value: 4.50e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279  515 RPDVLVLQGLTFTLRPGEVTALVGPNGSGKST-VAALLQNLyQPTEGQLLLDGkplpqyehrylhrQVAAVGQEPQVFGR 593
Cdd:TIGR00957  648 RDLPPTLNGITFSIPEGALVAVVGQVGCGKSSlLSALLAEM-DKVEGHVHMKG-------------SVAYVPQQAWIQND 713
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279  594 SLQENIAYG--LTQKPTMEEITAAAVKSGahsfISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATS 671
Cdd:TIGR00957  714 SLRENILFGkaLNEKYYQQVLEACALLPD----LEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLS 789
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279  672 ALDANsqlqVEQLLYES---PE--LYSRSVLLITQHLSLVEQADHILFLEGGTIREGGTHQQLMEKKGCY 736
Cdd:TIGR00957  790 AVDAH----VGKHIFEHvigPEgvLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAF 855
ABC_FtsE_transporter cd03292
ATP-binding cassette domain of the cell division transporter; FtsE is a hydrophilic ...
503-720 4.59e-25

ATP-binding cassette domain of the cell division transporter; FtsE is a hydrophilic nucleotide-binding protein that binds FtsX to form a heterodimeric ATP-binding cassette (ABC)-type transporter that associates with the bacterial inner membrane. The FtsE/X transporter is thought to be involved in cell division and is important for assembly or stability of the septal ring.


Pssm-ID: 213259 [Multi-domain]  Cd Length: 214  Bit Score: 103.64  E-value: 4.59e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPNrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHR---YLHR 579
Cdd:cd03292     1 IEFINVTKTYPN--GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRaipYLRR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 580 QVAAVGQEPQVF-GRSLQENIAYGL--TQKPTME---EITAAAVKSGAHSFISGLPqgydtevgeagSQLSGGQRQAVAL 653
Cdd:cd03292    79 KIGVVFQDFRLLpDRNVYENVAFALevTGVPPREirkRVPAALELVGLSHKHRALP-----------AELSGGEQQRVAI 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2468698279 654 ARALIRKPCVLILDDATSALDANSQLQVEQLLyESPELYSRSVLLITQHLSLVEQADH-ILFLEGGTI 720
Cdd:cd03292   148 ARAIVNSPTILIADEPTGNLDPDTTWEIMNLL-KKINKAGTTVVVATHAKELVDTTRHrVIALERGKL 214
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
502-729 5.07e-25

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


Pssm-ID: 226641 [Multi-domain]  Cd Length: 534  Bit Score: 109.67  E-value: 5.07e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAY-PNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKS-TVAALLQNLYQPT----EGQLLLDGKPLPQYEHR 575
Cdd:COG4172     6 LLSIRNLSVAFhQEGGTVEAVKGISFDIEAGETLALVGESGSGKSvTALSILGLLPSPAaahpSGSILFDGEDLLAASER 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 576 YLHR----QVAAVGQEPQV-------FGRSLQENIA--YGLTQKPTMEEITAAAVKSG---AHSFISGLPQgydtevgea 639
Cdd:COG4172    86 QLRGvrgnKIGMIFQEPMTslnplhtIGKQLAEVLRlhRGLSRAAARARALELLELVGipePEKRLDAYPH--------- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 640 gsQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQ-ADHILFLEGG 718
Cdd:COG4172   157 --ELSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKELQAELGMAILFITHDLGIVRKfADRVYVMQHG 234
                         250
                  ....*....|.
gi 2468698279 719 TIREGGTHQQL 729
Cdd:COG4172   235 EIVETGTTETL 245
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
500-733 5.44e-25

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 104.47  E-value: 5.44e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 500 EGLVQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTvaaLLQNLYQ--------PTEGQLLLDGKPL-- 569
Cdd:PRK14239    3 EPILQVSDLSVYYNKKK---ALNSVSLDFYPNEITALIGPSGSGKST---LLRSINRmndlnpevTITGSIVYNGHNIys 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 570 PQYEHRYLHRQVAAVGQEPQVFGRSLQENIAYGL-----TQKPTMEEITAAAVKsGAHSFISGLPQGYDTEVGeagsqLS 644
Cdd:PRK14239   77 PRTDTVDLRKEIGMVFQQPNPFPMSIYENVVYGLrlkgiKDKQVLDEAVEKSLK-GASIWDEVKDRLHDSALG-----LS 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 645 GGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYsrSVLLITQHLslvEQADHI-----LFLEGGT 719
Cdd:PRK14239  151 GGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSM---QQASRIsdrtgFFLDGDL 225
                         250
                  ....*....|....
gi 2468698279 720 IREGGTHQQLMEKK 733
Cdd:PRK14239  226 IEYNDTKQMFMNPK 239
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
502-731 9.80e-25

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 103.63  E-value: 9.80e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYPnrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPL--PQYEHRYLHR 579
Cdd:PRK09493    1 MIEFKNVSKHFG---PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndPKVDERLIRQ 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 580 QVAAVGQEPQVFGR-SLQENIAYGLTQkptmeeiTAAAVKSGAHSFISGLPqgydTEVGEAG------SQLSGGQRQAVA 652
Cdd:PRK09493   78 EAGMVFQQFYLFPHlTALENVMFGPLR-------VRGASKEEAEKQARELL----AKVGLAErahhypSELSGGQQQRVA 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 653 LARALIRKPCVLILDDATSALDANSQ---LQVEQLLYESpelySRSVLLITQHLSLVEQ-ADHILFLEGGTIREGGTHQQ 728
Cdd:PRK09493  147 IARALAVKPKLMLFDEPTSALDPELRhevLKVMQDLAEE----GMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQV 222

                  ...
gi 2468698279 729 LME 731
Cdd:PRK09493  223 LIK 225
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
496-731 9.92e-25

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 104.10  E-value: 9.92e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 496 PLHLEGLVQFQDVSFAYPNRpdvLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHR 575
Cdd:PRK10575    5 TNHSDTTFALRNVSFRVPGR---TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 576 YLHRQVAAVGQE-PQVFGRSLQENIA------------YGLTQKPTMEE-ITAAAVKSGAHSFIsglpqgydtevgeagS 641
Cdd:PRK10575   82 AFARKVAYLPQQlPAAEGMTVRELVAigrypwhgalgrFGAADREKVEEaISLVGLKPLAHRLV---------------D 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 642 QLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQ-ADHILFLEGGTI 720
Cdd:PRK10575  147 SLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARyCDYLVALRGGEM 226
                         250
                  ....*....|.
gi 2468698279 721 REGGTHQQLME 731
Cdd:PRK10575  227 IAQGTPAELMR 237
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
490-729 1.21e-24

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 108.64  E-value: 1.21e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 490 PSGLLTPL--HLEGLVQFQDVSFAYPNRPDVL--------VLQGLTFTLRPGEVTALVGPNGSGKSTVA-ALLQNLyqPT 558
Cdd:PRK15134  261 PSGDPVPLpePASPLLDVEQLQVAFPIRKGILkrtvdhnvVVKNISFTLRPGETLGLVGESGSGKSTTGlALLRLI--NS 338
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 559 EGQLLLDGKPLPQYEHRYL---HRQVAAVGQEPQvfgRSL------QENIAYGLT-QKPTMeeiTAAAVKSgahSFISGL 628
Cdd:PRK15134  339 QGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDPN---SSLnprlnvLQIIEEGLRvHQPTL---SAAQREQ---QVIAVM 409
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 629 pqgydTEVG-------EAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQ 701
Cdd:PRK15134  410 -----EEVGldpetrhRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISH 484
                         250       260
                  ....*....|....*....|....*....
gi 2468698279 702 HLSLVEQADH-ILFLEGGTIREGGTHQQL 729
Cdd:PRK15134  485 DLHVVRALCHqVIVLRQGEVVEQGDCERV 513
ABC_6TM_bac_exporter_ABCB8_10_like cd18575
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ...
203-478 2.39e-24

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: 103.72  E-value: 2.39e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 203 AIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGdgIYN-NTMG-HVHSHLQGEVFGAVLRQETEFFQQNQ 280
Cdd:cd18575    14 ALGQGLRLLIDQGFAAGNTALLNRAFLLLLAVALVLALASALR--FYLvSWLGeRVVADLRKAVFAHLLRLSPSFFETTR 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 281 TGNITSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEVQVRESL 360
Cdd:cd18575    92 TGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFGRRVRRLSRASQDRL 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 361 AKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSGAVS 440
Cdd:cd18575   172 ADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRARALLTALVIFLVFGAIVFVLWLGAHDVLAGRMS 251
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 2468698279 441 SGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18575   252 AGELSQFVFYAVLAAGSVGALSEVWGDLQRAAGAAERL 289
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
506-730 2.52e-24

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 102.78  E-value: 2.52e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 506 QDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQVAAVG 585
Cdd:PRK11231    6 ENLTVGYGTKR---ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 586 QEPQV-FGRSLQENIAYG----------LTQKPtmEEITAAAVKsgahsfisglpqgyDTEVGEAG----SQLSGGQRQA 650
Cdd:PRK11231   83 QHHLTpEGITVRELVAYGrspwlslwgrLSAED--NARVNQAME--------------QTRINHLAdrrlTDLSGGQRQR 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 651 VALARALIRKPCVLILDDATSALDANSQLQVEQLLYespELYSRSVLLITQhLSLVEQA----DHILFLEGGTIREGGTH 726
Cdd:PRK11231  147 AFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMR---ELNTQGKTVVTV-LHDLNQAsrycDHLVVLANGHVMAQGTP 222

                  ....
gi 2468698279 727 QQLM 730
Cdd:PRK11231  223 EEVM 226
COG4559 COG4559
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
520-728 2.92e-24

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


Pssm-ID: 226929 [Multi-domain]  Cd Length: 259  Bit Score: 102.82  E-value: 2.92e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQV-FGRSLQEN 598
Cdd:COG4559    16 LLDGVSLDLRPGEVLAILGPNGAGKSTLLKALSGELSPDSGEVTLNGVPLNSWPPEELARHRAVLPQNSSLaFPFTVQEV 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 599 IAYGL------TQKPTMEEITAAAVksgAHSFISGLPQGYDTEvgeagsqLSGGQRQAVALARAL------IRKPCVLIL 666
Cdd:COG4559    96 VQMGRiphrsgREPEEDERIAAQAL---AATDLSGLAGRDYRT-------LSGGEQQRVQLARVLaqlwppVPSGRWLFL 165
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2468698279 667 DDATSALDANSQLQVEQLLYespELYSR--SVLLITQHLSLVEQ-ADHILFLEGGTIREGGTHQQ 728
Cdd:COG4559   166 DEPTSALDIAHQHHTLRLAR---QLAREggAVLAVLHDLNLAAQyADRIVLLHQGRVIASGSPQD 227
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
503-729 4.21e-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: 101.04  E-value: 4.21e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPNRPdVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLpqYEHRYLHRQVa 582
Cdd:cd03263     1 LQIRNLTKTYKKGT-KPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI--RTDRKAARQS- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 583 aVGQEPQvfGRSL------QENIAY-----GLTQKPTMEEITAAAVKsgahsfiSGLPQGYDTEVGeagsQLSGGQRQAV 651
Cdd:cd03263    77 -LGYCPQ--FDALfdeltvREHLRFyarlkGLPKSEIKEEVELLLRV-------LGLTDKANKRAR----TLSGGMKRKL 142
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2468698279 652 ALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPElySRSVLLITQHLSLVEQ-ADHILFLEGGTIREGGTHQQL 729
Cdd:cd03263   143 SLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
520-729 4.59e-24

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 104.40  E-value: 4.59e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRylHRQVAAVGQEPQVFGR-SLQEN 598
Cdd:PRK10851   17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHAR--DRKVGFVFQHYALFRHmTVFDN 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 599 IAYGLTQKPTMEEITAAAVKSGAHSFI-----SGLPQGYDtevgeagSQLSGGQRQAVALARALIRKPCVLILDDATSAL 673
Cdd:PRK10851   95 IAFGLTVLPRRERPNAAAIKAKVTQLLemvqlAHLADRYP-------AQLSGGQKQRVALARALAVEPQILLLDEPFGAL 167
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2468698279 674 DANSQLQVEQLLYE-SPELYSRSVLLITQHLSLVEQADHILFLEGGTIREGGTHQQL 729
Cdd:PRK10851  168 DAQVRKELRRWLRQlHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
503-720 5.32e-24

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


Pssm-ID: 213265 [Multi-domain]  Cd Length: 211  Bit Score: 100.65  E-value: 5.32e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPNRPDVLVLqgltfTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRylHRQVA 582
Cdd:cd03298     1 VRLDKIRFSYGEQPMHFDL-----TFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVS 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 583 AVGQEPQVFGR-SLQENIAYGLTQKPTMEEITAAAVKSGAHSFisGLpQGYDTEVGEagsQLSGGQRQAVALARALIRKP 661
Cdd:cd03298    74 MLFQENNLFAHlTVEQNVGLGLSPGLKLTAEDRQAIEVALARV--GL-AGLEKRLPG---ELSGGERQRVALARVLVRDK 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 662 CVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQ-ADHILFLEGGTI 720
Cdd:cd03298   148 PVLLLDEPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRI 207
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
497-723 8.72e-24

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: 100.59  E-value: 8.72e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 497 LHLEGLVqfqdVSFAypnrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQY-EHR 575
Cdd:cd03219     1 LEVRGLT----KRFG-----GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLpPHE 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 576 YLHRQVAAVGQEPQVFGR-SLQENIA--------YGLTQKPTMEEITAAAVKsgAHSFIS--GLPQGYDTEVGEagsqLS 644
Cdd:cd03219    72 IARLGIGRTFQIPRLFPElTVLENVMvaaqartgSGLLLARARREEREARER--AEELLErvGLADLADRPAGE----LS 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 645 GGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELySRSVLLITQHLSLVEQ-ADHILFLEGGT-IRE 722
Cdd:cd03219   146 YGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSlADRVTVLDQGRvIAE 224

                  .
gi 2468698279 723 G 723
Cdd:cd03219   225 G 225
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
507-724 9.13e-24

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 104.54  E-value: 9.13e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 507 DVSFAypnrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQVAAVGQ 586
Cdd:PRK09536   10 SVEFG-----DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQ 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 587 EPQV-FGRSLQENIAYG----LTQKPTMEEITAAAVKSGAHSfiSGLPQGYDTEVgeagSQLSGGQRQAVALARALIRKP 661
Cdd:PRK09536   85 DTSLsFEFDVRQVVEMGrtphRSRFDTWTETDRAAVERAMER--TGVAQFADRPV----TSLSGGERQRVLLARALAQAT 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2468698279 662 CVLILDDATSALDANSQLQVEQLLYESPElYSRSVLLITQHLSLVEQ-ADHILFLEGGTIREGG 724
Cdd:PRK09536  159 PVLLLDEPTASLDINHQVRTLELVRRLVD-DGKTAVAAIHDLDLAARyCDELVLLADGRVRAAG 221
ABC_6TM_TmrA_like cd18544
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ...
201-478 1.32e-23

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: 101.70  E-value: 1.32e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 201 EMAIPFFTGRLTDWILQDGSADTftRNLTLMSILTIASAVLEFVGDGIYN---NTMG-HVHSHLQGEVFGAVLRQETEFF 276
Cdd:cd18544    15 ELLGPLLIKRAIDDYIVPGQGDL--QGLLLLALLYLGLLLLSFLLQYLQTyllQKLGqRIIYDLRRDLFSHIQRLPLSFF 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 277 QQNQTGNITSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVT----LPLLFLLPKKVGKWYQll 352
Cdd:cd18544    93 DRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVlpllLLATYLFRKKSRKAYR-- 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 353 evQVRESLAK-SSQVAiEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGG 431
Cdd:cd18544   171 --EVREKLSRlNAFLQ-ESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELLSSLALALVLWYGG 247
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 2468698279 432 QLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18544   248 GQVLSGAVTLGVLYAFIQYIQRFFRPIRDLAEKFNILQSAMASAERI 294
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
502-734 2.02e-23

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


Pssm-ID: 226927 [Multi-domain]  Cd Length: 245  Bit Score: 99.80  E-value: 2.02e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYPnrPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYlHRQV 581
Cdd:COG4555     1 MLEVTDLTKSYG--SKVQAVRDVSFEAEEGEITGLLGENGAGKTTLLRMIATLLIPDSGKVTIDGVDTVRDPSFV-RRKI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 582 AAVGQEPQVFGR-SLQENIAY-----GLTQKpTMEEITAAAVKSgahsfiSGLPQGYDTEVGEagsqLSGGQRQAVALAR 655
Cdd:COG4555    78 GVLFGERGLYARlTARENLKYfarlnGLSRK-EIKARIAELSKR------LQLLEYLDRRVGE----FSTGMKQKVAIAR 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 656 ALIRKPCVLILDDATSALDANSQLQVEQLLYESPElYSRSVLLITQHLSLVEQ-ADHILFLEGGTIREGGTHQQLMEKKG 734
Cdd:COG4555   147 ALVHDPSILVLDEPTSGLDIRTRRKFHDFIKQLKN-EGRAVIFSSHIMQEVEAlCDRVIVLHKGEVVLEGSIEALDARTV 225
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
515-725 2.12e-23

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 100.25  E-value: 2.12e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 515 RPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQVAAVGQEP------ 588
Cdd:PRK15112   23 RQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDPstslnp 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 589 -----QVFGRSLQENIAygLTQKPTMEEITAAAVKSGAhsfisgLPQgydtEVGEAGSQLSGGQRQAVALARALIRKPCV 663
Cdd:PRK15112  103 rqrisQILDFPLRLNTD--LEPEQREKQIIETLRQVGL------LPD----HASYYPHMLAPGQKQRLGLARALILRPKV 170
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2468698279 664 LILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQ-ADHILFLEGGTIREGGT 725
Cdd:PRK15112  171 IIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGS 233
ABC_6TM_Tm288_like cd18547
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ...
203-478 3.89e-23

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: 100.17  E-value: 3.89e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 203 AIPFFTGRLTDWILQDGSA------DTFTRNLTLMSILTIASAVLEFvgdgIYNNTMGHVhshlqgeVFGAV--LRQETE 274
Cdd:cd18547    17 LGPYLLGKAIDLIIEGLGGgggvdfSGLLRILLLLLGLYLLSALFSY----LQNRLMARV-------SQRTVydLRKDLF 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 275 ---------FFQQNQTGNITSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKV 345
Cdd:cd18547    86 eklqrlplsYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLLVTKFI 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 346 GKWYQLLEVQVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQK-EAVAYAVNSWTTSISGMLLkV 424
Cdd:cd18547   166 AKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFKaQFYSGLLMPIMNFINNLGY-V 244
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2468698279 425 GILYIGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18547   245 LVAVVGGLLVINGALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAGAERV 298
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
515-712 3.91e-23

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 101.19  E-value: 3.91e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 515 RPDVLV--LQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEH---RYLHRQVAAVGQEP- 588
Cdd:PRK11308   23 KPERLVkaLDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPeaqKLLRQKIQIVFQNPy 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 589 ------QVFGRSLQENIAYGltqkptmEEITAAAVKSGAHSFIS--GL-PQGYDtevgEAGSQLSGGQRQAVALARALIR 659
Cdd:PRK11308  103 gslnprKKVGQILEEPLLIN-------TSLSAAERREKALAMMAkvGLrPEHYD----RYPHMFSGGQRQRIAIARALML 171
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2468698279 660 KPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEqadHI 712
Cdd:PRK11308  172 DPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVE---HI 221
ProV COG4175
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ...
518-729 4.01e-23

ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];


Pssm-ID: 226643 [Multi-domain]  Cd Length: 386  Bit Score: 102.07  E-value: 4.01e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 518 VLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGK---PLPQYEHRYLHR-QVAAVGQEpqvFG- 592
Cdd:COG4175    41 VVGVNDASLDVEEGEIFVIMGLSGSGKSTLVRLLNRLIEPTRGEILVDGKdiaKLSAAELRELRRkKISMVFQS---FAl 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 593 ---RSLQENIAYGLT---------QKPTMEEITAAAVKSGAHSFISglpqgydtevgeagsQLSGGQRQAVALARALIRK 660
Cdd:COG4175   118 lphRTVLENVAFGLEvqgvpkaerEERALEALELVGLEGYADKYPN---------------ELSGGMQQRVGLARALAND 182
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2468698279 661 PCVLILDDATSALDA--NSQLQvEQLLYESPELySRSVLLITQHLslvEQA----DHILFLEGGTIREGGTHQQL 729
Cdd:COG4175   183 PDILLMDEAFSALDPliRTEMQ-DELLELQAKL-KKTIVFITHDL---DEAlrigDRIAIMKDGEIVQVGTPEEI 252
PLN03232 PLN03232
ABC transporter C family member; Provisional
369-734 4.58e-23

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 105.44  E-value: 4.58e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279  369 EALSAMPTVRSFANEegeaQKFREKLQEIK----TLNQKEAVAYAVNSW---TTSISGMLLKVGI-LYIGGQLVTSGAVS 440
Cdd:PLN03232   484 EILASMDTVKCYAWE----KSFESRIQGIRneelSWFRKAQLLSAFNSFilnSIPVVVTLVSFGVfVLLGGDLTPARAFT 559
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279  441 SGNLVTFVLYQMQ-----FTQAVEVLLSIyPRVQKAVGSSEKIfeyLDRTPRCPPSgllTPLhleglVQFQDVSFAYPNR 515
Cdd:PLN03232   560 SLSLFAVLRSPLNmlpnlLSQVVNANVSL-QRIEELLLSEERI---LAQNPPLQPG---APA-----ISIKNGYFSWDSK 627
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279  516 PDVLVLQGLTFTLRPGEVTALVGPNGSGK-STVAALLQNLYQPTEGQLLLDGkplpqyehrylhrQVAAVGQEPQVFGRS 594
Cdd:PLN03232   628 TSKPTLSDINLEIPVGSLVAIVGGTGEGKtSLISAMLGELSHAETSSVVIRG-------------SVAYVPQVSWIFNAT 694
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279  595 LQENIAYGLTQKPtmeEITAAAVKSGAHSFISGLPQGYD-TEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATSAL 673
Cdd:PLN03232   695 VRENILFGSDFES---ERYWRAIDVTALQHDLDLLPGRDlTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSAL 771
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2468698279  674 DANSQLQVeqllYES---PELYSRSVLLITQHLSLVEQADHILFLEGGTIREGGT----------HQQLMEKKG 734
Cdd:PLN03232   772 DAHVAHQV----FDScmkDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTfaelsksgslFKKLMENAG 841
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
518-722 6.52e-23

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


Pssm-ID: 226647 [Multi-domain]  Cd Length: 228  Bit Score: 97.86  E-value: 6.52e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 518 VLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEH----RYLHRQVAAVGQEPQVFGR 593
Cdd:COG4181    23 LSILKGVELVVKRGETVAIVGPSGSGKSTLLAVLAGLDDPSSGEVRLLGQPLHKLDEdaraALRARHVGFVFQSFHLIPN 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 594 -SLQENIAYGLTqkptMEEITAAAVKSGAHSFISGLpqGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATSA 672
Cdd:COG4181   103 lTALENVALPLE----LRGESSADSRAGAKALLEAV--GLGKRLTHYPAQLSGGEQQRVALARAFAGRPDVLFADEPTGN 176
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2468698279 673 LDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQADHILFLEGGTIRE 722
Cdd:COG4181   177 LDRATGDKIADLLFALNRERGTTLVLVTHDPQLAARCDRQLRLRSGRLVE 226
ABC_6TM_exporter_like cd18563
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
201-478 7.26e-23

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: 99.51  E-value: 7.26e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 201 EMAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSH----LQGEVFGAVLRQETEFF 276
Cdd:cd18563    15 GLVPPYLTKILIDDVLIQLGPGGNTSLLLLLVLGLAGAYVLSALLGILRGRLLARLGERitadLRRDLYEHLQRLSLSFF 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 277 QQNQTGNITSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEVQV 356
Cdd:cd18563    95 DKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVVWGSYFFWKKIRRLFHRQ 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 357 RESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEI----KTLNQKEAVAYAVNSWTTSISGMLlkvgILYIGGQ 432
Cdd:cd18563   175 WRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELldanIRAEKLWATFFPLLTFLTSLGTLI----VWYFGGR 250
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 2468698279 433 LVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18563   251 QVLSGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRALTSAERI 296
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
525-674 7.95e-23

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 97.73  E-value: 7.95e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 525 TFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKplpqyEHRYL---HRQVAAVGQEPQVFGR-SLQENIA 600
Cdd:PRK10771   19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQ-----DHTTTppsRRPVSMLFQENNLFSHlTVAQNIG 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 601 YGL--------TQKPTMEEItaaAVKSGAHSFISGLPqgydtevgeagSQLSGGQRQAVALARALIRKPCVLILDDATSA 672
Cdd:PRK10771   94 LGLnpglklnaAQREKLHAI---ARQMGIEDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEPFSA 159

                  ..
gi 2468698279 673 LD 674
Cdd:PRK10771  160 LD 161
ABCC_SUR2 cd03288
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...
487-742 8.21e-23

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: 98.44  E-value: 8.21e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 487 RCPPSGLLTplhLEGLVQFQDVSFAYPN--RPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLL 564
Cdd:cd03288     7 GSSNSGLVG---LGGEIKIHDLCVRYENnlKP---VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 565 DGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQENI--AYGLTQKPTMEEITAAAVKSgahsFISGLPQGYDTEVGEAGSQ 642
Cdd:cd03288    81 DGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLdpECKCTDDRLWEALEIAQLKN----MVKSLPGGLDAVVTEGGEN 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 643 LSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESpeLYSRSVLLITQHLSLVEQADHILFLEGGTIRE 722
Cdd:cd03288   157 FSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTA--FADRTVVTIAHRVSTILDADLVLVLSRGILVE 234
                         250       260
                  ....*....|....*....|.
gi 2468698279 723 GGTHQQLMEKK-GCYWAMVQA 742
Cdd:cd03288   235 CDTPENLLAQEdGVFASLVRT 255
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
520-729 9.03e-23

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 98.28  E-value: 9.03e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQL-----LLDG-KPLPQYEH--RYLHRQVAAVGQEPQVF 591
Cdd:PRK11264   18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgdiTIDTaRSLSQQKGliRQLRQHVGFVFQNFNLF 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 592 -GRSLQENIAYG--LTQKPTMEEITAAAVKSGAHSFISGLPQGYDtevgeagSQLSGGQRQAVALARALIRKPCVLILDD 668
Cdd:PRK11264   98 pHRTVLENIIEGpvIVKGEPKEEATARARELLAKVGLAGKETSYP-------RRLSGGQQQRVAIARALAMRPEVILFDE 170
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2468698279 669 ATSALDANSQLQV----EQLLYEspelySRSVLLITQHLSLV-EQADHILFLEGGTIREGGTHQQL 729
Cdd:PRK11264  171 PTSALDPELVGEVlntiRQLAQE-----KRTMVIVTHEMSFArDVADRAIFMDQGRIVEQGPAKAL 231
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
502-733 1.19e-22

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


Pssm-ID: 223562 [Multi-domain]  Cd Length: 530  Bit Score: 102.33  E-value: 1.19e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKP----LPQYEHRYL 577
Cdd:COG0488     3 MITLENLSLAYGDRP---LLENVSLTLNPGERIGLVGRNGAGKSTLLKILAGELEPDSGEVTRPKGLrvgyLSQEPPLDP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 578 HRQV-----AAVGQEPQVFGRSLQENIAYGLTQKPTMEEITAAAVKSGAHSFIS---------GLPQgYDTEVGEagsqL 643
Cdd:COG0488    80 EKTVldyviEGFGELRELLAELEEAYALLADPDDELLAELEALLEELDGWTLEAraeeallglGFPD-EDRPVSS----L 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 644 SGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYEspelYSRSVLLIT--QHLsLVEQADHILFLEGGTIR 721
Cdd:COG0488   155 SGGWRRRVALARALLEEPDLLLLDEPTNHLDLESIEWLEDYLKR----YPGTVIVVShdRYF-LDNVATHILELDRGKLT 229
                         250
                  ....*....|...
gi 2468698279 722 E-GGTHQQLMEKK 733
Cdd:COG0488   230 PyKGNYSSYLEQK 242
cbiO PRK13644
energy-coupling factor transporter ATPase;
502-730 1.27e-22

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 98.52  E-value: 1.27e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYPNrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEH-RYLHRQ 580
Cdd:PRK13644    1 MIRLENVSYSYPD--GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKlQGIRKL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 581 VAAVGQEP--QVFGRSLQENIAYG---LTQKPT--MEEITAAAVKSGAHSFISGLPQgydtevgeagsQLSGGQRQAVAL 653
Cdd:PRK13644   79 VGIVFQNPetQFVGRTVEEDLAFGpenLCLPPIeiRKRVDRALAEIGLEKYRHRSPK-----------TLSGGQGQCVAL 147
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2468698279 654 ARALIRKPCVLILDDATSALDANSQLQVEQLLYESPElYSRSVLLITQHLSLVEQADHILFLEGGTIREGGTHQQLM 730
Cdd:PRK13644  148 AGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHE-KGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVL 223
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
520-732 1.43e-22

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: 97.02  E-value: 1.43e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGK---PLPQYEhrylhRQVAAVGQEPQVFGR-SL 595
Cdd:cd03299    14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKditNLPPEK-----RDISYVPQNYALFPHmTV 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 596 QENIAYGLTQKPTMEEITAAAVKSGAHSF-ISGLPQGYDTevgeagsQLSGGQRQAVALARALIRKPCVLILDDATSALD 674
Cdd:cd03299    89 YKNIAYGLKKRKVDKKEIERKVLEIAEMLgIDHLLNRKPE-------TLSGGEQQRVAIARALVVNPKILLLDEPFSALD 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2468698279 675 ANSQLQVEQLLYESPELYSRSVLLITQhlSLVEQ---ADHILFLEGGTIREGGTHQQLMEK 732
Cdd:cd03299   162 VRTKEKLREELKKIRKEFGVTVLHVTH--DFEEAwalADKVAIMLNGKLIQVGKPEEVFKK 220
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
518-746 1.59e-22

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


Pssm-ID: 213261 [Multi-domain]  Cd Length: 269  Bit Score: 97.71  E-value: 1.59e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 518 VLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYL----HRQVAAVGQEpqvFG- 592
Cdd:cd03294    37 TVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQS---FAl 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 593 ---RSLQENIAYGLT---------QKPTMEEITAAAVKSGAHSFISglpqgydtevgeagsQLSGGQRQAVALARALIRK 660
Cdd:cd03294   114 lphRTVLENVAFGLEvqgvpraerEERAAEALELVGLEGWEHKYPD---------------ELSGGMQQRVGLARALAVD 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 661 PCVLILDDATSALDA--NSQLQvEQLLYESPELySRSVLLITQHLS-LVEQADHILFLEGGTIREGGTHQQLmekkgcyw 737
Cdd:cd03294   179 PDILLMDEAFSALDPliRREMQ-DELLRLQAEL-QKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEI-------- 248

                  ....*....
gi 2468698279 738 amVQAPADA 746
Cdd:cd03294   249 --LTNPAND 255
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
503-735 2.56e-22

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 98.34  E-value: 2.56e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPnrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRqva 582
Cdd:PRK13537    8 IDFRNVEKRYG---DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQR--- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 583 aVGQEPQ---------------VFGRSlqeniaYGLTQKptmeeiTAAAVKSGAHSFiSGLPQGYDTEVGEagsqLSGGQ 647
Cdd:PRK13537   82 -VGVVPQfdnldpdftvrenllVFGRY------FGLSAA------AARALVPPLLEF-AKLENKADAKVGE----LSGGM 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 648 RQAVALARALIRKPCVLILDDATSALDAnsqlQVEQLLYESPE--LYSRSVLLITQHlsLVEQA----DHILFLEGG-TI 720
Cdd:PRK13537  144 KRRLTLARALVNDPDVLVLDEPTTGLDP----QARHLMWERLRslLARGKTILLTTH--FMEEAerlcDRLCVIEEGrKI 217
                         250
                  ....*....|....*
gi 2468698279 721 REGGTHQQLMEKKGC 735
Cdd:PRK13537  218 AEGAPHALIESEIGC 232
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
489-735 2.79e-22

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 98.75  E-value: 2.79e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 489 PPSGLLTPLHLEglvqFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKP 568
Cdd:PRK13536   32 SIPGSMSTVAID----LAGVSKSYGDKA---VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVP 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 569 LPQyEHRYLHRQVAAVGQ----EPQVfgrSLQEN-IAYGLTQKPTMEEItaAAVKSGAHSFiSGLPQGYDTEVgeagSQL 643
Cdd:PRK13536  105 VPA-RARLARARIGVVPQfdnlDLEF---TVRENlLVFGRYFGMSTREI--EAVIPSLLEF-ARLESKADARV----SDL 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 644 SGGQRQAVALARALIRKPCVLILDDATSALDANSQlqveQLLYESpelySRSVL------LITQHlsLVEQA----DHIL 713
Cdd:PRK13536  174 SGGMKRRLTLARALINDPQLLILDEPTTGLDPHAR----HLIWER----LRSLLargktiLLTTH--FMEEAerlcDRLC 243
                         250       260
                  ....*....|....*....|...
gi 2468698279 714 FLEGG-TIREGGTHQQLMEKKGC 735
Cdd:PRK13536  244 VLEAGrKIAEGRPHALIDEHIGC 266
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
503-731 3.33e-22

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 96.64  E-value: 3.33e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLqNLYQPTEGQLLLDGKP--LPQ--YEHRY-- 576
Cdd:PRK14258    8 IKVNNLSFYYDTQK---ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNELESEVRVEGRVefFNQniYERRVnl 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 577 --LHRQVAAVGQEPQVFGRSLQENIAYGLT-----QKPTMEEITAAAVKSgahsfiSGLPQGYDTEVGEAGSQLSGGQRQ 649
Cdd:PRK14258   84 nrLRRQVSMVHPKPNLFPMSVYDNVAYGVKivgwrPKLEIDDIVESALKD------ADLWDEIKHKIHKSALDLSGGQQQ 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 650 AVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQ-ADHILFLEGGTIREGgthqQ 728
Cdd:PRK14258  158 RLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRlSDFTAFFKGNENRIG----Q 233

                  ...
gi 2468698279 729 LME 731
Cdd:PRK14258  234 LVE 236
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
520-723 3.34e-22

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: 94.93  E-value: 3.34e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALL--QNLYQPTEGQLLLDGKPLPQYEHRylhRQVAAVGQEPQVFGR-SLQ 596
Cdd:cd03213    24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLDKRSFR---KIIGYVPQDDILHPTlTVR 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 597 ENIAYgltqkptmeeitAAAVKSgahsfisglpqgydtevgeagsqLSGGQRQAVALARALIRKPCVLILDDATSALDAN 676
Cdd:cd03213   101 ETLMF------------AAKLRG-----------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSS 145
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2468698279 677 SQLQVEQLLYESPELySRSVLLITQHLS--LVEQADHILFL-EGGTIREG 723
Cdd:cd03213   146 SALQVMSLLRRLADT-GRTIICSIHQPSseIFELFDKLLLLsQGRVIYFG 194
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
502-734 5.85e-22

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


Pssm-ID: 223562 [Multi-domain]  Cd Length: 530  Bit Score: 100.40  E-value: 5.85e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYPNRPdvLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLdGKPLPQYehrYLHRQV 581
Cdd:COG0488   321 VLEFENVSKGYDGGR--LLLKDLSFRIDRGDRIAIVGPNGAGKSTLLKLLAGELGPLSGTVKV-GETVKIG---YFDQHR 394
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 582 AAVGQEpqvfgRSLQENIAYGLTQKPTMEeitaaaVKSGAHSFisGLPQgydTEVGEAGSQLSGGQRQAVALARALIRKP 661
Cdd:COG0488   395 DELDPD-----KTVLEELSEGFPDGDEQE------VRAYLGRF--GFTG---EDQEKPVGVLSGGEKARLLLAKLLLQPP 458
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2468698279 662 CVLILDDATSALDANSQLQVEQLLYEspelYSRSVLLITQHLSLVEQ-ADHILFLEGGTIREGGTHQQLMEKKG 734
Cdd:COG0488   459 NLLLLDEPTNHLDIESLEALEEALLD----FEGTVLLVSHDRYFLDRvATRIWLVEDKVEEFEGGYEDYLEQKK 528
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
520-676 7.69e-22

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 97.87  E-value: 7.69e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLpqyEHRYL-HRQVAAVGQEPQVFGR-SLQE 597
Cdd:PRK11432   21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDV---THRSIqQRDICMVFQSYALFPHmSLGE 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 598 NIAYGL-TQKPTMEEITAAAVKSGAHSFISGLPQGY-DtevgeagsQLSGGQRQAVALARALIRKPCVLILDDATSALDA 675
Cdd:PRK11432   98 NVGYGLkMLGVPKEERKQRVKEALELVDLAGFEDRYvD--------QISGGQQQRVALARALILKPKVLLFDEPLSNLDA 169

                  .
gi 2468698279 676 N 676
Cdd:PRK11432  170 N 170
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
502-733 9.01e-22

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 96.07  E-value: 9.01e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYPNRPDVLvlQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLpQYEHR---YLH 578
Cdd:PRK13636    5 ILKVEELNYNYSDGTHAL--KGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKglmKLR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 579 RQVAAVGQEP--QVFGRSLQENIAYG-----LTQKPTMEEITAAAVKSGahsfISGLPQgydtevgEAGSQLSGGQRQAV 651
Cdd:PRK13636   82 ESVGMVFQDPdnQLFSASVYQDVSFGavnlkLPEDEVRKRVDNALKRTG----IEHLKD-------KPTHCLSFGQKKRV 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 652 ALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVE-QADHILFL-EGGTIREGGTHQQL 729
Cdd:PRK13636  151 AIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPlYCDNVFVMkEGRVILQGNPKEVF 230

                  ....
gi 2468698279 730 MEKK 733
Cdd:PRK13636  231 AEKE 234
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
503-724 1.24e-21

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: 93.44  E-value: 1.24e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPlPQYEHRYLhRQVA 582
Cdd:cd03268     1 LKTNDLTKTYGKKR---VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKS-YQKNIEAL-RRIG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 583 AVGQEPQVFG-RSLQENI-----AYGLTQKPTMEEITaaavksgahsfISGLPQGYDTEVGeagsQLSGGQRQAVALARA 656
Cdd:cd03268    76 ALIEAPGFYPnLTARENLrllarLLGIRKKRIDEVLD-----------VVGLKDSAKKKVK----GFSLGMKQRLGIALA 140
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2468698279 657 LIRKPCVLILDDATSALDANSQLQVEQLLYESPElYSRSVLLITQHLSLVEQ-ADHILFLEGGTIREGG 724
Cdd:cd03268   141 LLGNPDLLILDEPTNGLDPDGIKELRELILSLRD-QGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
TauB COG4525
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
508-721 1.27e-21

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


Pssm-ID: 226905 [Multi-domain]  Cd Length: 259  Bit Score: 94.82  E-value: 1.27e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 508 VSFAYPNRPdVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPL--PQYEHrylhrqvAAVG 585
Cdd:COG4525     9 LSLSYEGKP-RSALEDVSLTIASGELVVVLGPSGCGKTTLLNLIAGFVTPSRGSIQLNGRRIegPGAER-------GVVF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 586 QEPQVFG-RSLQENIAYGLtQKPTMEEITAAAVksgAHSFISglpqgydtEVGEAGS------QLSGGQRQAVALARALI 658
Cdd:COG4525    81 QNEALLPwLNVIDNVAFGL-QLRGIEKAQRREI---AHQMLA--------LVGLEGAehkyiwQLSGGMRQRVGIARALA 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2468698279 659 RKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHL-SLVEQADHILFLEGGTIR 721
Cdd:COG4525   149 VEPQLLLLDEPFGALDALTREQMQELLLDLWQETGKQVLLITHDIeEALFLATRLVVLSPGPGR 212
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
502-682 1.36e-21

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 97.33  E-value: 1.36e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRylHRQV 581
Cdd:PRK09452   14 LVELRGISKSFDGKE---VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHV 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 582 AAVGQEPQVFGR-SLQENIAYGL-TQKPTMEEITaaavksgahsfisglpqgydTEVGEA-------------GSQLSGG 646
Cdd:PRK09452   89 NTVFQSYALFPHmTVFENVAFGLrMQKTPAAEIT--------------------PRVMEAlrmvqleefaqrkPHQLSGG 148
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2468698279 647 QRQAVALARALIRKPCVLILDDATSALDAN--SQLQVE 682
Cdd:PRK09452  149 QQQRVAIARAVVNKPKVLLLDESLSALDYKlrKQMQNE 186
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
499-731 1.77e-21

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 94.85  E-value: 1.77e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 499 LEGLVQFQDVSFAYPNRpdvLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQ--PT---EGQLLLDGKPL--PQ 571
Cdd:PRK14243    7 TETVLRTENLNVYYGSF---LAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGfrvEGKVTFHGKNLyaPD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 572 YEHRYLHRQVAAVGQEPQVFGRSLQENIAYG---LTQKPTMEEITAAAVKSGAhsfisgLPQGYDTEVGEAGSQLSGGQR 648
Cdd:PRK14243   84 VDPVEVRRRIGMVFQKPNPFPKSIYDNIAYGariNGYKGDMDELVERSLRQAA------LWDEVKDKLKQSGLSLSGGQQ 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 649 QAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYsrSVLLITQHLslvEQA----DHILFLEGGTIREGG 724
Cdd:PRK14243  158 QRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQY--TIIIVTHNM---QQAarvsDMTAFFNVELTEGGG 232

                  ....*..
gi 2468698279 725 THQQLME 731
Cdd:PRK14243  233 RYGYLVE 239
PTZ00243 PTZ00243
ABC transporter; Provisional
485-742 1.84e-21

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 100.24  E-value: 1.84e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279  485 TPRCPPSGLLTPLHLEGLVqFQDVSFAYpnRPDV-LVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLL 563
Cdd:PTZ00243  1292 EPASPTSAAPHPVQAGSLV-FEGVQMRY--REGLpLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIR 1368
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279  564 LDGKPLPQYEHRYLHRQVAAVGQEPQVFGRSLQENIAYGLTQKPtmEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQL 643
Cdd:PTZ00243  1369 VNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVDPFLEASS--AEVWAALELVGLRERVASESEGIDSRVLEGGSNY 1446
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279  644 SGGQRQAVALARALIRKPCVLIL-DDATSALDANSQLQVEQLLYESPELYsrSVLLITQHLSLVEQADHILFLEGGTIRE 722
Cdd:PTZ00243  1447 SVGQRQLMCMARALLKKGSGFILmDEATANIDPALDRQIQATVMSAFSAY--TVITIAHRLHTVAQYDKIIVMDHGAVAE 1524
                          250       260
                   ....*....|....*....|.
gi 2468698279  723 GGTHQQL-MEKKGCYWAMVQA 742
Cdd:PTZ00243  1525 MGSPRELvMNRQSIFHSMVEA 1545
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
503-724 3.18e-21

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: 92.64  E-value: 3.18e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPNRpdvLVLQGLTFTLRPGeVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEhRYLHRQVA 582
Cdd:cd03264     1 LQLENLTKRYGKK---RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQP-QKLRRRIG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 583 AVGQEPQVFGR-SLQENIAYgltqKPTMEEITAAAVKSGAHSFIS--GLPQGYDTEVGeagsQLSGGQRQAVALARALIR 659
Cdd:cd03264    76 YLPQEFGVYPNfTVREFLDY----IAWLKGIPSKEVKARVDEVLElvNLGDRAKKKIG----SLSGGMRRRVGIAQALVG 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2468698279 660 KPCVLILDDATSALDANSQLQVEQLLYESPElySRSVLLITQHLSLVEQ-ADHILFLEGGTIREGG 724
Cdd:cd03264   148 DPSILIVDEPTAGLDPEERIRFRNLLSELGE--DRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
ABC_6TM_TmrB_like cd18541
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ...
202-455 4.00e-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: 4.00e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 202 MAIPFFTGRLTDwILQDGSADTftRNLTLMSILTIASAVLEFVGDGIYNNT-MG---HVHSHLQGEVFGAVLRQETEFFQ 277
Cdd:cd18541    16 LLIPRIIGRAID-ALTAGTLTA--SQLLRYALLILLLALLIGIFRFLWRYLiFGasrRIEYDLRNDLFAHLLTLSPSFYQ 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 278 QNQTGNITSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEVQVR 357
Cdd:cd18541    93 KNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLVYRLGKKIHKRFRKVQ 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 358 ESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVayaVNSWTTSISGMLLKVG---ILYIGGQLV 434
Cdd:cd18541   173 EAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLAR---VDALFFPLIGLLIGLSfliVLWYGGRLV 249
                         250       260
                  ....*....|....*....|.
gi 2468698279 435 TSGAVSSGNLVTFVLYQMQFT 455
Cdd:cd18541   250 IRGTITLGDLVAFNSYLGMLI 270
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
507-729 4.30e-21

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 93.57  E-value: 4.30e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 507 DVSFAYPNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQ------PTEGQLLLDGKPLPQYEHRYLHRQ 580
Cdd:PRK14246   12 NISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIKLRKE 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 581 VAAVGQEPQVFGR-SLQENIAY-----GLTQKPTMEEITAAAVKSgahsfiSGLPQGYDTEVGEAGSQLSGGQRQAVALA 654
Cdd:PRK14246   92 VGMVFQQPNPFPHlSIYDNIAYplkshGIKEKREIKKIVEECLRK------VGLWKEVYDRLNSPASQLSGGQQQRLTIA 165
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2468698279 655 RALIRKPCVLILDDATSALDANSQLQVEQLLyesPELYSRSVLLITQH--LSLVEQADHILFLEGGTIREGGTHQQL 729
Cdd:PRK14246  166 RALALKPKVLLMDEPTSMIDIVNSQAIEKLI---TELKNEIAIVIVSHnpQQVARVADYVAFLYNGELVEWGSSNEI 239
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
504-732 5.62e-21

ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism, Cell wall/membrane/envelope biogenesis];


Pssm-ID: 224057 [Multi-domain]  Cd Length: 249  Bit Score: 92.68  E-value: 5.62e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 504 QFQDVSFAYPNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEhrylhrqvAA 583
Cdd:COG1134    26 RLKGLAKGGRKVAEFWALKDISFEIYKGERVGIIGHNGAGKSTLLKLIAGIYKPTSGKVKVTGKVAPLIE--------LG 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 584 VGQEPQVFGRslqENIA-----YGLTQKPT---MEEITAAAvksgahsfisglpqgydtEVGEAGSQ----LSGGQRQAV 651
Cdd:COG1134    98 AGFDPELTGR---ENIYlrgliLGLTRKEIdekVDEIIEFA------------------ELGDFIDQpvktYSSGMYARL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 652 ALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPElYSRSVLLITQHLSLVEQA-DHILFLEGGTIREGGTHQQLM 730
Cdd:COG1134   157 AFSVATHVEPDILLLDEVLAVGDAAFQEKCLERLNELVE-KNKTIVLVSHDLGAIKQYcDRAIWLEHGQIRMEGSPEEVI 235

                  ..
gi 2468698279 731 EK 732
Cdd:COG1134   236 PA 237
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only] ...
509-734 9.11e-21

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


Pssm-ID: 226952 [Multi-domain]  Cd Length: 325  Bit Score: 93.99  E-value: 9.11e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 509 SFAYPNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKpLPQYEHRYLHRQVAAVgqep 588
Cdd:COG4586    28 HFFHRKERSIEAVQDISFEIPKGEIVGFLGANGAGKSTTLKMLTGLLLPTSGKVRVNGK-DPFRRREEYLRSIGLV---- 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 589 qvFGRSLQenIAYGLTQKPTME------EITAAAVKSGAHSFISGLpqGYDTEVGEAGSQLSGGQRQAVALARALIRKPC 662
Cdd:COG4586   103 --MGQKLQ--LWWDLPALDSLEvlkliyEIPDDEFAERLDFLTEIL--DLEGFLKWPVRKLSLGQRMRAELAAALLHPPK 176
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2468698279 663 VLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQ-ADHILFLEGGTIREGGTHQQLMEKKG 734
Cdd:COG4586   177 VLFLDEPTVGLDVNAQANIREFLKEYNEERQATVLLTTHIFDDIATlCDRVLLIDQGQLVFDGTLAQLQEQFG 249
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
503-719 1.00e-20

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: 89.04  E-value: 1.00e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKplpqyehrylhrqva 582
Cdd:cd03221     1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST--------------- 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 583 avgqepqvfgrslqENIAYgltqkptmeeitaaavksgahsFisglpqgydtevgeagSQLSGGQRQAVALARALIRKPC 662
Cdd:cd03221    63 --------------VKIGY----------------------F----------------EQLSGGEKMRLALAKLLLENPN 90
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2468698279 663 VLILDDATSALDANSQLQVEQLLYEspelYSRSVLLITQHLSLVEQ-ADHILFLEGGT 719
Cdd:cd03221    91 LLLLDEPTNHLDLESIEALEEALKE----YPGTVILVSHDRYFLDQvATKIIELEDGK 144
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
517-724 1.22e-20

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 91.90  E-value: 1.22e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 517 DVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQ-----PTEGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQ-V 590
Cdd:PRK14247   15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPNpI 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 591 FGRSLQENIAYGL-------TQKPTMEEITAAAVKSGahsfisgLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCV 663
Cdd:PRK14247   95 PNLSIFENVALGLklnrlvkSKKELQERVRWALEKAQ-------LWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEV 167
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2468698279 664 LILDDATSALDANSQLQVEQLLYESPElySRSVLLITQHLSLVEQ-ADHILFLEGGTIREGG 724
Cdd:PRK14247  168 LLADEPTANLDPENTAKIESLFLELKK--DMTIVLVTHFPQQAARiSDYVAFLYKGQIVEWG 227
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
519-719 1.55e-20

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


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 91.59  E-value: 1.55e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 519 LVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKP---LP-----------QYEHRYLHRQVAA- 583
Cdd:PRK11300   19 LAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHiegLPghqiarmgvvrTFQHVRLFREMTVi 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 584 ----VGQEpqvfgRSLQENIAYGLTQKPTMEEITAAAVKSGAHSF-ISGLpqgydTEVG--EAGSqLSGGQRQAVALARA 656
Cdd:PRK11300   99 enllVAQH-----QQLKTGLFSGLLKTPAFRRAESEALDRAATWLeRVGL-----LEHAnrQAGN-LAYGQQRRLEIARC 167
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2468698279 657 LIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLV-EQADHILFLEGGT 719
Cdd:PRK11300  168 MVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVmGISDRIYVVNQGT 231
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
502-724 1.73e-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: 90.50  E-value: 1.73e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAY-PNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQyEHRYLHRQ 580
Cdd:cd03266     1 MITADALTKRFrDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 581 VAAVGQEPQVFGR-SLQENIAY-----GLtqKPTmeEITaAAVKSGAHSFisGLPQGYDTEVGEagsqLSGGQRQAVALA 654
Cdd:cd03266    80 LGFVSDSTGLYDRlTARENLEYfaglyGL--KGD--ELT-ARLEELADRL--GMEELLDRRVGG----FSTGMRQKVAIA 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2468698279 655 RALIRKPCVLILDDATSALDANSQLQVEQLLYESPELySRSVLLITQHLSLVEQ-ADHILFLEGGTIREGG 724
Cdd:cd03266   149 RALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRAL-GKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
500-725 1.74e-20

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 92.07  E-value: 1.74e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 500 EGLVQFQDVSFAYPNRPD---VLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRY 576
Cdd:PRK13633    2 NEMIKCKNVSYKYESNEEsteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLW 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 577 LHRQVAA-VGQEP--QVFGRSLQENIAYG---LTQKPtmEEITA----AAVKSGAHSFISGLPQgydtevgeagsQLSGG 646
Cdd:PRK13633   82 DIRNKAGmVFQNPdnQIVATIVEEDVAFGpenLGIPP--EEIRErvdeSLKKVGMYEYRRHAPH-----------LLSGG 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2468698279 647 QRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQADHILFLEGGTIREGGT 725
Cdd:PRK13633  149 QKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGT 227
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
524-685 1.88e-20

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 94.13  E-value: 1.88e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 524 LTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPL---PQYEhrylhRQVAAVGQEPQVFGR-SLQENI 599
Cdd:PRK11607   38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLshvPPYQ-----RPINMMFQSYALFPHmTVEQNI 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 600 AYGLTQ-KPTMEEITA--AAVKSGAH--SFISGLPQgydtevgeagsQLSGGQRQAVALARALIRKPCVLILDDATSALD 674
Cdd:PRK11607  113 AFGLKQdKLPKAEIASrvNEMLGLVHmqEFAKRKPH-----------QLSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
                         170
                  ....*....|....*
gi 2468698279 675 AN----SQLQVEQLL 685
Cdd:PRK11607  182 KKlrdrMQLEVVDIL 196
PhnC COG3638
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ...
503-685 1.88e-20

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


Pssm-ID: 226164 [Multi-domain]  Cd Length: 258  Bit Score: 91.55  E-value: 1.88e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPNrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGK---PLPQYEHRYLHR 579
Cdd:COG3638     4 IEVKNLSKTYPG--GHQALKDVNLEINQGEMVAIIGPSGAGKSTLLRSLNGLVDPTSGEILFNGVqitKLKGKELRKLRR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 580 QVAAVGQEPQVFGR-SLQENIAYG-LTQKPTMeeitaaavksgaHSFIsGLP------QGYD--TEVG------EAGSQL 643
Cdd:COG3638    82 DIGMIFQQFNLVPRlSVLENVLLGrLGYTSTW------------RSLF-GLFskedkaQALDalERVGildkayQRASTL 148
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2468698279 644 SGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLL 685
Cdd:COG3638   149 SGGQQQRVAIARALVQQPKIILADEPVASLDPESAKKVMDIL 190
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
502-723 1.94e-20

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 90.70  E-value: 1.94e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYPNRPDVLvlQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHR---YLH 578
Cdd:PRK10908    1 MIRFEHVSKAYLGGRQAL--QGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNRevpFLR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 579 RQVAAVGQEPQVF-GRSLQENIAY-----GLTQKPTMEEITAAAVKSGAHSFISGLPqgydtevgeagSQLSGGQRQAVA 652
Cdd:PRK10908   79 RQIGMIFQDHHLLmDRTVYDNVAIpliiaGASGDDIRRRVSAALDKVGLLDKAKNFP-----------IQLSGGEQQRVG 147
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2468698279 653 LARALIRKPCVLILDDATSALDANSQLQVEQLLYEspelYSR---SVLLITQHLSLVEQADH-ILFLEGGTIREG 723
Cdd:PRK10908  148 IARAVVNKPAVLLADEPTGNLDDALSEGILRLFEE----FNRvgvTVLMATHDIGLISRRSYrMLTLSDGHLHGG 218
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
503-725 1.99e-20

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 93.33  E-value: 1.99e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYP-NRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQY---EHRYLH 578
Cdd:PRK11153    2 IELKNISKVFPqGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALsekELRKAR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 579 RQVAAVGQEpqvF----GRSLQENIAYGLTqkptMEEITAAAVKSGAHSFIS--GLPQGYDTevgeAGSQLSGGQRQAVA 652
Cdd:PRK11153   82 RQIGMIFQH---FnllsSRTVFDNVALPLE----LAGTPKAEIKARVTELLElvGLSDKADR----YPAQLSGGQKQRVA 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2468698279 653 LARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQ-ADHILFLEGGTIREGGT 725
Cdd:PRK11153  151 IARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRiCDRVAVIDAGRLVEQGT 224
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
503-721 2.52e-20

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


Pssm-ID: 213236 [Multi-domain]  Cd Length: 210  Bit Score: 90.03  E-value: 2.52e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPnrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLpQYEHRylHRqva 582
Cdd:cd03269     1 LEVENVTKRFG---RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL-DIAAR--NR--- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 583 aVGQEPQVFG----RSLQENIAY-----GLTQKPTMEEITAAAVKSGahsfISglpqGYDTEVGEagsQLSGGQRQAVAL 653
Cdd:cd03269    72 -IGYLPEERGlypkMKVIDQLVYlaqlkGLKKEEARRRIDEWLERLE----LS----EYANKRVE---ELSKGNQQKVQF 139
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2468698279 654 ARALIRKPCVLILDDATSALDANSQLQVEQLLYESPElYSRSVLLITQHLSLVEQ-ADHILFLEGGTIR 721
Cdd:cd03269   140 IAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELAR-AGKTVILSTHQMELVEElCDRVLLLNKGRAV 207
cbiO PRK13643
energy-coupling factor transporter ATPase;
502-732 2.85e-20

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 91.72  E-value: 2.85e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAY-PNRP-DVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQL----LLDGKPLPQYEHR 575
Cdd:PRK13643    1 MIKFEKVNYTYqPNSPfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdIVVSSTSKQKEIK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 576 YLHRQVAAVGQEP--QVFGRSLQENIAYGLTQ----KPTMEEITAAAVKSgahsfisglpQGYDTEVGEAGS-QLSGGQR 648
Cdd:PRK13643   81 PVRKKVGVVFQFPesQLFEETVLKDVAFGPQNfgipKEKAEKIAAEKLEM----------VGLADEFWEKSPfELSGGQM 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 649 QAVALARALIRKPCVLILDDATSALDANSQLQVEQlLYESPELYSRSVLLITQHL-SLVEQADHILFLEGGTIREGGTHQ 727
Cdd:PRK13643  151 RRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQ-LFESIHQSGQTVVLVTHLMdDVADYADYVYLLEKGHIISCGTPS 229

                  ....*
gi 2468698279 728 QLMEK 732
Cdd:PRK13643  230 DVFQE 234
ABC_6TM_YknV_like cd18545
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ...
202-478 3.19e-20

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: 91.76  E-value: 3.19e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 202 MAIPFFTGRLTDWILQDGSadtfTRNLTLMSILTIASAVLEFVGDGIYNNTMGHV------------HSHLQGEVFGavl 269
Cdd:cd18545    17 LAGPYLIKIAIDEYIPNGD----LSGLLIIALLFLALNLVNWVASRLRIYLMAKVgqrilydlrqdlFSHLQKLSFS--- 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 270 rqeteFFQQNQTGNITSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVT----LPLLFLLPKKV 345
Cdd:cd18545    90 -----FFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVlpllVLVVFLLRRRA 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 346 GKWYQllevQVRESLAK-SSQVAiEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKeavAYAVNSW---TTSISGML 421
Cdd:cd18545   165 RKAWQ----RVRKKISNlNAYLH-ESISGIRVIQSFAREDENEEIFDELNRENRKANMR---AVRLNALfwpLVELISAL 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2468698279 422 LKVGILYIGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18545   237 GTALVYWYGGKLVLGGAITVGVLVAFIGYVGRFWQPIRNLSNFYNQLQSAMASAERI 293
ABC_6TM_exporter_like cd18550
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
202-478 4.26e-20

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


Pssm-ID: 349994 [Multi-domain]  Cd Length: 294  Bit Score: 91.39  E-value: 4.26e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 202 MAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEfVGDGIYNNTMG-HVHSHLQGEVFGAVLRQETEFFQQNQ 280
Cdd:cd18550    16 LLPPLLLREIIDDALPQGDLGLLVLLALGMVAVAVASALLG-VVQTYLSARIGqGVMYDLRVQLYAHLQRMSLAFFTRTR 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 281 TGNITSRVTED--------TSTLSDSLSENLSLFLwylvrglcLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLL 352
Cdd:cd18550    95 TGEIQSRLNNDvggaqsvvTGTLTSVVSNVVTLVA--------TLVAMLALDWRLALLSLVLLPLFVLPTRRVGRRRRKL 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 353 EVQVRESLAKSSQVAIEALSA--MPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAyavNSWTTSISGMLLKVG---IL 427
Cdd:cd18550   167 TREQQEKLAELNSIMQETLSVsgALLVKLFGREDDEAARFARRSRELRDLGVRQALA---GRWFFAALGLFTAIGpalVY 243
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2468698279 428 YIGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18550   244 WVGGLLVIGGGLTIGTLVAFTALLGRLYGPLTQLLNIQVDLMTSLALFERI 294
ModF COG1119
ABC-type molybdenum transport system, ATPase component/photorepair protein PhrA [Inorganic ion ...
502-725 4.70e-20

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


Pssm-ID: 224044 [Multi-domain]  Cd Length: 257  Bit Score: 90.45  E-value: 4.70e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGkplpqyeHRYLHRQV 581
Cdd:COG1119    31 LIELKNVSVRRNGKK---ILGDLSWQVNPGEHWAIVGPNGAGKTTLLSLLTGEHPPSSGDVTLLG-------RRFGKGET 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 582 aavgqepqvfGRSLQENIAY-----GLTQKP--TMEEItaaaVKSGAHSFISGLPQGYD----------TEVGEAGS--- 641
Cdd:COG1119   101 ----------IFELRKRIGLvsselHERFRVreTVRDV----VLSGFFASIGIYQEDLTaedlaaaqwlLELLGAKHlad 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 642 ----QLSGGQRQAVALARALIRKPCVLILDDATSALD--ANSQLqVEQLLYESPELYSRSVLLITQHlslVEQA----DH 711
Cdd:COG1119   167 rpfgSLSQGEQRRVLIARALVKDPELLILDEPAQGLDliAREQL-LNRLEELAASPGAPALLFVTHH---AEEIppcfTH 242
                         250
                  ....*....|....
gi 2468698279 712 ILFLEGGTIREGGT 725
Cdd:COG1119   243 RLLLKEGEVVAQGK 256
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
507-681 5.35e-20

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 90.45  E-value: 5.35e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 507 DVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLpQYEHR---YLHRQVAA 583
Cdd:PRK13638    6 DLWFRYQDEP---VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL-DYSKRgllALRQQVAT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 584 VGQEP--QVFGRSLQENIAYGLTQKPTMEEITAAAVKSgAHSFISGlpQGYDTEVGEAgsqLSGGQRQAVALARALIRKP 661
Cdd:PRK13638   82 VFQDPeqQIFYTDIDSDIAFSLRNLGVPEAEITRRVDE-ALTLVDA--QHFRHQPIQC---LSHGQKKRVAIAGALVLQA 155
                         170       180
                  ....*....|....*....|
gi 2468698279 662 CVLILDDATSALDANSQLQV 681
Cdd:PRK13638  156 RYLLLDEPTAGLDPAGRTQM 175
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
509-720 5.52e-20

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: 89.70  E-value: 5.52e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 509 SFAYPNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKpLPqYEHR--YLHRQVAAVGQ 586
Cdd:cd03267    25 SLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL-VP-WKRRkkFLRRIGVVFGQ 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 587 EPQVF-------GRSLQENIaYGLTQ---KPTMEEITAAAvksgahsfisGLPQGYDTEVgeagSQLSGGQRQAVALARA 656
Cdd:cd03267   103 KTQLWwdlpvidSFYLLAAI-YDLPParfKKRLDELSELL----------DLEELLDTPV----RQLSLGQRMRAEIAAA 167
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2468698279 657 LIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQ-ADHILFLEGGTI 720
Cdd:cd03267   168 LLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEAlARRVLVIDKGRL 232
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
499-724 8.48e-20

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 90.18  E-value: 8.48e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 499 LEGLVQFQDVSFAYPNrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLH 578
Cdd:PRK13647    1 MDNIIEVEDLHFRYKD--GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 579 RQVAAVGQEP--QVFGRSLQENIAYG-----LTQKPTMEEITAAAVKSGAHSFISGLPQgydtevgeagsQLSGGQRQAV 651
Cdd:PRK13647   79 SKVGLVFQDPddQVFSSTVWDDVAFGpvnmgLDKDEVERRVEEALKAVRMWDFRDKPPY-----------HLSYGQKKRV 147
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2468698279 652 ALARALIRKPCVLILDDATSALDANSQLQVEQLLYespELYSR--SVLLITQHLSL-VEQADHILFL-EGGTIREGG 724
Cdd:PRK13647  148 AIAGVLAMDPDVIVLDEPMAYLDPRGQETLMEILD---RLHNQgkTVIVATHDVDLaAEWADQVIVLkEGRVLAEGD 221
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
503-720 1.25e-19

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: 88.48  E-value: 1.25e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPN-RPDVLVLQGLTFTLRPGEVTALVGPNGSGKST----VAALLQNLYQpTEGQLLLDGKPLpqyeHRYL 577
Cdd:cd03234     4 LPWWDVGLKAKNwNKYARILNDVSLHVESGQVMAILGSSGSGKTTlldaISGRVEGGGT-TSGQILFNGQPR----KPDQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 578 HRQVAAVGQEPQVFGRSL--QENIAYGLTQKptMEEITAAAVKSgAHSFISGLPQGYDTEVGEAG-SQLSGGQRQAVALA 654
Cdd:cd03234    79 FQKCVAYVRQDDILLPGLtvRETLTYTAILR--LPRKSSDAIRK-KRVEDVLLRDLALTRIGGNLvKGISGGERRRVSIA 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2468698279 655 RALIRKPCVLILDDATSALDANSQLQVEQLLYEspelYSR--SVLLITQHL---SLVEQADHILFLEGGTI 720
Cdd:cd03234   156 VQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQ----LARrnRIVILTIHQprsDLFRLFDRILLLSSGEI 222
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
495-720 1.26e-19

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 88.97  E-value: 1.26e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 495 TPLHLEGlvqfqdVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQY-- 572
Cdd:PRK11247   11 TPLLLNA------VSKRYGERT---VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAre 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 573 EHRYLHrqvaavgQEPQVFG-RSLQENIAYGLTQ--KPTMEEITAAAvksgahsfisglpqGYDTEVGEAGSQLSGGQRQ 649
Cdd:PRK11247   82 DTRLMF-------QDARLLPwKKVIDNVGLGLKGqwRDAALQALAAV--------------GLADRANEWPAALSGGQKQ 140
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2468698279 650 AVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLS-LVEQADHILFLEGGTI 720
Cdd:PRK11247  141 RVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
502-720 1.49e-19

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 92.81  E-value: 1.49e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYPNrpdVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPL----PQYEHR-- 575
Cdd:PRK15439   11 LLCARSISKQYSG---VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCarltPAKAHQlg 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 576 -YLhrqvaaVGQEPQVF-GRSLQENIAYGLTQKP-TMEEITAAAVKSGAHsfisglpqgYDTEVgEAGSqLSGGQRQAVA 652
Cdd:PRK15439   88 iYL------VPQEPLLFpNLSVKENILFGLPKRQaSMQKMKQLLAALGCQ---------LDLDS-SAGS-LEVADRQIVE 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2468698279 653 LARALIRKPCVLILDDATSALdanSQLQVEQLLYESPELYSRSV--LLITQHLSLVEQ-ADHILFLEGGTI 720
Cdd:PRK15439  151 ILRGLMRDSRILILDEPTASL---TPAETERLFSRIRELLAQGVgiVFISHKLPEIRQlADRISVMRDGTI 218
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
505-733 1.91e-19

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 89.31  E-value: 1.91e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 505 FQDVSFAY-PNRP-DVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLP----QYEHRYLH 578
Cdd:PRK13634    5 FQKVEHRYqYKTPfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkkNKKLKPLR 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 579 RQVAAVGQ--EPQVFGRSLQENIAYGltqkPTMEEITAAAVKSGAHSFIS--GLPQGYDTEvgeAGSQLSGGQRQAVALA 654
Cdd:PRK13634   85 KKVGIVFQfpEHQLFEETVEKDICFG----PMNFGVSEEDAKQKAREMIElvGLPEELLAR---SPFELSGGQMRRVAIA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 655 RALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQ-ADHILFLEGGTIREGGTHQQLMEKK 733
Cdd:PRK13634  158 GVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREIFADP 237
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
495-724 2.03e-19

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: 87.59  E-value: 2.03e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 495 TPLHLEGLVQFQDVSFAYPNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEh 574
Cdd:cd03220    12 TYKGGSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLG- 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 575 rylhrqvAAVGQEPQVFGRslqENIA-----YGLTQK---PTMEEItaaavksgaHSFiSGLPQGYDTEVGEagsqLSGG 646
Cdd:cd03220    91 -------LGGGFNPELTGR---ENIYlngrlLGLSRKeidEKIDEI---------IEF-SELGDFIDLPVKT----YSSG 146
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2468698279 647 QRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPElYSRSVLLITQHLSLVEQ-ADHILFLEGGTIREGG 724
Cdd:cd03220   147 MKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLK-QGKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
ABC_6TM_Pgp_ABCB1_D2_like cd18578
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ...
206-487 4.26e-19

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: 88.66  E-value: 4.26e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 206 FFTGRLTDwILQDGSADTFTRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHL----QGEVFGAVLRQETEFFQQ--N 279
Cdd:cd18578    30 ILFSKLIS-VFSLPDDDELRSEANFWALMFLVLAIVAGIAYFLQGYLFGIAGERLtrrlRKLAFRAILRQDIAWFDDpeN 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 280 QTGNITSRVTEDTSTLSDSLSENLSLflwyLVRGLCLLGI-MLWGSVS---LTMVTLVTLPLLFLLPKKVGKWYQLLEVQ 355
Cdd:cd18578   109 STGALTSRLSTDASDVRGLVGDRLGL----ILQAIVTLVAgLIIAFVYgwkLALVGLATVPLLLLAGYLRMRLLSGFEEK 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 356 VRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAV-NSWTTSISgMLLKVGILYIGGQLV 434
Cdd:cd18578   185 NKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGLgFGLSQSLT-FFAYALAFWYGGRLV 263
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2468698279 435 TSGAVSSGNLVTfVLYQMQFT-QAVEVLLSIYPRVQKAVGSSEKIFEYLDRTPR 487
Cdd:cd18578   264 ANGEYTFEQFFI-VFMALIFGaQSAGQAFSFAPDIAKAKAAAARIFRLLDRKPE 316
HisP COG4598
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
520-731 4.39e-19

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


Pssm-ID: 226961 [Multi-domain]  Cd Length: 256  Bit Score: 87.48  E-value: 4.39e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDG-------------KPLPQYEHRYLHRQVAAVGQ 586
Cdd:COG4598    21 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSAGSIRVNGeeirlkrdkdgqlKPADKRQLQRLRTRLGMVFQ 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 587 EPQVFG-RSLQENI------AYGLTQKPTMEEITAAAVKSGAHSFISGLPqgydtevgeagSQLSGGQRQAVALARALIR 659
Cdd:COG4598   101 HFNLWShMTVLENVieapvhVLGVSKAEAIERAEKYLAKVGIAEKADAYP-----------AHLSGGQQQRVAIARALAM 169
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2468698279 660 KPCVLILDDATSALD---ANSQLQVEQLLYESpelySRSVLLITQHLSLVEQ-ADHILFLEGGTIREGGTHQQLME 731
Cdd:COG4598   170 EPEVMLFDEPTSALDpelVGEVLKVMQDLAEE----GRTMVVVTHEMGFARDvSSHVIFLHQGKIEEEGPPEQVFG 241
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
516-719 4.40e-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: 86.62  E-value: 4.40e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 516 PDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLL-------LDGKPLPQYEHRYlhrQVAAVGQEP 588
Cdd:cd03290    12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnknesEPSFEATRSRNRY---SVAYAAQKP 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 589 QVFGRSLQENIAYGltqKPTMEEITAAAVKSGA-HSFISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILD 667
Cdd:cd03290    89 WLLNATVEENITFG---SPFNKQRYKAVTDACSlQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLD 165
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2468698279 668 DATSALDAN-----SQLQVEQLLYESpelySRSVLLITQHLSLVEQADHILFLEGGT 719
Cdd:cd03290   166 DPFSALDIHlsdhlMQEGILKFLQDD----KRTLVLVTHKLQYLPHADWIIAMKDGS 218
PTZ00243 PTZ00243
ABC transporter; Provisional
484-731 5.46e-19

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 92.53  E-value: 5.46e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279  484 RTPRCPPSGLLTPLHLEGLVQFQDVSFAYPNrpdvlvlqgltftlrpGEVTALVGPNGSGKSTvaaLLQNL---YQPTEG 560
Cdd:PTZ00243   655 RSAKTPKMKTDDFFELEPKVLLRDVSVSVPR----------------GKLTVVLGATGSGKST---LLQSLlsqFEISEG 715
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279  561 QLLLDgkplpqyehrylhRQVAAVGQEPQVFGRSLQENIaygLTQKPTMEEITAAAVK-SGAHSFISGLPQGYDTEVGEA 639
Cdd:PTZ00243   716 RVWAE-------------RSIAYVPQQAWIMNATVRGNI---LFFDEEDAARLADAVRvSQLEADLAQLGGGLETEIGEK 779
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279  640 GSQLSGGQRQAVALARALIRKPCVLILDDATSALDAN-SQLQVEQLLYESpeLYSRSVLLITQHLSLVEQADHILFLEGG 718
Cdd:PTZ00243   780 GVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHvGERVVEECFLGA--LAGKTRVLATHQVHVVPRADYVVALGDG 857
                          250
                   ....*....|...
gi 2468698279  719 TIREGGTHQQLME 731
Cdd:PTZ00243   858 RVEFSGSSADFMR 870
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
502-700 9.46e-19

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 86.68  E-value: 9.46e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPL--PQYEhrylhR 579
Cdd:PRK11248    1 MLQISHLYADYGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVegPGAE-----R 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 580 QVAaVGQEPQVFGRSLQENIAYGL----TQKPTMEEITAAAVKsgahsfisglpqgydtEVGEAGS------QLSGGQRQ 649
Cdd:PRK11248   73 GVV-FQNEGLLPWRNVQDNVAFGLqlagVEKMQRLEIAHQMLK----------------KVGLEGAekryiwQLSGGQRQ 135
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2468698279 650 AVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLIT 700
Cdd:PRK11248  136 RVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLIT 186
cbiO PRK13646
energy-coupling factor transporter ATPase;
503-733 1.20e-18

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 86.76  E-value: 1.20e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPN-RP-DVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPL----PQYEHRY 576
Cdd:PRK13646    3 IRFDNVSYTYQKgTPyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktKDKYIRP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 577 LHRQVAAVGQ--EPQVFGRSLQENIAYGltqkPTMEEITAAAVKSGAHSFISGLpqGYDTEVGEAGS-QLSGGQRQAVAL 653
Cdd:PRK13646   83 VRKRIGMVFQfpESQLFEDTVEREIIFG----PKNFKMNLDEVKNYAHRLLMDL--GFSRDVMSQSPfQMSGGQMRKIAI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 654 ARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQ-ADHILFLEGGTIREGGTHQQLMEK 732
Cdd:PRK13646  157 VSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKELFKD 236

                  .
gi 2468698279 733 K 733
Cdd:PRK13646  237 K 237
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
514-723 1.35e-18

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


Pssm-ID: 226617 [Multi-domain]  Cd Length: 209  Bit Score: 85.04  E-value: 1.35e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 514 NRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYlHRQVAAVGQEPQVFGR 593
Cdd:COG4133    11 ERGERTLFSDLSFTLNAGEALQITGPNGAGKTTLLRILAGLLRPDAGEVYWQGEPIQNVRESY-HQALLYLGHQPGIKTE 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 594 -SLQENIAY--GLTQKPTMEEITAAAVKSGAHSFIsglpqgyDTEVGeagsQLSGGQRQAVALARALIRKPCVLILDDAT 670
Cdd:COG4133    90 lTALENLHFwqRFHGSGNAATIWEALAQVGLAGLE-------DLPVG----QLSAGQQRRVALARLWLSPAPLWILDEPF 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2468698279 671 SALDANSQLQVEQLLYEspELYSRSVLLITQHLSLVEQADHILFLEGGTIREG 723
Cdd:COG4133   159 TALDKEGVALLTALMAA--HAAQGGIVLLTTHQPLPIASAQIRRLDLTATKAT 209
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
512-731 1.65e-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: 85.29  E-value: 1.65e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 512 YPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYE-HRYLHRQVAAVGQEPQV 590
Cdd:cd03218    10 YGKRK---VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPmHKRARLGIGYLPQEASI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 591 FGR-SLQENIAYGLTQKPTMEEITAAAVKSGAHSF-ISGLPQGYdtevgeaGSQLSGGQRQAVALARALIRKPCVLILDD 668
Cdd:cd03218    87 FRKlTVEENILAVLEIRGLSKKEREEKLEELLEEFhITHLRKSK-------ASSLSGGERRRVEIARALATNPKFLLLDE 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2468698279 669 ATSALDANSQLQVEQLLYespELYSRSV-LLITQH-----LSLVEQAdHILFleGGTIREGGTHQQLME 731
Cdd:cd03218   160 PFAGVDPIAVQDIQKIIK---ILKDRGIgVLITDHnvretLSITDRA-YIIY--EGKVLAEGTPEEIAA 222
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
517-729 2.08e-18

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: 84.73  E-value: 2.08e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 517 DVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQyEHRYLHRQVAAVGQEPQVfGRSLQ 596
Cdd:cd03265    12 DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLSV-DDELT 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 597 --ENIA-----YGLTQKPTMEEITAAAvksgahSFIsglpqgydtEVGEAGSQL----SGGQRQAVALARALIRKPCVLI 665
Cdd:cd03265    90 gwENLYiharlYGVPGAERRERIDELL------DFV---------GLLEAADRLvktySGGMRRRLEIARSLVHRPEVLF 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2468698279 666 LDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQ-ADHILFLEGGTIREGGTHQQL 729
Cdd:cd03265   155 LDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
515-685 3.52e-18

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 83.31  E-value: 3.52e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 515 RPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYlHRQVAAVGQEPQVFGR- 593
Cdd:PRK13538   11 RDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEY-HQDLLYLGHQPGIKTEl 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 594 SLQENIAY--GLTQKPTMEEITAAAVKsgahsfisglpqgydteVGEAG------SQLSGGQRQAVALARALIRKPCVLI 665
Cdd:PRK13538   90 TALENLRFyqRLHGPGDDEALWEALAQ-----------------VGLAGfedvpvRQLSAGQQRRVALARLWLTRAPLWI 152
                         170       180
                  ....*....|....*....|
gi 2468698279 666 LDDATSALDANSQLQVEQLL 685
Cdd:PRK13538  153 LDEPFTAIDKQGVARLEALL 172
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
515-678 3.94e-18

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 83.38  E-value: 3.94e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 515 RPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHR----YL-HRQvaavGQEPQ 589
Cdd:PRK13539   12 RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAeachYLgHRN----AMKPA 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 590 VfgrSLQENIA-----YGltQKPTMEEITAAAVKSGAhsfISGLPQGYdtevgeagsqLSGGQRQAVALARALIRKPCVL 664
Cdd:PRK13539   88 L---TVAENLEfwaafLG--GEELDIAAALEAVGLAP---LAHLPFGY----------LSAGQKRRVALARLLVSNRPIW 149
                         170
                  ....*....|....
gi 2468698279 665 ILDDATSALDANSQ 678
Cdd:PRK13539  150 ILDEPTAALDAAAV 163
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
520-685 4.30e-18

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


Pssm-ID: 273491 [Multi-domain]  Cd Length: 198  Bit Score: 83.18  E-value: 4.30e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYlHRQVAAVGQEPQVFGR-SLQEN 598
Cdd:TIGR01189  15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEP-HENILYLGHLPGLKPElSALEN 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 599 I----AYGLTQKPTMEEITAAAvksgahsfisGLPQGYDTEVGeagsQLSGGQRQAVALARALIRKPCVLILDDATSALD 674
Cdd:TIGR01189  94 LhfwaAIHGGAQRTIEDALAAV----------GLTGFEDLPAA----QLSAGQQRRLALARLWLSRRPLWILDEPTTALD 159
                         170
                  ....*....|.
gi 2468698279 675 ANSQLQVEQLL 685
Cdd:TIGR01189 160 KAGVALLAGLL 170
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
502-729 5.20e-18

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 87.84  E-value: 5.20e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYPNRPDV-LVLQGLTFTLRPGEVTALVGPNGSGKSTVA-ALLQNLYQP----TEGQLLLDGKPLPQYEHR 575
Cdd:PRK15134    5 LLAIENLSVAFRQQQTVrTVVNDVSLQIEAGETLALVGESGSGKSVTAlSILRLLPSPpvvyPSGDIRFHGESLLHASEQ 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 576 YLHR----QVAAVGQEPQV-------FGRSLQENIAY--GLTQKPTMEEITAAAVKSG---AHSFISGLPQgydtevgea 639
Cdd:PRK15134   85 TLRGvrgnKIAMIFQEPMVslnplhtLEKQLYEVLSLhrGMRREAARGEILNCLDRVGirqAAKRLTDYPH--------- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 640 gsQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQ-ADHILFLEGG 718
Cdd:PRK15134  156 --QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKlADRVAVMQNG 233
                         250
                  ....*....|.
gi 2468698279 719 TIREGGTHQQL 729
Cdd:PRK15134  234 RCVEQNRAATL 244
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
515-712 7.52e-18

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


Pssm-ID: 213198 [Multi-domain]  Cd Length: 201  Bit Score: 82.54  E-value: 7.52e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 515 RPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYlHRQVAAVGQEPQVFGR- 593
Cdd:cd03231    10 RDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSI-ARGLLYLGHAPGIKTTl 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 594 SLQENIAY--GLTQKPTMEEITAAAVKSGAHSFISGlpqgydtevgeagsQLSGGQRQAVALARALIRKPCVLILDDATS 671
Cdd:cd03231    89 SVLENLRFwhADHSDEQVEEALARVGLNGFEDRPVA--------------QLSAGQQRRVALARLLLSGRPLWILDEPTT 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2468698279 672 ALDANSQLQVEQLLyeSPELYSRSVLLITQHLSLVEQADHI 712
Cdd:cd03231   155 ALDKAGVARFAEAM--AGHCARGGMVVLTTHQDLGLSEAGA 193
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
503-675 1.13e-17

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


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 85.28  E-value: 1.13e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPNrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRylHRQVA 582
Cdd:PRK11650    4 LKLQAVRKSYDG--KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPA--DRDIA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 583 AVGQE----PQVfgrSLQENIAYGL----TQKPTMEE-ITAAAVKSGAHSFISGLPQgydtevgeagsQLSGGQRQAVAL 653
Cdd:PRK11650   80 MVFQNyalyPHM---SVRENMAYGLkirgMPKAEIEErVAEAARILELEPLLDRKPR-----------ELSGGQRQRVAM 145
                         170       180
                  ....*....|....*....|..
gi 2468698279 654 ARALIRKPCVLILDDATSALDA 675
Cdd:PRK11650  146 GRAIVREPAVFLFDEPLSNLDA 167
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
520-731 1.14e-17

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 83.35  E-value: 1.14e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQ-----PTEGQLLLDGKPL--PQYEHRYLHRQVAAVGQEPQVFG 592
Cdd:PRK14267   19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIysPDVDPIEVRREVGMVFQYPNPFP 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 593 R-SLQENIAYGL------TQKPTMEEITAAAVKSGAhsfisgLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLI 665
Cdd:PRK14267   99 HlTIYDNVAIGVklnglvKSKKELDERVEWALKKAA------LWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILL 172
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2468698279 666 LDDATSALDANSQLQVEQLLYESPELYsrSVLLITQHLSLVEQ-ADHILFLEGGTIREGGTHQQLME 731
Cdd:PRK14267  173 MDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARvSDYVAFLYLGKLIEVGPTRKVFE 237
ABC_6TM_exporter_like cd18778
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
203-478 1.34e-17

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


Pssm-ID: 350051 [Multi-domain]  Cd Length: 293  Bit Score: 83.74  E-value: 1.34e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 203 AIPFFTGRLTDWILQD-GSADTFTRNLTLMSILTIASAVLEFVgDGIYNNTMG---------HVHSHLQgevfgavlRQE 272
Cdd:cd18778    17 VPPWLIRELVDLVTIGsKSLGLLLGLALLLLGAYLLRALLNFL-RIYLNHVAEqkvvadlrsDLYDKLQ--------RLS 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 273 TEFFQQNQTGNITSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLL 352
Cdd:cd18778    88 LRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLALGAWLYSKKVRPR 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 353 EVQVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKE----AVAYAVNSWTTSIsGMLLkvgILY 428
Cdd:cd18778   168 YRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAmklwAIFHPLMEFLTSL-GTVL---VLG 243
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 2468698279 429 IGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18778   244 FGGRLVLAGELTIGDLVAFLLYLGLFYEPITSLHGLNEMLQRALAGAERV 293
YufO COG3845
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
516-718 2.24e-17

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


Pssm-ID: 226364 [Multi-domain]  Cd Length: 501  Bit Score: 85.67  E-value: 2.24e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 516 PDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPL----PqyehrylhRQVAAVG-----Q 586
Cdd:COG3845    15 PGVVANDDVSLSVKKGEIHALLGENGAGKSTLMKILFGLYQPDSGEIRVDGKEVriksP--------RDAIRLGigmvhQ 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 587 EPQVFGR-SLQENIAYGL-TQKPTMEEITAAAVKSGAHSFISGLPQGYDTEVGEagsqLSGGQRQAVALARALIRKPCVL 664
Cdd:COG3845    87 HFMLVPTlTVAENIILGLePSKGGLIDRRQARARIKELSERYGLPVDPDAKVAD----LSVGEQQRVEILKALYRGARLL 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2468698279 665 ILDDATSALdanSQLQVEQLLYESPELYS--RSVLLITQHLSLV-EQADHILFLEGG 718
Cdd:COG3845   163 ILDEPTAVL---TPQEADELFEILRRLAAegKTIIFITHKLKEVmAIADRVTVLRRG 216
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
520-687 2.99e-17

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 82.34  E-value: 2.99e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGR-SLQEN 598
Cdd:PRK10253   22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDiTVQEL 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 599 IAYG-LTQKPTM-------EEITAAAVKSGAHSFISGlpQGYDTevgeagsqLSGGQRQAVALARALIRKPCVLILDDAT 670
Cdd:PRK10253  102 VARGrYPHQPLFtrwrkedEEAVTKAMQATGITHLAD--QSVDT--------LSGGQRQRAWIAMVLAQETAIMLLDEPT 171
                         170
                  ....*....|....*..
gi 2468698279 671 SALDANSQLQVEQLLYE 687
Cdd:PRK10253  172 TWLDISHQIDLLELLSE 188
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
520-729 3.12e-17

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 81.40  E-value: 3.12e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHR----YLHRQVAAVGQepqvFGRSL 595
Cdd:PRK11629   24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAakaeLRNQKLGFIYQ----FHHLL 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 596 Q-----ENIAYGL---TQKPtmeeitaAAVKSGAHSFISGLpqGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILD 667
Cdd:PRK11629  100 PdftalENVAMPLligKKKP-------AEINSRALEMLAAV--GLEHRANHRPSELSGGERQRVAIARALVNNPRLVLAD 170
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2468698279 668 DATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQADHILfleggTIREGGTHQQL 729
Cdd:PRK11629  171 EPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQL-----EMRDGRLTAEL 227
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
516-684 4.02e-17

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 84.96  E-value: 4.02e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 516 PDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPlpqyeHRY------LHRQVAAVGQEPQ 589
Cdd:PRK11288   15 PGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQE-----MRFasttaaLAAGVAIIYQELH 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 590 -VFGRSLQENIAYGltQKPT-MEEITAAAVKSGAHSFISGLpqGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILD 667
Cdd:PRK11288   90 lVPEMTVAENLYLG--QLPHkGGIVNRRLLNYEAREQLEHL--GVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFD 165
                         170
                  ....*....|....*..
gi 2468698279 668 DATSALdanSQLQVEQL 684
Cdd:PRK11288  166 EPTSSL---SAREIEQL 179
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only] ...
520-720 4.67e-17

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


Pssm-ID: 224026 [Multi-domain]  Cd Length: 263  Bit Score: 81.60  E-value: 4.67e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQY--EHRYLHrqVAAVGQEPQ--VFGR-S 594
Cdd:COG1101    21 ALNGLSLEIAEGDFVTVIGSNGAGKSTLLNAIAGDLKPTSGQILIDGVDVTKKsvAKRANL--LARVFQDPLagTAPElT 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 595 LQENIAYGLtQKPTMEEITAAAVKSGAHSF---ISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATS 671
Cdd:COG1101    99 IEENLALAE-SRGKKRGLSSALNERRRSSFrerLARLGLGLENRLSDRIGLLSGGQRQALSLLMATLHPPKILLLDEHTA 177
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2468698279 672 ALDANSQLQVEQLLYESPELYSRSVLLITQHLslvEQA----DHILFLEGGTI 720
Cdd:COG1101   178 ALDPKTAEFVMELTAKIVEEHKLTTLMVTHNM---EDAldygNRLIMLHSGKI 227
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
520-731 7.49e-17

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


Pssm-ID: 224060 [Multi-domain]  Cd Length: 243  Bit Score: 80.71  E-value: 7.49e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGK---PLPQyeHRYLHRQVAAVGQEPQVFGR-SL 595
Cdd:COG1137    19 VVNDVSLEVNSGEIVGLLGPNGAGKTTTFYMIVGLVRPDSGKILLDDEditKLPM--HKRARLGIGYLPQEASIFRKlTV 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 596 QENIAYGL--TQKPTMEEITAAAVKSGAHSF-ISGLpqgydteVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATSA 672
Cdd:COG1137    97 EDNIMAVLeiREKDLKKAERKEELDALLEEFhITHL-------RDSKAYSLSGGERRRVEIARALAANPKFILLDEPFAG 169
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2468698279 673 LDANSQLQVEQLLyesPELYSRSV-LLITQH-----LSLVEQAdHILFleGGTIREGGTHQQLME 731
Cdd:COG1137   170 VDPIAVIDIQRII---KHLKDRGIgVLITDHnvretLDICDRA-YIIS--DGKVLAEGSPEEIVN 228
cbiO PRK13637
energy-coupling factor transporter ATPase;
503-725 7.70e-17

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 81.63  E-value: 7.70e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAY-PNRP-DVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPL--PQYEHRYLH 578
Cdd:PRK13637    3 IKIENLTHIYmEGTPfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIR 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 579 RQVAAVGQEP--QVFGRSLQENIAYGLTQKPTMEEITAAAVKSGAHsfISGLPqgYDTEVGEAGSQLSGGQRQAVALARA 656
Cdd:PRK13637   83 KKVGLVFQYPeyQLFEETIEKDIAFGPINLGLSEEEIENRVKRAMN--IVGLD--YEDYKDKSPFELSGGQKRRVAIAGV 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2468698279 657 LIRKPCVLILDDATSALDANSQlqvEQLLYESPEL---YSRSVLLITQHLSLVEQ-ADHILFLEGGTIREGGT 725
Cdd:PRK13637  159 VAMEPKILILDEPTAGLDPKGR---DEILNKIKELhkeYNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGT 228
cbiO PRK13641
energy-coupling factor transporter ATPase;
503-718 9.00e-17

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 81.41  E-value: 9.00e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAY-PNRPdvLVLQGLT---FTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPL-PQYEHRYL 577
Cdd:PRK13641    3 IKFENVDYIYsPGTP--MEKKGLDnisFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItPETGNKNL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 578 ---HRQVAAVGQ--EPQVFGRSLQENIAYGltqkPTMEEITAAAVKSGAHSFISGLpqGYDTEVGEAGS-QLSGGQRQAV 651
Cdd:PRK13641   81 kklRKKVSLVFQfpEAQLFENTVLKDVEFG----PKNFGFSEDEAKEKALKWLKKV--GLSEDLISKSPfELSGGQMRRV 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2468698279 652 ALARALIRKPCVLILDDATSALDANSQLQVEQLLYEspelYSR---SVLLITQHLSLV-EQADHILFLEGG 718
Cdd:PRK13641  155 AIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKD----YQKaghTVILVTHNMDDVaEYADDVLVLEHG 221
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
525-730 1.12e-16

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


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 82.77  E-value: 1.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 525 TFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQY---EHRYLHRQ-VAAVGQEPQVFGR-SLQENI 599
Cdd:PRK10070   48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKIsdaELREVRRKkIAMVFQSFALMPHmTVLDNT 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 600 AYGL-----TQKPTMEEITAAAVKSGAHSFISGLPqgydtevgeagSQLSGGQRQAVALARALIRKPCVLILDDATSALD 674
Cdd:PRK10070  128 AFGMelagiNAEERREKALDALRQVGLENYAHSYP-----------DELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2468698279 675 ANSQLQVEQLLYESPELYSRSVLLITQHL-SLVEQADHILFLEGGTIREGGTHQQLM 730
Cdd:PRK10070  197 PLIRTEMQDELVKLQAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
503-717 1.59e-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: 77.58  E-value: 1.59e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPNrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLlldgkplpqyeHRYLHRQVA 582
Cdd:cd03223     1 IELENLSLATPD--GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI-----------GMPEGEDLL 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 583 AVGQEPQVFGRSLQENIAYgltqkPTMEEitaaavksgahsfisglpqgydtevgeagsqLSGGQRQAVALARALIRKPC 662
Cdd:cd03223    68 FLPQRPYLPLGTLREQLIY-----PWDDV-------------------------------LSGGEQQRLAFARLLLHKPK 111
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2468698279 663 VLILDDATSALDAnsqlQVEQLLYESPELYSRSVLLITQHLSLVEQADHILFLEG 717
Cdd:cd03223   112 FVFLDEATSALDE----ESEDRLYQLLKELGITVISVGHRPSLWKFHDRVLDLDG 162
SufC COG0396
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ...
520-736 1.72e-16

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


Pssm-ID: 223473 [Multi-domain]  Cd Length: 251  Bit Score: 79.93  E-value: 1.72e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNL--YQPTEGQLLLDGKP---LPQYEHrylhrqvAAVG-----QEP- 588
Cdd:COG0396    19 ILKGVNLTVKEGEVHAIMGPNGSGKSTLAYTIMGHpkYEVTEGEILFDGEDileLSPDER-------ARAGiflafQYPv 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 589 QVFGRSLQENIAYGLTQKPTMEEITAAA---VKSGAHSFisGLPQGY-DTEVGEAgsqLSGGQRQAVALARALIRKPCVL 664
Cdd:COG0396    92 EIPGVTNSDFLRAAMNARRGARGILPEFikeLKEKAELL--GLDEEFlERYVNEG---FSGGEKKRNEILQLLLLEPKLA 166
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2468698279 665 ILDDATSALDANSQLQVEQLL--YESPElysRSVLLITQHLSLVE--QADHILFLEGGTI-REGGTHQQLMEKKGCY 736
Cdd:COG0396   167 ILDEPDSGLDIDALKIVAEGInaLREEG---RGVLIITHYQRLLDyiKPDKVHVLYDGRIvKSGDPELAEELEEKGY 240
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
521-715 1.79e-16

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: 79.43  E-value: 1.79e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 521 LQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPL--PQYEhrylhRQVaaVGQEPQVFG-RSLQE 597
Cdd:TIGR01184   1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQItePGPD-----RMV--VFQNYSLLPwLTVRE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 598 NIAYGLTQ-KPTMEEITAAAVKSgAHSFISGLPQGYDTEVGeagsQLSGGQRQAVALARALIRKPCVLILDDATSALDAN 676
Cdd:TIGR01184  74 NIALAVDRvLPDLSKSERRAIVE-EHIALVGLTEAADKRPG----QLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAL 148
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2468698279 677 SQLQVEQLLYESPELYSRSVLLITQHLslveqaDHILFL 715
Cdd:TIGR01184 149 TRGNLQEELMQIWEEHRVTVLMVTHDV------DEALLL 181
ABC_6TM_ABCB8_like cd18574
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ...
265-449 2.15e-16

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


Pssm-ID: 350018 [Multi-domain]  Cd Length: 295  Bit Score: 80.28  E-value: 2.15e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 265 FGAVLRQETEFFQQNQTGNITSRVTEDT----STLSDSLSENLSLFLwyLVRGLC--LLGImlwgSVSLTMVTLVTLPLL 338
Cdd:cd18574    82 FSSLLRQDIAFFDTHRTGELVNRLTADVqefkSSFKQCVSQGLRSVT--QTVGCVvsLYLI----SPKLTLLLLVIVPVV 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 339 FLLPKKVGKWYQLLEVQVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAV-----Nsw 413
Cdd:cd18574   156 VLVGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYEEEVEKAAKLNEKLGLGIGIfqglsN-- 233
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2468698279 414 tTSISGMLLkvGILYIGGQLVTSGAVSSGNLVTFVL 449
Cdd:cd18574   234 -LALNGIVL--GVLYYGGSLVSRGELTAGDLMSFLV 266
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
500-729 2.63e-16

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 80.92  E-value: 2.63e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 500 EGLVQFQD--VSFAYPNrPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQP---TEGQLLLDGKPLPQYEH 574
Cdd:PRK09473   10 DALLDVKDlrVTFSTPD-GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREILNLPE 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 575 RYLHR----QVAAVGQEPQV-------FGRSLQENIAY--GLTQKPTMEEITAA--AVK-SGAHSFISGLPQgydtevge 638
Cdd:PRK09473   89 KELNKlraeQISMIFQDPMTslnpymrVGEQLMEVLMLhkGMSKAEAFEESVRMldAVKmPEARKRMKMYPH-------- 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 639 agsQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQ-ADHILFLEG 717
Cdd:PRK09473  161 ---EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGiCDKVLVMYA 237
                         250
                  ....*....|..
gi 2468698279 718 GTIREGGTHQQL 729
Cdd:PRK09473  238 GRTMEYGNARDV 249
cbiO PRK13649
energy-coupling factor transporter ATPase;
503-733 3.75e-16

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 79.40  E-value: 3.75e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAY-PNRP-DVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQY----EHRY 576
Cdd:PRK13649    3 INLQNVSYTYqAGTPfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTsknkDIKQ 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 577 LHRQVAAVGQ--EPQVFGRSLQENIAYGltqkP-----TMEEITAAAVKSGAHSFISglpqgyDTEVGEAGSQLSGGQRQ 649
Cdd:PRK13649   83 IRKKVGLVFQfpESQLFEETVLKDVAFG----PqnfgvSQEEAEALAREKLALVGIS------ESLFEKNPFELSGGQMR 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 650 AVALARALIRKPCVLILDDATSALDANSQLQVEQlLYESPELYSRSVLLITqHL--SLVEQADHILFLEGGTIREGGTHQ 727
Cdd:PRK13649  153 RVAIAGILAMEPKILVLDEPTAGLDPKGRKELMT-LFKKLHQSGMTIVLVT-HLmdDVANYADFVYVLEKGKLVLSGKPK 230
                         250
                  ....*....|..
gi 2468698279 728 Q------LMEKK 733
Cdd:PRK13649  231 DifqdvdFLEEK 242
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
515-729 4.72e-16

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 82.21  E-value: 4.72e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 515 RPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLpqyehRYLHRQV------------- 581
Cdd:PRK10261   26 QQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLL-----RRRSRQVielseqsaaqmrh 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 582 ------AAVGQEPQ-----VF--GRSLQENIAygLTQKPTMEEITAAAVK-------SGAHSFISGLPQgydtevgeags 641
Cdd:PRK10261  101 vrgadmAMIFQEPMtslnpVFtvGEQIAESIR--LHQGASREEAMVEAKRmldqvriPEAQTILSRYPH----------- 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 642 QLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLV-EQADHILFLEGGTI 720
Cdd:PRK10261  168 QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVaEIADRVLVMYQGEA 247

                  ....*....
gi 2468698279 721 REGGTHQQL 729
Cdd:PRK10261  248 VETGSVEQI 256
ABC_6TM_YwjA_like cd18549
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ...
201-470 5.32e-16

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: 79.03  E-value: 5.32e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 201 EMAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGDGiYNNTMG-HVHSHLQGEVFGAVLRQETEFFQQN 279
Cdd:cd18549    18 DLVFPLIVRYIIDDLLPSKNLRLILIIGAILLALYILRTLLNYFVTY-WGHVMGaRIETDMRRDLFEHLQKLSFSFFDNN 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 280 QTGNITSRVTEDTSTLSDsLS----ENLslflwyLVRGLCLLG---IMLWGSVSLTMVTLVT----LPLLFLLPKKVGKW 348
Cdd:cd18549    97 KTGQLMSRITNDLFDISE-LAhhgpEDL------FISIITIIGsfiILLTINVPLTLIVFALlplmIIFTIYFNKKMKKA 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 349 YQllevQVRESLAK-SSQVAiEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKeavAYAVNSWTTSISGM---LLKV 424
Cdd:cd18549   170 FR----RVREKIGEiNAQLE-DSLSGIRVVKAFANEEYEIEKFDEGNDRFLESKKK---AYKAMAYFFSGMNFftnLLNL 241
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 2468698279 425 GILYIGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQK 470
Cdd:cd18549   242 VVLVAGGYFIIKGEITLGDLVAFLLYVNVFIKPIRRLVNFTEQYQK 287
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
503-717 6.89e-16

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


Pssm-ID: 226646 [Multi-domain]  Cd Length: 604  Bit Score: 81.59  E-value: 6.89e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPNRpDVLvLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLlldgkplpqyeHRYLHRQVA 582
Cdd:COG4178   393 ITLENLSLRTPDG-QTL-LSELNFEVRPGERLLITGESGAGKTSLLRALAGLWPWGSGRI-----------SMPADSALL 459
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 583 AVGQEPQVFGRSLQENIAY-GLTQKPTMEEITAAAVKSGAHSFISGLpqgydTEVGEAGSQLSGGQRQAVALARALIRKP 661
Cdd:COG4178   460 FLPQRPYLPQGTLREALCYpNAAPDFSDAELVAVLHKVGLGDLAERL-----DEEDRWDRVLSGGEQQRLAFARLLLHKP 534
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2468698279 662 CVLILDDATSALDANSQLQVEQLLYEspELYSRSVLLITQHLSLVEQADHILFLEG 717
Cdd:COG4178   535 KWVFLDEATSALDEETEDRLYQLLKE--ELPDATVISVGHRPTLWNFHSRQLELLD 588
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
520-720 7.45e-16

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: 75.93  E-value: 7.45e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQ-VAAVGQEPQVFG----RS 594
Cdd:cd03215    15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVPEDRKREGlvldLS 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 595 LQENIAygltqkptmeeitaaavksgahsfisglpqgydtevgeAGSQLSGGQRQAVALARALIRKPCVLILDDATSALD 674
Cdd:cd03215    95 VAENIA--------------------------------------LSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVD 136
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2468698279 675 ANSQLQVEQLLYESPElYSRSVLLITQHLS-LVEQADHILFLEGGTI 720
Cdd:cd03215   137 VGAKAEIYRLIRELAD-AGKAVLLISSELDeLLGLCDRILVMYEGRI 182
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
520-733 1.18e-15

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 77.83  E-value: 1.18e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEG-----QLLLDGKPLPQYEHRY-LHRQVAAVGQEPQVFGR 593
Cdd:PRK14271   36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRDVLeFRRRVGMLFQRPNPFPM 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 594 SLQENIAYGLTQKPTMEEITAAAVKSGAHSFIsGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATSAL 673
Cdd:PRK14271  116 SIMDNVLAGVRAHKLVPRKEFRGVAQARLTEV-GLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSAL 194
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2468698279 674 DANSQLQVEQLLYESPElySRSVLLITQHLSlveQADHI-----LFLEGGTIREGGTHQQLMEKK 733
Cdd:PRK14271  195 DPTTTEKIEEFIRSLAD--RLTVIIVTHNLA---QAARIsdraaLFFDGRLVEEGPTEQLFSSPK 254
PRK10522 PRK10522
multidrug transporter membrane component/ATP-binding component; Provisional
505-722 1.36e-15

multidrug transporter membrane component/ATP-binding component; Provisional


Pssm-ID: 236707 [Multi-domain]  Cd Length: 547  Bit Score: 80.40  E-value: 1.36e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 505 FQDVSFAYPNRPdvLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQyEHRYLHRQ-VAA 583
Cdd:PRK10522  325 LRNVTFAYQDNG--FSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTA-EQPEDYRKlFSA 401
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 584 VGQEPQVFGRSLqeniaygltqKPTMEEITAAAVKsgahSFISGLPQGYDTEVGE---AGSQLSGGQRQAVALARALIRK 660
Cdd:PRK10522  402 VFTDFHLFDQLL----------GPEGKPANPALVE----KWLERLKMAHKLELEDgriSNLKLSKGQKKRLALLLALAEE 467
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2468698279 661 PCVLILDDAtsALDANSQLQVE---QLLyesPELYS--RSVLLITQHLSLVEQADHILFLEGGTIRE 722
Cdd:PRK10522  468 RDILLLDEW--AADQDPHFRREfyqVLL---PLLQEmgKTIFAISHDDHYFIHADRLLEMRNGQLSE 529
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
502-720 1.83e-15

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 80.15  E-value: 1.83e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYPN-RPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLhrq 580
Cdd:PRK10535    4 LLELKDIRRSYPSgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADAL--- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 581 vAAVGQEPqvFGRSLQEniaYGLTQKPTME---EITA-------AAVKSGAHSFISGLpqGYDTEVGEAGSQLSGGQRQA 650
Cdd:PRK10535   81 -AQLRREH--FGFIFQR---YHLLSHLTAAqnvEVPAvyaglerKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQR 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 651 VALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPElYSRSVLLITQHLSLVEQADHILFLEGGTI 720
Cdd:PRK10535  153 VSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRD-RGHTVIIVTHDPQVAAQAERVIEIRDGEI 221
ABC_6TM_PCAT1_LagD_like cd18570
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ...
202-471 2.55e-15

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: 77.10  E-value: 2.55e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 202 MAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVgDGIYNNTMG-HVHSHLQGEVFGAVLRQETEFFQQNQ 280
Cdd:cd18570    19 IAGSFFFQILIDDIIPSGDINLLNIISIGLILLYLFQSLLSYI-RSYLLLKLSqKLDIRLILGYFKHLLKLPLSFFETRK 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 281 TGNITSRVTeDTSTLSDSLSEN-LSLFLWYLVrGLCLLGIMLWGSVSLTMVTLVT----LPLLFLLPKKVGKWYQllevQ 355
Cdd:cd18570    98 TGEIISRFN-DANKIREAISSTtISLFLDLLM-VIISGIILFFYNWKLFLITLLIiplyILIILLFNKPFKKKNR----E 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 356 VRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVT 435
Cdd:cd18570   172 VMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLISLIGSLLILWIGSYLVI 251
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 2468698279 436 SGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKA 471
Cdd:cd18570   252 KGQLSLGQLIAFNALLGYFLGPIENLINLQPKIQEA 287
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
501-713 2.72e-15

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


Pssm-ID: 226620 [Multi-domain]  Cd Length: 213  Bit Score: 75.25  E-value: 2.72e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 501 GLVQFQDVSFAYPNRpdvLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPT---EGQLLLDGKPLPQY-EHRy 576
Cdd:COG4136     1 GMLCLKNVSLRLPGS---CLLANVNFTIAKGEIVTLMGPSGCGKSTLLSWMIGALAGQfscTGELWLNEQRLDMLpAAQ- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 577 lhRQVAAVGQEPQVFGR-SLQENIAYGLTQKPTMEE----ITAAAVKSGAHSFISGLPQgydtevgeagsQLSGGQRQAV 651
Cdd:COG4136    77 --RQIGILFQDALLFPHlSVGQNLLFALPATLKGNArrnaANAALERSGLDGAFHQDPA-----------TLSGGQRARV 143
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2468698279 652 ALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQADHIL 713
Cdd:COG4136   144 ALLRALLAQPKALLLDEPFSRLDVALRDQFRQWVFSEVRAAGIPTVQVTHDLQDVPAGSRVI 205
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
520-733 2.91e-15

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


Pssm-ID: 226635 [Multi-domain]  Cd Length: 242  Bit Score: 76.03  E-value: 2.91e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEH------RYLHRQVAAVGQEPQVFGR 593
Cdd:COG4161    17 ALFDITLDCPEGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKTpsdkaiRDLRRNVGMVFQQYNLWPH 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 594 -SLQENI------AYGLTQKPTMEEITAAAVKSGAHSFISGLPQgydtevgeagsQLSGGQRQAVALARALIRKPCVLIL 666
Cdd:COG4161    97 lTVQENLieapcrVLGLSKDQALARAEKLLKRLRLKPYADRYPL-----------HLSGGQQQRVAIARALMMEPQVLLF 165
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2468698279 667 DDATSALDANSQLQVEQLLYESPELYSRSVlLITQHLSLVEQ-ADHILFLEGGTIREGGTHQQLMEKK 733
Cdd:COG4161   166 DEPTAALDPEITAQIVSIIKELAETGITQV-IVTHEVEVARKtASRVVYMENGHIVEQGDASCFTEPQ 232
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
520-730 3.71e-15

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 76.16  E-value: 3.71e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDG-------------KPLPQYEHRYLHRQVAAVGQ 586
Cdd:PRK10619   20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtinlvrdkdgqlKVADKNQLRLLRTRLTMVFQ 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 587 EPQVFGR-SLQENI------AYGLTQKPTMEEitaaAVKSGAHSFISGLPQGydtevgEAGSQLSGGQRQAVALARALIR 659
Cdd:PRK10619  100 HFNLWSHmTVLENVmeapiqVLGLSKQEARER----AVKYLAKVGIDERAQG------KYPVHLSGGQQQRVSIARALAM 169
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2468698279 660 KPCVLILDDATSALD---ANSQLQVEQLLYESpelySRSVLLITQHLSLVEQ-ADHILFLEGGTIREGGTHQQLM 730
Cdd:PRK10619  170 EPEVLLFDEPTSALDpelVGEVLRIMQQLAEE----GKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLF 240
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
502-715 3.79e-15

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 75.92  E-value: 3.79e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQV 581
Cdd:PRK09544    4 LVSLENVSVSFGQRR---VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGKLRIGYVPQKLYLDT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 582 AAvgqePQVFGRSLQeniaygLTQKPTMEEITAAAVKSGAHSFISGLPQgydtevgeagsQLSGGQRQAVALARALIRKP 661
Cdd:PRK09544   81 TL----PLTVNRFLR------LRPGTKKEDILPALKRVQAGHLIDAPMQ-----------KLSGGETQRVLLARALLNRP 139
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2468698279 662 CVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLV-EQADHILFL 715
Cdd:PRK09544  140 QLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVmAKTDEVLCL 194
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
251-730 4.06e-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: 79.95  E-value: 4.06e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279  251 NTMGHVHSHLQGEVFGAVLRQETEFFQQNQTGNITSRVTEDTSTLSDSLSenLSLF----LWYLVRG-LCLLGIMLWGSV 325
Cdd:TIGR01271  951 HTLLTVSKRLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLP--LTLFdfiqLTLIVLGaIFVVSVLQPYIF 1028
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279  326 SLTMVTLVTLPLLFLLPKKVGKWYQLLEVQVRESLAKSsqvAIEALSAMPTVRSFANeegeaQKFREKLQEiKTLNQKEA 405
Cdd:TIGR01271 1029 IAAIPVAVIFIMLRAYFLRTSQQLKQLESEARSPIFSH---LITSLKGLWTIRAFGR-----QSYFETLFH-KALNLHTA 1099
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279  406 VAYAvnsWTTSISGMLLKVGILY-----------IGGQLVTSGAVssGNLVTFVLYQMQFTQAVeVLLSIypRVQKAVGS 474
Cdd:TIGR01271 1100 NWFL---YLSTLRWFQMRIDIIFvfffiavtfiaIGTNQDGEGEV--GIILTLAMNILSTLQWA-VNSSI--DVDGLMRS 1171
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279  475 SEKIFEYLDRTPRCP-PSGLLTPLHL-----------------EGLVQFQDVSFAYPNRPDVlVLQGLTFTLRPGEVTAL 536
Cdd:TIGR01271 1172 VSRVFKFIDLPQEEPrPSGGGGKYQLstvlvienphaqkcwpsGGQMDVQGLTAKYTEAGRA-VLQDLSFSVEGGQRVGL 1250
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279  537 VGPNGSGKSTV-AALLQNLyqPTEGQLLLDGKplpQYEHRYLHRQVAAVGQEPQ---VFGRSLQENI-AYgltQKPTMEE 611
Cdd:TIGR01271 1251 LGRTGSGKSTLlSALLRLL--STEGEIQIDGV---SWNSVTLQTWRKAFGVIPQkvfIFSGTFRKNLdPY---EQWSDEE 1322
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279  612 ITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESpel 691
Cdd:TIGR01271 1323 IWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQS--- 1399
                          490       500       510       520
                   ....*....|....*....|....*....|....*....|
gi 2468698279  692 YSRSVLLITQH-LSLVEQADHILFLEGGTIREGGTHQQLM 730
Cdd:TIGR01271 1400 FSNCTVILSEHrVEALLECQQFLVIEGSSVKQYDSIQKLL 1439
COG4674 COG4674
ABC-type uncharacterized transport system, ATPase component [General function prediction only] ...
521-723 4.12e-15

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


Pssm-ID: 227019 [Multi-domain]  Cd Length: 249  Bit Score: 75.83  E-value: 4.12e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 521 LQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGK----PLPqyEHRYLHRQVAAVGQEPQVF-GRSL 595
Cdd:COG4674    21 LNDLSFSVDPGELRVLIGPNGAGKTTLMDVITGKTRPQEGEVLFDGDtdltKLP--EHRIARAGIGRKFQKPTVFeNLTV 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 596 QENIAYGLTQKPTMEEITAAAVKSGAHSFISGLPQ--GYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATSAL 673
Cdd:COG4674    99 RENLELALNRDKSVFASLFARLRAEERRRIDELLAtiGLGDERDRLAALLSHGQKQWLEIGMLLAQDPKLLLLDEPVAGM 178
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2468698279 674 DANSQLQVEQLLYESPElySRSVLLITQHLSLVEQ-ADHILFL-EGGTIREG 723
Cdd:COG4674   179 TDAETEKTAELLKSLAG--KHSILVVEHDMGFVREiADKVTVLhEGSVLAEG 228
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
516-724 4.14e-15

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 75.89  E-value: 4.14e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 516 PDVLVLQGLTFTLRPGEVTALVGPNGSGKS-TVAALLQNL---YQPTEGQLLLDGKPLPQYEHRylHRQVAAVGQEPQVF 591
Cdd:PRK10418   14 AAQPLVHGVSLTLQRGRVLALVGGSGSGKSlTCAAALGILpagVRQTAGRVLLDGKPVAPCALR--GRKIATIMQNPRSA 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 592 GRSLQENIAYGL-----TQKPTMEEITAAAVKSGAHSFISGLPQGYDTEvgeagsqLSGGQRQAVALARALIRKPCVLIL 666
Cdd:PRK10418   92 FNPLHTMHTHARetclaLGKPADDATLTAALEAVGLENAARVLKLYPFE-------MSGGMLQRMMIALALLCEAPFIIA 164
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2468698279 667 DDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQ-ADHILFLEGGTIREGG 724
Cdd:PRK10418  165 DEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARlADDVAVMSHGRIVEQG 223
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
520-727 4.37e-15

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 75.44  E-value: 4.37e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDG-------KPLPQyEHRYLHRQVAAVGQepqvfg 592
Cdd:PRK11124   17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfskTPSDK-AIRELRRNVGMVFQ------ 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 593 rslQENIAYGLTqkpTMEEITAAAVKsgahsfISGLPQgyDTEVGEAGS----------------QLSGGQRQAVALARA 656
Cdd:PRK11124   90 ---QYNLWPHLT---VQQNLIEAPCR------VLGLSK--DQALARAEKllerlrlkpyadrfplHLSGGQQQRVAIARA 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2468698279 657 LIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVlLITQHLSLVEQ-ADHILFLEGGTIREGGTHQ 727
Cdd:PRK11124  156 LMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQV-IVTHEVEVARKtASRVVYMENGHIVEQGDAS 226
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
431-731 4.58e-15

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 78.74  E-value: 4.58e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 431 GQLVTSGAVSSgnlvTFVLYQMQFTQAvevLLSIYPRVQKAVGSS-EKIFEYL---DRTPRCPPSGLLTPLHLEGLVQFQ 506
Cdd:PRK10261  245 GEAVETGSVEQ----IFHAPQHPYTRA---LLAAVPQLGAMKGLDyPRRFPLIsleHPAKQEPPIEQDTVVDGEPILQVR 317
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 507 DVSFAYPNRPDVL--------VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGK---PLPQYEHR 575
Cdd:PRK10261  318 NLVTRFPLRSGLLnrvtrevhAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridTLSPGKLQ 397
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 576 YLHRQVAAVGQEP-------QVFGRSLQENI-AYGLTQKPTMEEITAAAVKSgahsfISGLPQgydtEVGEAGSQLSGGQ 647
Cdd:PRK10261  398 ALRRDIQFIFQDPyasldprQTVGDSIMEPLrVHGLLPGKAAAARVAWLLER-----VGLLPE----HAWRYPHEFSGGQ 468
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 648 RQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQADH---ILFLegGTIREGG 724
Cdd:PRK10261  469 RQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHrvaVMYL--GQIVEIG 546

                  ....*..
gi 2468698279 725 THQQLME 731
Cdd:PRK10261  547 PRRAVFE 553
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
520-722 4.59e-15

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 75.20  E-value: 4.59e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQY--EHRYLHRqVAAVGQEPQVF----GR 593
Cdd:PRK10584   25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMdeEARAKLR-AKHVGFVFQSFmlipTL 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 594 SLQENIAY-----GLTQKPTMEEITAAAVKSGAHSFISGLPqgydtevgeagSQLSGGQRQAVALARALIRKPCVLILDD 668
Cdd:PRK10584  104 NALENVELpallrGESSRQSRNGAKALLEQLGLGKRLDHLP-----------AQLSGGEQQRVALARAFNGRPDVLFADE 172
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2468698279 669 ATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQADHILFLEGGTIRE 722
Cdd:PRK10584  173 PTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQLQE 226
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
520-733 5.71e-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: 79.18  E-value: 5.71e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279  520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKplpqyehrylhrqVAAVGQEPQVFGRSLQENI 599
Cdd:TIGR01271  441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQTSWIMPGTIKDNI 507
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279  600 AYGLTqkptMEEITAAAVKSGAH--SFISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDans 677
Cdd:TIGR01271  508 IFGLS----YDEYRYTSVIKACQleEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLD--- 580
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2468698279  678 qLQVEQLLYES---PELYSRSVLLITQHLSLVEQADHILFLEGGTIREGGTHQQLMEKK 733
Cdd:TIGR01271  581 -VVTEKEIFESclcKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKR 638
PvdE COG4615
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...
260-722 6.86e-15

ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];


Pssm-ID: 226968 [Multi-domain]  Cd Length: 546  Bit Score: 78.30  E-value: 6.86e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 260 LQGEVFGAVLRQETEFFQQNQTGNITSRVTEDTSTLSDSLSENLSL------------FLWYL---VRGLCLLGIML--W 322
Cdd:COG4615    83 LRSEFIKKILDTPLERIERLGSARLLAGLTSDVRNISFAFSRLPELvqaiiltlgsaaYLAYLspkMFLLTVVWIVVtiW 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 323 GSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEVQVRESLakssqvaieaLSAMPTVRSFANE-EGEAQKFREKLQEIKTLN 401
Cdd:COG4615   163 GGFVLMARVYKHMAAARETEDKLQNDYQTILEGRKELT----------LNRERAEYVHNNLyIPDAQEYRHHIIRANTFH 232
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 402 QkeavayAVNSWTTSIsgMLLKVGI-LYIGGQLvtsGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKIfE 480
Cdd:COG4615   233 L------LAVNWSNIM--LLGLIGLvFWLALSL---GWASTNVAATIVLVLLFLRTPLLSAVGILPTLLTAQVAFNKI-A 300
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 481 YLDRTPrcPPSGLLTPLHLEGL--VQFQDVSFAYPnrPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPT 558
Cdd:COG4615   301 KLELAP--YKADFPRPQAFPDWktLELRNVRFAYQ--DNAFHVGPINLTIKRGELVFLIGGNGSGKSTLAMLLTGLYQPQ 376
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 559 EGQLLLDGKPL-PQYEHRYlhRQV-AAVGQEPQVFGRSLqeniayGLTQKPTMEEITAaavksgahsFISGLPQGYDTEV 636
Cdd:COG4615   377 SGEILLDGKPVsAEQLEDY--RKLfSAVFSDYHLFDQLL------GPEGKASPQLIEK---------WLQRLELAHKTSL 439
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 637 GE---AGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQADHIL 713
Cdd:COG4615   440 NDgrfSNLKLSTGQKKRLALLLALLEERDILVLDEWAADQDPAFRREFYQVLLPLLKEQGKTIFAISHDDHYFIHADRLL 519

                  ....*....
gi 2468698279 714 FLEGGTIRE 722
Cdd:COG4615   520 EMRNGQLSE 528
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
516-684 6.94e-15

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 77.90  E-value: 6.94e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 516 PDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQ-VAAVGQEPQVFGR- 593
Cdd:PRK09700   16 GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLgIGIIYQELSVIDEl 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 594 SLQENIAYG--LTQK---------PTMEEITAAAVKsgahsfISGLPQGYDTEVGEagsqLSGGQRQAVALARALIRKPC 662
Cdd:PRK09700   96 TVLENLYIGrhLTKKvcgvniidwREMRVRAAMMLL------RVGLKVDLDEKVAN----LSISHKQMLEIAKTLMLDAK 165
                         170       180
                  ....*....|....*....|..
gi 2468698279 663 VLILDDATSALdanSQLQVEQL 684
Cdd:PRK09700  166 VIIMDEPTSSL---TNKEVDYL 184
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
520-733 7.05e-15

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 75.89  E-value: 7.05e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQ---LLLDGKPLPQYEH---------------------R 575
Cdd:PRK13651   22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTiewIFKDEKNKKKTKEkekvleklviqktrfkkikkiK 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 576 YLHRQVAAVGQ--EPQVFGRSLQENIAYGltqkPTMEEITAAAVKSGAHSFIS--GLPQGYdteVGEAGSQLSGGQRQAV 651
Cdd:PRK13651  102 EIRRRVGVVFQfaEYQLFEQTIEKDIIFG----PVSMGVSKEEAKKRAAKYIElvGLDESY---LQRSPFELSGGQKRRV 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 652 ALARALIRKPCVLILDDATSALDANSQLQVEQLLYespELYS--RSVLLITQHL-SLVEQADHILFL-EGGTIREGGTHQ 727
Cdd:PRK13651  175 ALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFD---NLNKqgKTIILVTHDLdNVLEWTKRTIFFkDGKIIKDGDTYD 251

                  ....*.
gi 2468698279 728 QLMEKK 733
Cdd:PRK13651  252 ILSDNK 257
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
520-735 1.68e-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: 72.56  E-value: 1.68e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNL--YQPTEGQLLLDGK---PLPQYEhrylhrqvaavgqepqvfgRS 594
Cdd:cd03217    15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEditDLPPEE-------------------RA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 595 LQeniayGLT---QKPtmEEITAAAVKsgahSFISGLPQGydtevgeagsqLSGGQRQAVALARALIRKPCVLILDDATS 671
Cdd:cd03217    76 RL-----GIFlafQYP--PEIPGVKNA----DFLRYVNEG-----------FSGGEKKRNEILQLLLLEPDLAILDEPDS 133
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2468698279 672 ALDANS----QLQVEQLLYEspelySRSVLLITQHLSLVE--QADHILFLEGGTIREGGTHQ--QLMEKKGC 735
Cdd:cd03217   134 GLDIDAlrlvAEVINKLREE-----GKSVLIITHYQRLLDyiKPDRVHVLYDGRIVKSGDKElaLEIEKKGY 200
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
523-729 1.80e-14

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 75.13  E-value: 1.80e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 523 GLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEH---RYLHRQVAAVGQEPQVfgrSLQ--- 596
Cdd:PRK15079   39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDdewRAVRSDIQMIFQDPLA---SLNprm 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 597 ---ENIAYGL-TQKPTM------EEITAAAVKSGahsFISGLPQGYDTEvgeagsqLSGGQRQAVALARALIRKPCVLIL 666
Cdd:PRK15079  116 tigEIIAEPLrTYHPKLsrqevkDRVKAMMLKVG---LLPNLINRYPHE-------FSGGQCQRIGIARALILEPKLIIC 185
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2468698279 667 DDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQ-ADHILFLEGGTIREGGTHQQL 729
Cdd:PRK15079  186 DEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV 249
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
509-718 2.83e-14

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: 72.30  E-value: 2.83e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 509 SFAYPNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNL---YQPTEGQLLLDGKPLPQYEHRYlHRQVAAVG 585
Cdd:cd03233    11 FTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRtegNVSVEGDIHYNGIPYKEFAEKY-PGEIIYVS 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 586 QEpqvfgrslQENIAYgLTQKPTMEeitaAAVKSGAHSFISGlpqgydtevgeagsqLSGGQRQAVALARALIRKPCVLI 665
Cdd:cd03233    90 EE--------DVHFPT-LTVRETLD----FALRCKGNEFVRG---------------ISGGERKRVSIAEALVSRASVLC 141
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2468698279 666 LDDATSALDANSQLQVEQLLYE-SPELYSRSVLLITQ-HLSLVEQADHILFLEGG 718
Cdd:cd03233   142 WDNSTRGLDSSTALEILKCIRTmADVLKTTTFVSLYQaSDEIYDLFDKVLVLYEG 196
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
520-729 3.22e-14

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


Pssm-ID: 213258 [Multi-domain]  Cd Length: 282  Bit Score: 73.74  E-value: 3.22e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKplpqyehrylhrqVAAVGQEPQVFGRSLQENI 599
Cdd:cd03291    52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQFSWIMPGTIKENI 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 600 AYGLT--QKPTMEEITAAAVKSGahsfISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDans 677
Cdd:cd03291   119 IFGVSydEYRYKSVVKACQLEED----ITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLD--- 191
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2468698279 678 qLQVEQLLYES---PELYSRSVLLITQHLSLVEQADHILFLEGGTIREGGTHQQL 729
Cdd:cd03291   192 -VFTEKEIFEScvcKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
ModC COG4148
ABC-type molybdate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
526-724 3.89e-14

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


Pssm-ID: 226628 [Multi-domain]  Cd Length: 352  Bit Score: 74.30  E-value: 3.89e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 526 FTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYE-------HRylhRQVAAVGQEPQVFGR-SLQE 597
Cdd:COG4148    19 FTLPARGITALFGPSGSGKTSLINMIAGLTRPDEGRIELNGRVLVDAEkgiflppEK---RRIGYVFQDARLFPHyTVRG 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 598 NIAYGL--TQKPTMEEITAAAvksGAHSFISGLPqgydtevgeagSQLSGGQRQAVALARALIRKPCVLILDDATSALDA 675
Cdd:COG4148    96 NLRYGMwkSMRAQFDQLVALL---GIEHLLDRYP-----------GTLSGGEKQRVAIGRALLTAPELLLMDEPLASLDL 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2468698279 676 NSQLQVEQLLYESPELYSRSVLLITQHLSLVEQ-ADHILFLEGGTIREGG 724
Cdd:COG4148   162 PRKREILPYLERLRDEINIPILYVSHSLDEVLRlADRVVVLENGKVKASG 211
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
516-685 4.24e-14

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 75.35  E-value: 4.24e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 516 PDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYqPT---EGQLLLDGKPLPQYEHRYLHRQ-VAAVGQE---- 587
Cdd:PRK13549   16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQASNIRDTERAgIAIIHQElalv 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 588 PQVfgrSLQENIAYGltqkptmEEITA------AAVKSGAHSFISGLpqGYDTEVGEAGSQLSGGQRQAVALARALIRKP 661
Cdd:PRK13549   95 KEL---SVLENIFLG-------NEITPggimdyDAMYLRAQKLLAQL--KLDINPATPVGNLGLGQQQLVEIAKALNKQA 162
                         170       180
                  ....*....|....*....|....
gi 2468698279 662 CVLILDDATSALDANsqlQVEQLL 685
Cdd:PRK13549  163 RLLILDEPTASLTES---ETAVLL 183
CeuD COG4604
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ...
502-731 8.90e-14

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


Pssm-ID: 226963 [Multi-domain]  Cd Length: 252  Bit Score: 71.95  E-value: 8.90e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQV 581
Cdd:COG4604     1 MITIENVSKSYGTKV---VLDDVSLDIPKGGITSIIGPNGAGKSTLLSMMSRLLKKDSGEITIDGLELTSTPSKELAKKL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 582 AAVGQEPQV-----------FGRslqeniaYGLTQ-KPTME--EITAAAVKsgaHSFISGLPQGYDTEvgeagsqLSGGQ 647
Cdd:COG4604    78 SILKQENHInsrltvrdlvgFGR-------FPYSQgRLTKEdrRIINEAIE---YLHLEDLSDRYLDE-------LSGGQ 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 648 RQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQ-ADHILFLEGGTIREGGTH 726
Cdd:COG4604   141 RQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQIMKILRRLADELGKTIVVVLHDINFASCySDHIVALKNGKVVKQGSP 220

                  ....*
gi 2468698279 727 QQLME 731
Cdd:COG4604   221 DEIIQ 225
hmuV PRK13547
heme ABC transporter ATP-binding protein;
520-747 1.30e-13

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 71.78  E-value: 1.30e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 520 VLQGLTFTLRPGEVTALVGPNGSGKST-VAALLQNLYQPTE-------GQLLLDGKPLPQYEHRYLHRQVAAVGQEPQ-V 590
Cdd:PRK13547   16 ILRDLSLRIEPGRVTALLGRNGAGKSTlLKALAGDLTGGGAprgarvtGDVTLNGEPLAAIDAPRLARLRAVLPQAAQpA 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 591 FGRSLQENIAYGltQKPTMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAVALARAL---------IRKP 661
Cdd:PRK13547   96 FAFSAREIVLLG--RYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQPP 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 662 CVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQ-ADHILFLEGGTIREGGTHQQLMEK---KGCYW 737
Cdd:PRK13547  174 RYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARhADRIAMLADGAIVAHGAPADVLTPahiARCYG 253
                         250
                  ....*....|...
gi 2468698279 738 ---AMVQAPADAP 747
Cdd:PRK13547  254 favRLVDAGDGVP 266
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
520-733 1.73e-13

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: 71.42  E-value: 1.73e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 520 VLQGLTFTLRPGEVTALVGPNGSGKSTV-AALLQNLYqpTEGQLLLDGKplpQYEHRYLHRQVAAVGQEPQ---VFGRSL 595
Cdd:cd03289    19 VLENISFSISPGQRVGLLGRTGSGKSTLlSAFLRLLN--TEGDIQIDGV---SWNSVPLQKWRKAFGVIPQkvfIFSGTF 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 596 QENI-AYGltqKPTMEEITAAAVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALD 674
Cdd:cd03289    94 RKNLdPYG---KWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLD 170
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 675 ANSQLQVEQLLYESpelYSRSVLLITQH-LSLVEQADHILFLEGGTIREGGTHQQLMEKK 733
Cdd:cd03289   171 PITYQVIRKTLKQA---FADCTVILSEHrIEAMLECQRFLVIEENKVRQYDSIQKLLNEK 227
cbiO PRK13645
energy-coupling factor transporter ATPase;
507-732 2.01e-13

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 71.58  E-value: 2.01e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 507 DVSFAYPNRP--DVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQ-----YEHRYLHR 579
Cdd:PRK13645   11 NVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAnlkkiKEVKRLRK 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 580 QVAAVGQEP--QVFGRSLQENIAYGltqkptmeEITAAAVKSGAHSFIS------GLPQGYdteVGEAGSQLSGGQRQAV 651
Cdd:PRK13645   91 EIGLVFQFPeyQLFQETIEKDIAFG--------PVNLGENKQEAYKKVPellklvQLPEDY---VKRSPFELSGGQKRRV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 652 ALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQ-ADHILFL-EGGTIREGG----- 724
Cdd:PRK13645  160 ALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRiADEVIVMhEGKVISIGSpfeif 239

                  ....*...
gi 2468698279 725 THQQLMEK 732
Cdd:PRK13645  240 SNQELLTK 247
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only] ...
517-718 2.14e-13

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


Pssm-ID: 226631 [Multi-domain]  Cd Length: 300  Bit Score: 71.62  E-value: 2.14e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 517 DVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQyehrylhRQVAAVGQEPQvfgrslq 596
Cdd:COG4152    14 DKKAVDNISFEVPPGEIFGLLGPNGAGKTTTFRMILGLLEPTEGEITWNGGPLSQ-------EIKNRIGYLPE------- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 597 eniAYGLTQKPTMEEITAaavksgahsFISGLpQGYDT--------------EVGEAGS----QLSGGQRQAVALARALI 658
Cdd:COG4152    80 ---ERGLYPKMTVEDQLK---------YLAEL-KGMPKaeiqkklqawlerlEIVGKKTkkikELSKGNQQKIQFISAVI 146
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2468698279 659 RKPCVLILDDATSALDANSQLQVEQLLYESPElYSRSVLLITQHLSLVEQ-ADHILFLEGG 718
Cdd:COG4152   147 HEPELLILDEPFSGLDPVNVELLKDAIFELKE-EGATIIFSSHRMEHVEElCDRLLMLKKG 206
ABC_6TM_Sav1866_like cd18554
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ...
202-478 5.00e-13

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: 70.53  E-value: 5.00e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 202 MAIPFFTGRLTDWILQD--GSADTFTRNLTLMS-----ILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETE 274
Cdd:cd18554    16 LLLPLILKYIVDDVIQGssLTLDEKVYKLFTIIgimffIFLILRPPVEYYRQYFAQWIANKILYDIRKDLFDHLQKLSLR 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 275 FFQQNQTGNITSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEV 354
Cdd:cd18554    96 YYANNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLVIFPFYILAVKYFFGRLRKLTK 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 355 QVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQ--EIKTLNQKEAVAYAVNSWTTSIS-GMLLKVGilyIGG 431
Cdd:cd18554   176 ERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGhfLTRALKHTRWNAKTFSAVNTITDlAPLLVIG---FAA 252
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 2468698279 432 QLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18554   253 YLVIEGNLTVGTLVAFVGYMERMYSPLRRLVNSFTTLTQSFASMDRV 299
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
503-724 6.77e-13

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 70.83  E-value: 6.77e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPnrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGK---PLPQYEhrylhR 579
Cdd:PRK11000    4 VTLRNVTKAYG---DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKrmnDVPPAE-----R 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 580 QVAAVGQE----PQVfgrSLQENIAYGLT-QKPTMEEI-----TAAAVKSGAHsFISGLPQGydtevgeagsqLSGGQRQ 649
Cdd:PRK11000   76 GVGMVFQSyalyPHL---SVAENMSFGLKlAGAKKEEInqrvnQVAEVLQLAH-LLDRKPKA-----------LSGGQRQ 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 650 AVALARALIRKPCVLILDDATSALDAnsQLQVeQLLYESPELYSR--SVLLITQHlSLVEQ---ADHILFLEGGTIREGG 724
Cdd:PRK11000  141 RVAIGRTLVAEPSVFLLDEPLSNLDA--ALRV-QMRIEISRLHKRlgRTMIYVTH-DQVEAmtlADKIVVLDAGRVAQVG 216
SapD COG4170
ABC-type antimicrobial peptide transport system, ATPase component [Defense mechanisms];
518-731 7.54e-13

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


Pssm-ID: 226639 [Multi-domain]  Cd Length: 330  Bit Score: 70.26  E-value: 7.54e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 518 VLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQP----TEGQLLLDGKPL----PQYEHRYLHRQVAAVGQEPQ 589
Cdd:COG4170    20 VKAVDRVSMTLNEGEIRGLVGESGSGKSLIAKAICGVNKDnwrvTADRMRFDDIDLlrlsPRERRKLVGHNVSMIFQEPQ 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 590 V-------FGRSLQENIA-----------YGLTQKPTMEEITAAAVKSgaHSFISglpQGYDTEVGEagsqlsgGQRQAV 651
Cdd:COG4170   100 ScldpserVGRQLIQNIPawtykgrwwqrFGWRKRRAIELLHRVGIKD--HKDIM---RSYPYELTE-------GECQKV 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 652 ALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHL-SLVEQADHILFLEGGTIREGGTHQQLM 730
Cdd:COG4170   168 MIAIALANQPRLLIADEPTNSMEPTTQAQIFRLLSRLNQNSNTTILLISHDLqMISQWADKINVLYCGQTVESAPSEELV 247

                  .
gi 2468698279 731 E 731
Cdd:COG4170   248 T 248
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
506-700 9.68e-13

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: 71.12  E-value: 9.68e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 506 QDVSFAYPnrPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQllldGKPLPQYEHRYLHrqvaavg 585
Cdd:TIGR03719   8 NRVSKVVP--PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGE----ARPQPGIKVGYLP------- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 586 QEPQ------VFG----------RSLQE----NIAYG---------LTQKPTMEEITAAAvksGAHSFISGL-------- 628
Cdd:TIGR03719  75 QEPQldptktVREnveegvaeikDALDRfneiSAKYAepdadfdklAAEQAELQEIIDAA---DAWDLDSQLeiamdalr 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2468698279 629 -PQGyDTEVgeagSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYEspelYSRSVLLIT 700
Cdd:TIGR03719 152 cPPW-DADV----TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQE----YPGTVVAVT 215
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
517-725 1.20e-12

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 69.49  E-value: 1.20e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 517 DVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQL--------------LLDGKPLPQYEHRY--LHRQ 580
Cdd:PRK13631   38 ELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdiyigdkknnhELITNPYSKKIKNFkeLRRR 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 581 VAAVGQEP--QVFGRSLQENIAYGltqkPTMEEITAAAVKSGAHSFISGLPQGYD-TEVGEAGsqLSGGQRQAVALARAL 657
Cdd:PRK13631  118 VSMVFQFPeyQLFKDTIEKDIMFG----PVALGVKKSEAKKLAKFYLNKMGLDDSyLERSPFG--LSGGQKRRVAIAGIL 191
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2468698279 658 IRKPCVLILDDATSALDANSQLQVEQLLYESPElYSRSVLLITQHLSLV-EQADHILFLEGGTIREGGT 725
Cdd:PRK13631  192 AIQPEILIFDEPTAGLDPKGEHEMMQLILDAKA-NNKTVFVITHTMEHVlEVADEVIVMDKGKILKTGT 259
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
502-713 1.25e-12

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


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 67.98  E-value: 1.25e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYPNrpdVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYE-HRYLHRQ 580
Cdd:PRK11614    5 MLSFDKVSAHYGK---IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQtAKIMREA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 581 VAAVGQEPQVFGR-SLQENIAYG--LTQKPTMEEITAAAVKSgahsfisgLPQGYDTEVGEAGSqLSGGQRQAVALARAL 657
Cdd:PRK11614   82 VAIVPEGRRVFSRmTVEENLAMGgfFAERDQFQERIKWVYEL--------FPRLHERRIQRAGT-MSGGEQQMLAIGRAL 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2468698279 658 IRKPCVLILDDATSAL---------DANSQLQ--------VEQLLYESPELYSRSVLLITQHLSLVEQADHIL 713
Cdd:PRK11614  153 MSQPRLLLLDEPSLGLapiiiqqifDTIEQLReqgmtiflVEQNANQALKLADRGYVLENGHVVLEDTGDALL 225
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
515-729 1.38e-12

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


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 70.85  E-value: 1.38e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 515 RPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNlYQPT----EGQLLLDGKPLpqyEHRYLHRQVAAVgQEPQV 590
Cdd:TIGR00955  35 RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAF-RSPKgvkgSGSVLLNGMPI---DAKEMRAISAYV-QQDDL 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 591 FGRSL--QENIAYGLTQKptMEEITAAAVKSGAHSFI---SGLPQGYDTEVGEAGSQ--LSGGQRQAVALARALIRKPCV 663
Cdd:TIGR00955 110 FIPTLtvREHLMFQAHLR--MPRRVTKKEKRERVDEVlqaLGLRKCANTRIGVPGRVkgLSGGERKRLAFASELLTDPPL 187
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2468698279 664 LILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLS-LVEQADHILFLEGGTIREGGTHQQL 729
Cdd:TIGR00955 188 LFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSeLFELFDKIILMAEGRVAYLGSPDQA 254
BtuD COG4138
ABC-type cobalamin transport system, ATPase component [Coenzyme transport and metabolism];
521-730 1.58e-12

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


Pssm-ID: 226622 [Multi-domain]  Cd Length: 248  Bit Score: 67.95  E-value: 1.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 521 LQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYqPTEGQLLLDGKPLPQYEHRYLHRQVAAVGQepqvfgrslQENia 600
Cdd:COG4138    15 LGPLSGEVRAGEILHLVGPNGAGKSTLLARMAGMT-SGSGSIQFAGQPLEAWSATELARHRAYLSQ---------QQT-- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 601 yGLTQKPTMEEIT---AAAVKSGAHSFISGLpQGYDTEVGEAGSQLSGGQRQAVALARALIR-----KPC--VLILDDAT 670
Cdd:COG4138    83 -PPFAMPVWHYLTlhqPDKTRTELLNDVAGA-LALDDKLGRSTNQLSGGEWQRVRLAAVVLQitpdaNPAgqLLLLDEPM 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2468698279 671 SALDANSQLQVEQLLYESPElYSRSVLLITQHLS-LVEQADHILFLEGGTIREGGTHQQLM 730
Cdd:COG4138   161 NSLDVAQQSALDRLLSALCQ-QGLAIVMSSHDLNhTLRHAHRAWLLKRGKLLASGRREEVL 220
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
524-730 2.04e-12

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 67.65  E-value: 2.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 524 LTFTLRPGEVTALVGPNGSGKSTVAALLQNLYqPTEGQLLLDGKPLPQYEHRYLHRQVAAVGQE-PQVFGRSLQENIAYG 602
Cdd:PRK03695   15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRAYLSQQqTPPFAMPVFQYLTLH 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 603 LTQKPTMEEItAAAVKSGAHSFisglpqGYDTEVGEAGSQLSGGQRQAVALARALIR-----KP--CVLILDDATSALDA 675
Cdd:PRK03695   94 QPDKTRTEAV-ASALNEVAEAL------GLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdiNPagQLLLLDEPMNSLDV 166
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2468698279 676 NSQLQVEQLLYESPELySRSVLLITQHLSLV-EQADHILFLEGGTIREGGTHQQLM 730
Cdd:PRK03695  167 AQQAALDRLLSELCQQ-GIAVVMSSHDLNHTlRHADRVWLLKQGKLLASGRRDEVL 221
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
500-731 2.23e-12

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


Pssm-ID: 132313 [Multi-domain]  Cd Length: 520  Bit Score: 70.22  E-value: 2.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 500 EGLVQFQDVSFAY--PNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQL-LLDG-------KPL 569
Cdd:TIGR03269 277 EPIIKVRNVSKRYisVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnVRVGdewvdmtKPG 356
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 570 PQYEHRyLHRQVAAVGQEPQVFG-RSLQENiaygLTQKPTMEEITAAAVKSGAHSFISGlpqGYDTEVGEA-----GSQL 643
Cdd:TIGR03269 357 PDGRGR-AKRYIGILHQEYDLYPhRTVLDN----LTEAIGLELPDELARMKAVITLKMV---GFDEEKAEEildkyPDEL 428
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 644 SGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLV-EQADHILFLEGGTIRE 722
Cdd:TIGR03269 429 SEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVlDVCDRAALMRDGKIVK 508

                  ....*....
gi 2468698279 723 GGTHQQLME 731
Cdd:TIGR03269 509 IGDPEEIVE 517
3a01203 TIGR00954
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...
427-717 2.60e-12

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: 70.16  E-value: 2.60e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 427 LYIGGQLVTSGAVSSGNLVTfVLYQMQ----FTQAVEVLLSIYPRVQK------AVGSSEKIFEYLDRTPRCPPSGLLtp 496
Cdd:TIGR00954 369 FYNNGRLLLKAADALGRLML-AGRDMTrlagFTARVDTLLQVLDDVKSgnfkrpRVEEIESGREGGRNSNLVPGRGIV-- 445
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 497 LHLEGLVQFQDVSFAYPNRpDVLVlQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYqPTEGQLLLdgKPLPQyehry 576
Cdd:TIGR00954 446 EYQDNGIKFENIPLVTPNG-DVLI-ESLSFEVPSGNNLLICGPNGCGKSSLFRILGELW-PVYGGRLT--KPAKG----- 515
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 577 lhrQVAAVGQEPQVFGRSLQENIAY----------GLTQKpTMEEITaAAVKSGahsFISGLPQGYDTeVGEAGSQLSGG 646
Cdd:TIGR00954 516 ---KLFYVPQRPYMTLGTLRDQIIYpdssedmkrrGLSDK-DLEQIL-DNVQLT---HILEREGGWSA-VQDWMDVLSGG 586
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2468698279 647 QRQAVALARALIRKPCVLILDDATSALdansQLQVEQLLYESPELYSRSVLLITQHLSLVEQADHILFLEG 717
Cdd:TIGR00954 587 EKQRIAMARLFYHKPQFAILDECTSAV----SVDVEGYMYRLCREFGITLFSVSHRKSLWKYHEYLLYMDG 653
ABC_6TM_exporter_like cd18564
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
233-478 2.85e-12

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


Pssm-ID: 350008 [Multi-domain]  Cd Length: 307  Bit Score: 68.31  E-value: 2.85e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 233 ILTIASAVLEFVGDgIYNNTMG-HVHSHLQGEVFGAVLRQETEFFQQNQTGNITSRVTEDTSTLSDSLSENLSLFLWYLV 311
Cdd:cd18564    62 GIALLRGLASYAGT-YLTALVGqRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLL 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 312 RGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEVQVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFR 391
Cdd:cd18564   141 TLVGMLGVMFWLDWQLALIALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFA 220
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 392 EklQEIKTLnQKEAVAYAVNSWTTSISGMLLKVG---ILYIGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRV 468
Cdd:cd18564   221 R--ENRKSL-RAGLRAARLQALLSPVVDVLVAVGtalVLWFGAWLVLAGRLTPGDLLVFLAYLKNLYKPVRDLAKLTGRI 297
                         250
                  ....*....|
gi 2468698279 469 QKAVGSSEKI 478
Cdd:cd18564   298 AKASASAERV 307
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
517-732 2.89e-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: 69.83  E-value: 2.89e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 517 DVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNL--YQPTEGQLLLDGKPLPQYEhrYLHRQvAAVGQEPQVFGRS 594
Cdd:TIGR03269  12 GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHVALCEKCG--YVERP-SKVGEPCPVCGGT 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 595 LQENIA--YGLTQKptmeeITAAAVKSGAHSF----------------ISGLPQ-GYDTE--VGEA-------------- 639
Cdd:TIGR03269  89 LEPEEVdfWNLSDK-----LRRRIRKRIAIMLqrtfalygddtvldnvLEALEEiGYEGKeaVGRAvdliemvqlshrit 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 640 --GSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSvLLITQHLSLV--EQADHILFL 715
Cdd:TIGR03269 164 hiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGIS-MVLTSHWPEVieDLSDKAIWL 242
                         250
                  ....*....|....*..
gi 2468698279 716 EGGTIREGGTHQQLMEK 732
Cdd:TIGR03269 243 ENGEIKEEGTPDEVVAV 259
ABC_6TM_exporter_like cd18565
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
230-478 5.94e-12

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


Pssm-ID: 350009 [Multi-domain]  Cd Length: 313  Bit Score: 67.21  E-value: 5.94e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 230 LMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQNQTGNITSRVTEDTSTLSDSLSENLSLFLWY 309
Cdd:cd18565    59 LTVAAFLLESLFQYLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRV 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 310 LVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEVQVRESLAK-SSQVAiEALSAMPTVRSFANEEGEAQ 388
Cdd:cd18565   139 VVTVLGIGAILFYLNWQLALVALLPVPLIIAGTYWFQRRIEPRYRAVREAVGDlNARLE-NNLSGIAVIKAFTAEDFERE 217
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 389 KFREKLQEIKTLNQKeavAYAVNSWTTSISGMLLKVG---ILYIGGQLVTSGAV------SSGNLVTFVLYQMQFTQAVE 459
Cdd:cd18565   218 RVADASEEYRDANWR---AIRLRAAFFPVIRLVAGAGfvaTFVVGGYWVLDGPPlftgtlTVGTLVTFLFYTQRLLWPLT 294
                         250
                  ....*....|....*....
gi 2468698279 460 VLLSIYPRVQKAVGSSEKI 478
Cdd:cd18565   295 RLGDLIDQYQRAMASAKRV 313
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
530-702 8.60e-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: 63.55  E-value: 8.60e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279  530 PGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLldgkplpqyehrylhrqvaavgqepqvfgrslqeniaygltqkptm 609
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVI---------------------------------------------- 34
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279  610 eeitaaaVKSGAHSFISGLPQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQ-----LQVEQL 684
Cdd:smart00382  35 -------YIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEallllLEELRL 107
                          170
                   ....*....|....*...
gi 2468698279  685 LYESPELYSRSVLLITQH 702
Cdd:smart00382 108 LLLLKSEKNLTVILTTND 125
ABC_6TM_Rv0194_D1_like cd18543
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ...
201-478 1.20e-11

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


Pssm-ID: 349987 [Multi-domain]  Cd Length: 291  Bit Score: 65.97  E-value: 1.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 201 EMAIPFFTGRLTDWILQDGSadtfTRNLTLMSILTIASAVLEFVGDGIYNNTMG----HVHSHLQGEVFGAVLRQETEFF 276
Cdd:cd18543    15 GLAIPLLTRRAIDGPIAHGD----RSALWPLVLLLLALGVAEAVLSFLRRYLAGrlslGVEHDLRTDLFAHLQRLDGAFH 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 277 QQNQTGNITSRVTEDTSTLSDSLSeNLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEVQV 356
Cdd:cd18543    91 DRWQSGQLLSRATSDLSLVQRFLA-FGPFLLGNLLTLVVGLVVMLVLSPPLALVALASLPPLVLVARRFRRRYFPASRRA 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 357 RESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTS 436
Cdd:cd18543   170 QDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWPLLEALPELGLAAVLALGGWLVAN 249
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 2468698279 437 GAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18543   250 GSLTLGTLVAFSAYLTMLVWPVRMLGWLLAMAQRARAAAERV 291
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
517-675 2.02e-11

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: 66.77  E-value: 2.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 517 DVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQ--PTEGQLLLDGKPLPQYEHRYLHRQ-VAAVGQE-PQVFG 592
Cdd:TIGR02633  13 GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLKASNIRDTERAgIVIIHQElTLVPE 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 593 RSLQENIAYGltqkptmEEITA-------AAVKSGAHSFISGLpQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVLI 665
Cdd:TIGR02633  93 LSVAENIFLG-------NEITLpggrmayNAMYLRAKNLLREL-QLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLLI 164
                         170
                  ....*....|
gi 2468698279 666 LDDATSALDA 675
Cdd:TIGR02633 165 LDEPSSSLTE 174
ABC_6TM_Rv0194_D2_like cd18546
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ...
202-478 2.02e-11

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: 65.59  E-value: 2.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 202 MAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGDgIYNNTMGH-VHSHLQGEVFGAVLRQETEFFQQNQ 280
Cdd:cd18546    16 LAGPLLVRYGIDSGVRAGDLGVLLLAAAAYLAVVLAGWVAQRAQT-RLTGRTGErLLYDLRLRVFAHLQRLSLDFHERET 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 281 TGNITSRVTEDTSTLSDSLSENLSLFLwylVRGLCLLGI---MLWGSVSLTMVTLVTLPLLFLlpkkVGKWYQLLEV--- 354
Cdd:cd18546    95 SGRIMTRMTSDIDALSELLQTGLVQLV---VSLLTLVGIavvLLVLDPRLALVALAALPPLAL----ATRWFRRRSSray 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 355 -QVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQL 433
Cdd:cd18546   168 rRARERIAAVNADLQETLAGIRVVQAFRRERRNAERFAELSDDYRDARLRAQRLVAIYFPGVELLGNLATAAVLLVGAWR 247
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2468698279 434 VTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18546   248 VAAGTLTVGVLVAFLLYLRRFFAPIQQLSQVFDSYQQARAALEKI 292
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
483-731 3.46e-11

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


Pssm-ID: 224053 [Multi-domain]  Cd Length: 500  Bit Score: 66.38  E-value: 3.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 483 DRTPRCPPSGLLTP-LHLEGL---VQFQDVSFaypnrpdvlvlqgltfTLRPGEVTALVGPNGSGKSTVAALLQNLYQPT 558
Cdd:COG1129   249 DLFPEPPEEGIGEPvLEVRNLsggGKVRDVSF----------------TVRAGEILGIAGLVGAGRTELARALFGARPAS 312
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 559 EGQLLLDGKPLPQY-EHRYLHRQVAAVGQEPQ----VFGRSLQENIAYG-LTQKPTMEEITAAAVKSGAHSFISGL---P 629
Cdd:COG1129   313 SGEILLDGKPVRIRsPRDAIKAGIAYVPEDRKseglVLDMSIAENITLAsLRRFSRRGLIDRRKERALAERYIRRLrikT 392
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 630 QGYDTEVGEagsqLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYEspelYSR---SVLLITQHLS-L 705
Cdd:COG1129   393 PSPEQPIGT----LSGGNQQKVVLARWLATDPKVLILDEPTRGIDVGAKAEIYRLIRE----LAAegkAILMISSELPeL 464
                         250       260       270
                  ....*....|....*....|....*....|.
gi 2468698279 706 VEQADHILFLEGGTI-----REGGTHQQLME 731
Cdd:COG1129   465 LGLSDRILVMREGRIvgeldREEATEEAIMA 495
ABC_6TM_HetC_like cd18568
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ...
203-478 3.59e-11

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: 64.50  E-value: 3.59e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 203 AIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQNQTG 282
Cdd:cd18568    20 ALPLFTQIILDRVLVHKNISLLNLILIGLLIVGIFQILLSAVRQYLLDYFANRIDLSLLSDFYKHLLSLPLSFFASRKVG 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 283 NITSRVTEdTSTLSDSLSEN-LSLFLwYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEVQVRESLA 361
Cdd:cd18568   100 DIITRFQE-NQKIRRFLTRSaLTTIL-DLLMVFIYLGLMFYYNLQLTLIVLAFIPLYVLLTLLSSPKLKRNSREIFQANA 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 362 KSSQVAIEALSAMPTVRSFANEegeaQKFREKLQE--IKTLNQ--KEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSG 437
Cdd:cd18568   178 EQQSFLVEALTGIATIKALAAE----RPIRWRWENkfAKALNTrfRGQKLSIVLQLISSLINHLGTIAVLWYGAYLVISG 253
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 2468698279 438 AVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18568   254 QLTIGQLVAFNMLFGSVINPLLALVGLWDELQETRISVERL 294
YufO COG3845
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
502-720 5.06e-11

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


Pssm-ID: 226364 [Multi-domain]  Cd Length: 501  Bit Score: 65.64  E-value: 5.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSfAYPNRPdVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHRQ- 580
Cdd:COG3845   257 VLEVEDLS-VKDRRG-VTAVKDVSFEVRAGEIVGIAGVAGNGQSELVEAISGLRKPASGRILLNGKDVLGRLSPRERRRl 334
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 581 -VAAVGQEPQ----VFGRSLQENIA-----------YGLTQKPTMEEITAAAVKSgahsfisglpqgYDTEVGEAGS--- 641
Cdd:COG3845   335 gLAYVPEDRHghglVLDLSLAENLVlgrhdkkpfsrGGFLDRRAIRKFARELIEE------------FDVRAPSPDApar 402
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 642 QLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYEspelySRS----VLLITQHL-SLVEQADHILFLE 716
Cdd:COG3845   403 SLSGGNQQKLILARELARRPDLLIAAQPTRGLDVGAIEFIHERLLE-----LRDagkaVLLISEDLdEILELSDRIAVIY 477

                  ....
gi 2468698279 717 GGTI 720
Cdd:COG3845   478 EGRI 481
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
500-668 6.64e-11

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 63.63  E-value: 6.64e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 500 EGLVQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLHR 579
Cdd:PRK11831    5 ANLVDMRGVSFTRGNRC---IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 580 ---------QVAAVGQEPQVFgrslqENIAYGL---TQKP-------TMEEITAAAVKSGAHSfisgLPqgydtevgeag 640
Cdd:PRK11831   82 vrkrmsmlfQSGALFTDMNVF-----DNVAYPLrehTQLPapllhstVMMKLEAVGLRGAAKL----MP----------- 141
                         170       180
                  ....*....|....*....|....*...
gi 2468698279 641 SQLSGGQRQAVALARALIRKPCVLILDD 668
Cdd:PRK11831  142 SELSGGMARRAALARAIALEPDLIMFDE 169
ABC_6TM_Pgp_ABCB1 cd18558
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ...
225-478 6.95e-11

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: 64.22  E-value: 6.95e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 225 TRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQNQTGNITSRVTEDTSTLSDSLSENLS 304
Cdd:cd18558    59 TLYAYYYLIIGAIVLITAYIQGSFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIG 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 305 LFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPkkvGKWYQLLEVQV---RESLAKSSQVAIEALSAMPTVRSFA 381
Cdd:cd18558   139 VIFQNIATFGTGFIIGFIRGWKLTLVILAISPVLGLSA---VVWAKILSGFTdkeKKAYAKAGAVAEEVLEAFRTVIAFG 215
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 382 NEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVL 461
Cdd:cd18558   216 GQQKEETRYAQNLEIAKRNGIKKAITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGEVLTVFFSVLIGAFSAGQQ 295
                         250
                  ....*....|....*..
gi 2468698279 462 LSIYPRVQKAVGSSEKI 478
Cdd:cd18558   296 VPSIEAFANARGAAYHI 312
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
506-702 8.67e-11

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 62.60  E-value: 8.67e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 506 QDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGK-----PLpqyeHRYLHRQ 580
Cdd:PRK10895    7 KNLAKAYKGRR---VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdisllPL----HARARRG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 581 VAAVGQEPQVFGR-SLQENIAYGLTQKptmEEITAAAVKSGAHSFISGLPQGYDTEvgEAGSQLSGGQRQAVALARALIR 659
Cdd:PRK10895   80 IGYLPQEASIFRRlSVYDNLMAVLQIR---DDLSAEQREDRANELMEEFHIEHLRD--SMGQSLSGGERRRVEIARALAA 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2468698279 660 KPCVLILDDATSALDANSQLQVEQLLyESPELYSRSVlLITQH 702
Cdd:PRK10895  155 NPKFILLDEPFAGVDPISVIDIKRII-EHLRDSGLGV-LITDH 195
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
642-725 1.95e-10

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 62.84  E-value: 1.95e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 642 QLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLV-EQADHILFLEGGTI 720
Cdd:PRK11022  153 QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVaEAAHKIIVMYAGQV 232

                  ....*
gi 2468698279 721 REGGT 725
Cdd:PRK11022  233 VETGK 237
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
524-725 2.44e-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: 64.26  E-value: 2.44e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279  524 LTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPL--------------PQYEHRYLHRQVAavgqEPQ 589
Cdd:TIGR01257  949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIetnldavrqslgmcPQHNILFHHLTVA----EHI 1024
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279  590 VFGRSLQeniayGLTQKPTMEEITAAAVKSGAHSfisglpqgydtEVGEAGSQLSGGQRQAVALARALIRKPCVLILDDA 669
Cdd:TIGR01257 1025 LFYAQLK-----GRSWEEAQLEMEAMLEDTGLHH-----------KRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEP 1088
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2468698279  670 TSALDANSQLQVEQLL--YESpelySRSVLLITQHLSLVE-QADHILFLEGGTIREGGT 725
Cdd:TIGR01257 1089 TSGVDPYSRRSIWDLLlkYRS----GRTIIMSTHHMDEADlLGDRIAIISQGRLYCSGT 1143
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
506-700 2.57e-10

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 63.60  E-value: 2.57e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 506 QDVSFAYPnrPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGqlllDGKPLPQYEHRYLHrqvaavg 585
Cdd:PRK11819   10 NRVSKVVP--PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEG----EARPAPGIKVGYLP------- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 586 QEPQV-FGRSLQENIAYGLTQKP----------------------------TMEEITAAAvksGAHSFIS---------G 627
Cdd:PRK11819   77 QEPQLdPEKTVRENVEEGVAEVKaaldrfneiyaayaepdadfdalaaeqgELQEIIDAA---DAWDLDSqleiamdalR 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2468698279 628 LPQGyDTEVgeagSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYEspelYSRSVLLIT 700
Cdd:PRK11819  154 CPPW-DAKV----TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHD----YPGTVVAVT 217
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
495-682 2.61e-10

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


Pssm-ID: 227118 [Multi-domain]  Cd Length: 235  Bit Score: 61.29  E-value: 2.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 495 TPLHLEGLVQfqdvSFAYPNRPDVL--VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLL----DGKP 568
Cdd:COG4778     3 TPLNVSNVSK----TFTLHQQGGVRlpVLRNVSLSVNAGECVVLHGPSGSGKSTLLRSLYANYLPDEGQILVrhegEWVD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 569 LPQYEHRYL----HRQVAAVGQepqvFGRSLQENIAYGLTQKPTMEE-ITAAAVKSGAHSFISGLpqgydtEVGE----- 638
Cdd:COG4778    79 LVTAEPREVlevrRTTIGYVSQ----FLRVIPRVSALDVVAEPLLARgVPREVARAKAADLLTRL------NLPErlwsl 148
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2468698279 639 AGSQLSGGQRQAVALARALIRKPCVLILDDATSALDA-NSQLQVE 682
Cdd:COG4778   149 APATFSGGEQQRVNIARGFIVDYPILLLDEPTASLDAtNRAVVVE 193
ABC_6TM_CyaB_HlyB_like cd18588
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ...
203-478 3.81e-10

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: 61.75  E-value: 3.81e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 203 AIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQNQTG 282
Cdd:cd18588    20 VTPLFFQVIIDKVLVHRSLSTLDVLAIGLLVVALFEAVLSGLRTYLFSHTTNRIDAELGARLFRHLLRLPLSYFESRQVG 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 283 NITSRVTEdTSTLSDSLSEN-LSLFLwYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQ-LLEVQVRESl 360
Cdd:cd18588   100 DTVARVRE-LESIRQFLTGSaLTLVL-DLVFSVVFLAVMFYYSPTLTLIVLASLPLYALLSLLVTPILRrRLEEKFQRG- 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 361 AKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKeavAYAVNSWTTSISGMLLK---VGILYIGGQLVTSG 437
Cdd:cd18588   177 AENQSFLVETVTGIETVKSLAVEPQFQRRWEELLARYVKASFK---TANLSNLASQIVQLIQKlttLAILWFGAYLVMDG 253
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 2468698279 438 AVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18588   254 ELTIGQLIAFNMLAGQVSQPVLRLVQLWQDFQQAKVSVERL 294
sufC TIGR01978
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ...
517-737 4.47e-10

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: 60.74  E-value: 4.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 517 DVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALL--QNLYQPTEGQLLLDGKPLPQYE--HRylhrqvAAVG-----QE 587
Cdd:TIGR01978  12 DKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIagHPSYEVTSGTILFKGQDLLELEpdER------ARAGlflafQY 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 588 P-QVFGRSLQENIAYGLT---QKPTMEEITAAAVKSGAHSFISGLpqGYDTEVGEAGSQ--LSGGQRQAVALARALIRKP 661
Cdd:TIGR01978  86 PeEIPGVSNLEFLRSALNarrSARGEEPLDLLDFEKLLKEKLALL--DMDEEFLNRSVNegFSGGEKKRNEILQMALLEP 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 662 CVLILDDATSALDANS-QLQVEQL-LYESPElysRSVLLITQHLSLVE--QADHILFLEGGTI-REGGTHqqLM---EKK 733
Cdd:TIGR01978 164 KLAILDEIDSGLDIDAlKIVAEGInRLREPD---RSFLIITHYQRLLNyiKPDYVHVLLDGRIvKSGDVE--LAkelEAK 238

                  ....
gi 2468698279 734 GCYW 737
Cdd:TIGR01978 239 GYDW 242
PLN03073 PLN03073
ABC transporter F family; Provisional
502-703 5.22e-10

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 62.96  E-value: 5.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYPNRPdvLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLpqyehrylhrqv 581
Cdd:PLN03073  508 IISFSDASFGYPGGP--LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVR------------ 573
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 582 AAVGQEPQVFGRSLQEN-IAYGLTQKPTMEEitaaaVKSGAH--SF-ISG---LPQGYdtevgeagsQLSGGQRQAVALA 654
Cdd:PLN03073  574 MAVFSQHHVDGLDLSSNpLLYMMRCFPGVPE-----QKLRAHlgSFgVTGnlaLQPMY---------TLSGGQKSRVAFA 639
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2468698279 655 RALIRKPCVLILDDATSALDANSqlqVEQLLyESPELYSRSVLLIT--QHL 703
Cdd:PLN03073  640 KITFKKPHILLLDEPSNHLDLDA---VEALI-QGLVLFQGGVLMVShdEHL 686
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
497-673 5.67e-10

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 62.33  E-value: 5.67e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 497 LHLEGLvqfqDVSFaypnrPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRy 576
Cdd:PRK10762    5 LQLKGI----DKAF-----PGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPK- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 577 lHRQVAAVG---QE----PQVfgrSLQENIAYGLTQKPTMEEITAAAVKSGAHSFIS--GLPQGYDTEVGEagsqLSGGQ 647
Cdd:PRK10762   75 -SSQEAGIGiihQElnliPQL---TIAENIFLGREFVNRFGRIDWKKMYAEADKLLArlNLRFSSDKLVGE----LSIGE 146
                         170       180
                  ....*....|....*....|....*.
gi 2468698279 648 RQAVALARALIRKPCVLILDDATSAL 673
Cdd:PRK10762  147 QQMVEIAKVLSFESKVIIMDEPTDAL 172
ABCG_PDR_domain2 cd03232
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...
503-718 5.98e-10

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: 59.18  E-value: 5.98e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYP-NRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTvaaLLQNLYQPT-----EGQLLLDGKPLPQyehrY 576
Cdd:cd03232     4 LTWKNLNYTVPvKGGKRQLLNNISGYVKPGTLTALMGESGAGKTT---LLDVLAGRKtagviTGEILINGRPLDK----N 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 577 LHRQVAAVGQEPQVFGrslqeniayGLTQKPTMEeitaaavksgahsfISGLPQGydtevgeagsqLSGGQRQAVALARA 656
Cdd:cd03232    77 FQRSTGYVEQQDVHSP---------NLTVREALR--------------FSALLRG-----------LSVEQRKRLTIGVE 122
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2468698279 657 LIRKPCVLILDDATSALDANSQLQVEQLLYESPElYSRSVLL-ITQ-HLSLVEQADHILFLEGG 718
Cdd:cd03232   123 LAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLAD-SGQAILCtIHQpSASIFEKFDRLLLLKRG 185
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
527-681 6.20e-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: 60.11  E-value: 6.20e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 527 TLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPL---PQY-EHRY-------LHRQVAAVGQEPQvfgrsL 595
Cdd:cd03237    21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVsykPQYiKADYegtvrdlLSSITKDFYTHPY-----F 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 596 QENIAygltqKPTMEEitaaavksgahsfisglpQGYDTEVGEagsqLSGGQRQAVALARALIRKPCVLILDDATSALDA 675
Cdd:cd03237    96 KTEIA-----KPLQIE------------------QILDREVPE----LSGGELQRVAIAACLSKDADIYLLDEPSAYLDV 148

                  ....*.
gi 2468698279 676 NSQLQV 681
Cdd:cd03237   149 EQRLMA 154
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
503-717 6.39e-10

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: 62.26  E-value: 6.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPNRpdvLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLdGKPLpqyehrylhrQVA 582
Cdd:TIGR03719 323 IEAENLTKAFGDK---LLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV----------KLA 388
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 583 AVGQEPQVF--GRSLQENIAYGLtqkptmEEITAAAVKSGAHSFISGLP-QGYDTE--VGeagsQLSGGQRQAVALARAL 657
Cdd:TIGR03719 389 YVDQSRDALdpNKTVWEEISGGL------DIIKLGKREIPSRAYVGRFNfKGSDQQkkVG----QLSGGERNRVHLAKTL 458
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2468698279 658 IRKPCVLILDDATSALDansqlqVEQL--LYESPELYSRSVLLITqH----LSLVeqADHILFLEG 717
Cdd:TIGR03719 459 KSGGNVLLLDEPTNDLD------VETLraLEEALLNFAGCAVVIS-HdrwfLDRI--ATHILAFEG 515
PLN03211 PLN03211
ABC transporter G-25; Provisional
520-729 7.34e-10

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 62.20  E-value: 7.34e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPT--EGQLLL-DGKPLPQyehryLHRQVAAVGQEPQVFGR-SL 595
Cdd:PLN03211   83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILAnNRKPTKQ-----ILKRTGFVTQDDILYPHlTV 157
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 596 QENIAY-GLTQKPtmEEITAAAVKSGAHSFIS--GLPQGYDTEVGEAGSQ-LSGGQRQAVALARALIRKPCVLILDDATS 671
Cdd:PLN03211  158 RETLVFcSLLRLP--KSLTKQEKILVAESVISelGLTKCENTIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDEPTS 235
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 672 ALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQA-DHILFL-EGGTIREGGTHQQL 729
Cdd:PLN03211  236 GLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMfDSVLVLsEGRCLFFGKGSDAM 295
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
516-684 7.74e-10

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 62.05  E-value: 7.74e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 516 PDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLP-QYEHRYLHRQVAAVGQE-PQVFGR 593
Cdd:PRK10982    9 PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQElNLVLQR 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 594 SLQENIAYGltQKPT---------MEEITAAAVKSgahsfisglpQGYDTEVGEAGSQLSGGQRQAVALARALIRKPCVL 664
Cdd:PRK10982   89 SVMDNMWLG--RYPTkgmfvdqdkMYRDTKAIFDE----------LDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIV 156
                         170       180
                  ....*....|....*....|
gi 2468698279 665 ILDDATSALdanSQLQVEQL 684
Cdd:PRK10982  157 IMDEPTSSL---TEKEVNHL 173
ABC_6TM_Tm287_like cd18548
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ...
200-469 9.12e-10

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: 60.49  E-value: 9.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 200 GEMAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLefvgdGIYNNTMGhvhSHL-QGevFGAVLRQET----- 273
Cdd:cd18548    14 LELLLPTLMADIIDEGIANGDLSYILRTGLLMLLLALLGLIA-----GILAGYFA---AKAsQG--FGRDLRKDLfekiq 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 274 ----EFFQQNQTGNITSRVTEDTSTLSDSLSenlsLFLWYLVRG--LCLLGI--MLWGSVSLTMVTLVT----LPLLFLL 341
Cdd:cd18548    84 sfsfAEIDKFGTSSLITRLTNDVTQVQNFVM----MLLRMLVRApiMLIGAIimAFRINPKLALILLVAipilALVVFLI 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 342 PKKVGKWYQllevQVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNS-WTTSISGM 420
Cdd:cd18548   160 MKKAIPLFK----KVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNpLMMLIMNL 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2468698279 421 LLkVGILYIGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVL---LSIYPRVQ 469
Cdd:cd18548   236 AI-VAILWFGGHLINAGSLQVGDLVAFINYLMQILMSLMMLsmvFVMLPRAS 286
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
507-711 9.44e-10

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127 [Multi-domain]  Cd Length: 200  Bit Score: 58.81  E-value: 9.44e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 507 DVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYlHRQVAAVGQ 586
Cdd:PRK13540    6 ELDFDYHDQP---LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTY-QKQLCFVGH 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 587 EPQVFGR-SLQENIAYGLTQKPTMEEITAAAVKSGAHSFISgLPQGYdtevgeagsqLSGGQRQAVALARALIRKPCVLI 665
Cdd:PRK13540   82 RSGINPYlTLRENCLYDIHFSPGAVGITELCRLFSLEHLID-YPCGL----------LSSGQKRQVALLRLWMSKAKLWL 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2468698279 666 LDDATSALDansQLQVEQLLYESPELYSR-SVLLITQHLSL-VEQADH 711
Cdd:PRK13540  151 LDEPLVALD---ELSLLTIITKIQEHRAKgGAVLLTSHQDLpLNKADY 195
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
504-715 1.39e-09

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


Pssm-ID: 225265 [Multi-domain]  Cd Length: 593  Bit Score: 61.40  E-value: 1.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 504 QFQDVSFAYPNRPDVL---VLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQ--------NLYQPTEGQLLLDGKPLPQY 572
Cdd:COG2401   379 EFQDILESFGVRQRVIeryVLRNLNLEIKPGDVVAVVGQSGAGKTTLLRMILgaqkgrgeEKYRPDSGKVEVPKNTVSAL 458
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 573 EHRYLhrqvaavgqEPQVFGRSLQENIAYGLTQKPTMEEITAAAVKSGAHSFISGLpqgydtevgeagSQLSGGQRQAVA 652
Cdd:COG2401   459 IPGEY---------EPEFGEVTILEHLRSKTGDLNAAVEILNRAGLSDAVLYRRKF------------SELSTGQKERAK 517
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2468698279 653 LARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQ--ADHILFL 715
Cdd:COG2401   518 LAKLLAERPNVLLIDEFAAHLDELTAVRVARKISELAREAGITLIVVTHRPEVGNAlrPDTLILV 582
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
521-725 1.51e-09

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 59.51  E-value: 1.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 521 LQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRYLhrqVAAVGQEPQVFGR--SLQEN 598
Cdd:PRK15056   23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VAYVPQSEEVDWSfpVLVED 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 599 IAY-------GLTQKPTMEE---ITAAAVKSGAHSFisglpqgYDTEVGEagsqLSGGQRQAVALARALIRKPCVLILDD 668
Cdd:PRK15056  100 VVMmgryghmGWLRRAKKRDrqiVTAALARVDMVEF-------RHRQIGE----LSGGQKKRVFLARAIAQQGQVILLDE 168
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2468698279 669 ATSALDANSQLQVEQLLYESPElYSRSVLLITQHL-SLVEQADHILFLEGGTIREGGT 725
Cdd:PRK15056  169 PFTGVDVKTEARIISLLRELRD-EGKTMLVSTHNLgSVTEFCDYTVMVKGTVLASGPT 225
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
516-717 1.65e-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: 59.30  E-value: 1.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 516 PDVLVLQGLTfTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQL--------LLD---GKPLPQYEHRYLHRQVAAV 584
Cdd:cd03236    12 PNSFKLHRLP-VPREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppdwdeILDefrGSELQNYFTKLLEGDVKVI 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 585 gQEPQ---VFGRSLQENIAYGLTQKP---TMEEITAAAvksgahsfisGLPQGYDTEVgeagSQLSGGQRQAVALARALI 658
Cdd:cd03236    91 -VKPQyvdLIPKAVKGKVGELLKKKDergKLDELVDQL----------ELRHVLDRNI----DQLSGGELQRVAIAAALA 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 659 RKPCVLILDDATSALDANSQLQVEQLLYESPElYSRSVLLITQHLSLVEQ-ADHILFLEG 717
Cdd:cd03236   156 RDADFYFFDEPSSYLDIKQRLNAARLIRELAE-DDNYVLVVEHDLAVLDYlSDYIHCLYG 214
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
527-718 4.14e-09

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


Pssm-ID: 224166 [Multi-domain]  Cd Length: 591  Bit Score: 59.62  E-value: 4.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 527 TLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQllLDGKPLPQYEHRYLHrqvaavGQEPQVFGRSLQENiAYGLTQK 606
Cdd:COG1245    96 TPRPGKVVGILGPNGIGKSTALKILAGELKPNLGR--YEDPPSWDEVIKRFR------GTELQNYFKKLYEG-ELRAVHK 166
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 607 PTMEEITAAAVKSGAHSFIS---------------GLPQGYDTEVgeagSQLSGGQRQAVALARALIRKPCVLILDDATS 671
Cdd:COG1245   167 PQYVDLIPKVVKGKVGELLKkvdergkfdevverlGLENVLDRDV----SELSGGELQRVAIAAALLRDADVYFFDEPSS 242
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2468698279 672 ALDANSQLQVEQLLYESPElYSRSVLLITQHLSLVEQ-AD--HILFLEGG 718
Cdd:COG1245   243 YLDIRQRLNAARVIRELAE-DGKYVIVVEHDLAVLDYlSDfvHILYGEPG 291
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
527-683 4.30e-09

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 59.82  E-value: 4.30e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 527 TLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPL--PQY-EHRYLHRQVAAVGQEPQVFGRS-LQENIAYG 602
Cdd:PRK13409  361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELKISykPQYiKPDYDGTVEDLLRSITDDLGSSyYKSEIIKP 440
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 603 LtqkptmeeitaaavksgahsfisGLPQGYDTEVGEagsqLSGGQRQAVALARALIRKPCVLILDDATSALDansqlqVE 682
Cdd:PRK13409  441 L-----------------------QLERLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLD------VE 487

                  .
gi 2468698279 683 Q 683
Cdd:PRK13409  488 Q 488
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
525-747 5.39e-09

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 59.15  E-value: 5.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 525 TFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPqyehryLHRQVAAV-----------GQEPQVFGR 593
Cdd:PRK11288  273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPID------IRSPRDAIragimlcpedrKAEGIIPVH 346
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 594 SLQENIA---------YGLTQKPTMEEITAAavksgahSFISGL----PQGyDTEVGeagsQLSGGQRQAVALARALIRK 660
Cdd:PRK11288  347 SVADNINisarrhhlrAGCLINNRWEAENAD-------RFIRSLniktPSR-EQLIM----NLSGGNQQKAILGRWLSED 414
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 661 PCVLILDDATSALDANSQLQVEQLLYESPElYSRSVLLITQHLSLVEQ-ADHILFLEGGTIREGGTHQQLMEKKGCYWAM 739
Cdd:PRK11288  415 MKVILLDEPTRGIDVGAKHEIYNVIYELAA-QGVAVLFVSSDLPEVLGvADRIVVMREGRIAGELAREQATERQALSLAL 493

                  ....*...
gi 2468698279 740 VQAPADAP 747
Cdd:PRK11288  494 PRTSAAVA 501
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
524-720 5.51e-09

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 59.29  E-value: 5.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 524 LTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHR-YLHRQVAAVGQEPQVFGRSLQENIAY- 601
Cdd:PRK15439  282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAqRLARGLVYLPEDRQSSGLYLDAPLAWn 361
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 602 ---------GLTQKPTMEeitaAAVKSGAHSFISGLPQGYDTEVGeagsQLSGGQRQAVALARALIRKPCVLILDDATSA 672
Cdd:PRK15439  362 vcalthnrrGFWIKPARE----NAVLERYRRALNIKFNHAEQAAR----TLSGGNQQKVLIAKCLEASPQLLIVDEPTRG 433
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2468698279 673 LDANSQLQVEQLLyESPELYSRSVLLITQHLSLVEQ-ADHILFLEGGTI 720
Cdd:PRK15439  434 VDVSARNDIYQLI-RSIAAQNVAVLFISSDLEEIEQmADRVLVMHQGEI 481
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
521-725 8.23e-09

ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.


Pssm-ID: 213205 [Multi-domain]  Cd Length: 176  Bit Score: 55.41  E-value: 8.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 521 LQGLTFTLRPGEVTALVGPNGSGKSTVaaLLQNLYqpTEGQLLLDgKPLPQYEHrylhrqvaavgqEPQVFGRSLQENIA 600
Cdd:cd03238    11 LQNLDVSIPLNVLVVVTGVSGSGKSTL--VNEGLY--ASGKARLI-SFLPKFSR------------NKLIFIDQLQFLID 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 601 YGLtqkptmeeitaaavksgahsfisglpqGYDTeVGEAGSQLSGGQRQAVALARALIR--KPCVLILDDATSALDansQ 678
Cdd:cd03238    74 VGL---------------------------GYLT-LGQKLSTLSGGELQRVKLASELFSepPGTLFILDEPSTGLH---Q 122
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2468698279 679 LQVEQLLYESPELYSR--SVLLITQHLSLVEQADHILFLEGGTIREGGT 725
Cdd:cd03238   123 QDINQLLEVIKGLIDLgnTVILIEHNLDVLSSADWIIDFGPGSGKSGGK 171
sufC PRK09580
cysteine desulfurase ATPase component; Reviewed
520-737 1.45e-08

cysteine desulfurase ATPase component; Reviewed


Pssm-ID: 181965 [Multi-domain]  Cd Length: 248  Bit Score: 56.34  E-value: 1.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 520 VLQGLTFTLRPGEVTALVGPNGSGKSTVAALL--QNLYQPTEGQLLLDGKPL----P------------QY--------E 573
Cdd:PRK09580   16 ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLlelsPedragegifmafQYpveipgvsN 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 574 HRYLHRQVAAV----GQEPQ---VFGRSLQENIAygLTQKPtmEEITAAAVKSGahsfisglpqgydtevgeagsqLSGG 646
Cdd:PRK09580   96 QFFLQTALNAVrsyrGQEPLdrfDFQDLMEEKIA--LLKMP--EDLLTRSVNVG----------------------FSGG 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 647 QRQAVALARALIRKPCVLILDDATSALDANSqLQVEQLLYESPELYSRSVLLITQHLSLVE--QADHILFLEGGTIREGG 724
Cdd:PRK09580  150 EKKRNDILQMAVLEPELCILDESDSGLDIDA-LKIVADGVNSLRDGKRSFIIVTHYQRILDyiKPDYVHVLYQGRIVKSG 228
                         250
                  ....*....|....*
gi 2468698279 725 THQ--QLMEKKGCYW 737
Cdd:PRK09580  229 DFTlvKQLEEQGYGW 243
PhnK COG4107
ABC-type phosphonate transport system, ATPase component [Inorganic ion transport and ...
524-731 1.77e-08

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


Pssm-ID: 226592 [Multi-domain]  Cd Length: 258  Bit Score: 55.91  E-value: 1.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 524 LTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQL---LLDGKPLPQY-----EHRYLHR-------QVAAVGQEP 588
Cdd:COG4107    25 VSFDLYPGEVLGIVGESGSGKTTLLKCISGRLTPDAGTVtyrMRDGQPRDLYtmseaERRRLLRtewgfvhQNPRDGLRM 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 589 QVfgrSLQENIA----------YGltqkptmeEITAAAVKSGAHSFISglpqgyDTEVGEAGSQLSGGQRQAVALARALI 658
Cdd:COG4107   105 QV---SAGGNIGerlmaigarhYG--------NIRAEAQDWLEEVEID------LDRIDDLPRTFSGGMQQRLQIARNLV 167
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2468698279 659 RKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVE-QADHILFLEGGTIREGGTHQQLME 731
Cdd:COG4107   168 TRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARlLADRLMVMKQGQVVESGLTDRVLD 241
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
519-722 1.82e-08

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 57.87  E-value: 1.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 519 LVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDG---------------KPLPQY------EHRYL 577
Cdd:PRK10636   15 VLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGnwqlawvnqetpalpQPALEYvidgdrEYRQL 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 578 HRQVAAVGQepqvfgRSLQENIAyglTQKPTMEEITAAAVKSGAHSFISGLpqGYDTE-VGEAGSQLSGGQRQAVALARA 656
Cdd:PRK10636   95 EAQLHDANE------RNDGHAIA---TIHGKLDAIDAWTIRSRAASLLHGL--GFSNEqLERPVSDFSGGWRMRLNLAQA 163
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2468698279 657 LIRKPCVLILDDATSALDANSQLQVEQLLyespELYSRSVLLITQHLSLVEQ-ADHILFLEGGTIRE 722
Cdd:PRK10636  164 LICRSDLLLLDEPTNHLDLDAVIWLEKWL----KSYQGTLILISHDRDFLDPiVDKIIHIEQQSLFE 226
ABC_6TM_exporter_like cd18540
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
203-478 1.99e-08

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


Pssm-ID: 349984 [Multi-domain]  Cd Length: 295  Bit Score: 56.33  E-value: 1.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 203 AIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFV---GDGIYNNTMGH-----VHSHLQgevfgavlRQETE 274
Cdd:cd18540    20 VFPLLTKYAIDHFITPGTLDGLTGFILLYLGLILIQALSVFLfirLAGKIEMGVSYdlrkkAFEHLQ--------TLSFS 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 275 FFQQNQTGNITSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLlpkkVGKWYQ--LL 352
Cdd:cd18540    92 YFDKTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVPVLAV----VSIYFQkkIL 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 353 EVQvRESLAKSSQV--AI-EALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYI 429
Cdd:cd18540   168 KAY-RKVRKINSRItgAFnEGITGAKTTKTLVREEKNLREFKELTEEMRRASVRAARLSALFLPIVLFLGSIATALVLWY 246
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 2468698279 430 GGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18540   247 GGILVLAGAITIGTLVAFISYATQFFEPIQQLARVLAELQSAQASAERV 295
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
525-730 2.21e-08

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 57.32  E-value: 2.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 525 TFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPL-PQYEHRYLHRQVAAVGQEPQ----VFGRSLQENI 599
Cdd:PRK10762  272 SFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVvTRSPQDGLANGIVYISEDRKrdglVLGMSVKENM 351
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 600 AygLTQKP----TMEEITAAAVKSGAHSFISGL----PqGYDTEVGEagsqLSGGQRQAVALARALIRKPCVLILDDATS 671
Cdd:PRK10762  352 S--LTALRyfsrAGGSLKHADEQQAVSDFIRLFniktP-SMEQAIGL----LSGGNQQKVAIARGLMTRPKVLILDEPTR 424
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2468698279 672 ALDANSQLQVEQLL--YESPELysrSVLLITQHLSLV-EQADHILFLEGGTI-----REGGTHQQLM 730
Cdd:PRK10762  425 GVDVGAKKEIYQLInqFKAEGL---SIILVSSEMPEVlGMSDRILVMHEGRIsgeftREQATQEKLM 488
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
521-729 5.37e-08

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 54.55  E-value: 5.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 521 LQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGK--------PLPQYEHRYLHR-------QVAAVG 585
Cdd:PRK11701   22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrdlyALSEAERRRLLRtewgfvhQHPRDG 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 586 QEPQVfgrSLQENIA----------YGltqkptmeEITAAAVKSGAH-----SFISGLPqgydtevgeagSQLSGGQRQA 650
Cdd:PRK11701  102 LRMQV---SAGGNIGerlmavgarhYG--------DIRATAGDWLERveidaARIDDLP-----------TTFSGGMQQR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 651 VALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQ-ADHILFLEGGTIREGG-THQQ 728
Cdd:PRK11701  160 LQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLlAHRLLVMKQGRVVESGlTDQV 239

                  .
gi 2468698279 729 L 729
Cdd:PRK11701  240 L 240
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
527-683 5.63e-08

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


Pssm-ID: 224166 [Multi-domain]  Cd Length: 591  Bit Score: 56.15  E-value: 5.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 527 TLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQlllDGKPLPQYEHRYLhrqvaavgqEPQVFGrslqeniaygltqk 606
Cdd:COG1245   363 EIYDGEVIGILGPNGIGKTTFVKLLAGVIKPDEGS---EEDLKVSYKPQYI---------SPDYDG-------------- 416
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 607 pTMEEITAAAVKSGAHS--FIS------GLPQGYDTEVGEagsqLSGGQRQAVALARALIRKPCVLILDDATSALDansq 678
Cdd:COG1245   417 -TVEDLLRSAIRSAFGSsyFKTeivkplNLEDLLERPVDE----LSGGELQRVAIAAALSREADLYLLDEPSAYLD---- 487

                  ....*
gi 2468698279 679 lqVEQ 683
Cdd:COG1245   488 --VEQ 490
PRK15093 PRK15093
peptide ABC transporter ATP-binding protein SapD;
508-730 5.64e-08

peptide ABC transporter ATP-binding protein SapD;


Pssm-ID: 185049 [Multi-domain]  Cd Length: 330  Bit Score: 55.19  E-value: 5.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 508 VSFAYPNRPdVLVLQGLTFTLRPGEVTALVGPNGSGKSTVA----ALLQNLYQPTEGQLLLDGKPL----PQYEHRYLHR 579
Cdd:PRK15093   11 IEFKTSDGW-VKAVDRVSMTLTEGEIRGLVGESGSGKSLIAkaicGVTKDNWRVTADRMRFDDIDLlrlsPRERRKLVGH 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 580 QVAAVGQEPQV-------FGRSLQENIA-----------YGLTQKPTMEEITAAAVKSgaHSFIsglpqgydteVGEAGS 641
Cdd:PRK15093   90 NVSMIFQEPQScldpserVGRQLMQNIPgwtykgrwwqrFGWRKRRAIELLHRVGIKD--HKDA----------MRSFPY 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 642 QLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPELYSRSVLLITQHLSLVEQ-ADHILFLEGGTI 720
Cdd:PRK15093  158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQwADKINVLYCGQT 237
                         250
                  ....*....|
gi 2468698279 721 REGGTHQQLM 730
Cdd:PRK15093  238 VETAPSKELV 247
ABC_6TM_PrtD_LapB_HlyB_like cd18782
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ...
202-478 5.75e-08

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: 54.91  E-value: 5.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 202 MAIPFFTGRLTDWILQDGSADTFTRNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQNQT 281
Cdd:cd18782    19 LANPLLFQVIIDKVLVQQDLATLYVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGTIIDHLLRLPLGFFDKRPV 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 282 GNITSRVTEdTSTLSDSLSEN-LSLFLwYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEVQVRESL 360
Cdd:cd18782    99 GELSTRISE-LDTIRGFLTGTaLTTLL-DVLFSVIYIAVLFSYSPLLTLVVLATVPLQLLLTFLFGPILRRQIRRRAEAS 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 361 AKSSQVAIEALSAMPTVRSFANEEgeaqKFREKLQEikTLNQ------KEAVAYAVNSWTTSISGMLLKVGILYIGGQLV 434
Cdd:cd18782   177 AKTQSYLVESLTGIQTVKAQNAEL----KARWRWQN--RYARslgegfKLTVLGTTSGSLSQFLNKLSSLLVLWVGAYLV 250
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 2468698279 435 TSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18782   251 LRGELTLGQLIAFRILSGYVTGPILRLSTLWQQFQELRVSLERL 294
PRK13543 PRK13543
heme ABC exporter ATP-binding protein CcmA;
502-702 6.05e-08

heme ABC exporter ATP-binding protein CcmA;


Pssm-ID: 184129 [Multi-domain]  Cd Length: 214  Bit Score: 53.70  E-value: 6.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAypnRPDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRylhRQV 581
Cdd:PRK13543   11 LLAAHALAFS---RNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRS---RFM 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 582 AAVGQEPqvfgrSLQENIAygltqkpTMEEITAAAVKSGAHSfiSGLPQGYDTEVGEAG------SQLSGGQRQAVALAR 655
Cdd:PRK13543   85 AYLGHLP-----GLKADLS-------TLENLHFLCGLHGRRA--KQMPGSALAIVGLAGyedtlvRQLSAGQKKRLALAR 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2468698279 656 ALIRKPCVLILDDATSALDANSQLQVEQLLyeSPELYSRSVLLITQH 702
Cdd:PRK13543  151 LWLSPAPLWLLDEPYANLDLEGITLVNRMI--SAHLRGGGAALVTTH 195
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
521-677 7.92e-08

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 54.25  E-value: 7.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 521 LQGLTFTLRPGEVTALVGPNGSGKSTvaaLLQNLYQptegqlLLDGKPLPQYEHRYLHRQVAAVGQEPQVFGRS------ 594
Cdd:PRK09984   20 LHAVDLNIHHGEMVALLGPSGSGKST---LLRHLSG------LITGDKSAGSHIELLGRTVQREGRLARDIRKSrantgy 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 595 --LQENIAYGLTqkpTMEEITAAAVKSGAH-----SFISGLPQGYD----TEVGEAG------SQLSGGQRQAVALARAL 657
Cdd:PRK09984   91 ifQQFNLVNRLS---VLENVLIGALGSTPFwrtcfSWFTREQKQRAlqalTRVGMVHfahqrvSTLSGGQQQRVAIARAL 167
                         170       180
                  ....*....|....*....|
gi 2468698279 658 IRKPCVLILDDATSALDANS 677
Cdd:PRK09984  168 MQQAKVILADEPIASLDPES 187
ABC_6TM_CvaB_RaxB_like cd18567
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ...
202-458 1.02e-07

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: 54.00  E-value: 1.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 202 MAIPFFTGRLTDWILQDGSADtftrNLTLMSI----LTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQ 277
Cdd:cd18567    19 LASPLYLQLVIDEVIVSGDRD----LLTVLAIgfglLLLLQALLSALRSWLVLYLSTSLNLQWTSNLFRHLLRLPLSYFE 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 278 QNQTGNITSR---VTEDTSTLSDSLSENL--SLFlwylvrGLCLLGIMLWGSVSLTMVTLVTLPLLFllpkkVGKW--YQ 350
Cdd:cd18567    95 KRHLGDIVSRfgsLDEIQQTLTTGFVEALldGLM------AILTLVMMFLYSPKLALIVLAAVALYA-----LLRLalYP 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 351 LLEVQVRESL---AKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLqeIKTLNQKEAVAYaVNSWTTSISGMLL---KV 424
Cdd:cd18567   164 PLRRATEEQIvasAKEQSHFLETIRGIQTIKLFGREAEREARWLNLL--VDAINADIRLQR-LQILFSAANGLLFgleNI 240
                         250       260       270
                  ....*....|....*....|....*....|....
gi 2468698279 425 GILYIGGQLVTSGAVSSGNLVTFVLYQMQFTQAV 458
Cdd:cd18567   241 LVIYLGALLVLDGEFTVGMLFAFLAYKDQFSSRA 274
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
528-688 1.24e-07

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


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 55.50  E-value: 1.24e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279  528 LRPGEVTALVGPNGSGKST-VAALLQNLYQ---PTEGQLLLDGKPLPQYEHRY-----------LHRQVAAVGqEPQVFG 592
Cdd:TIGR00956   84 IKPGELTVVLGRPGSGCSTlLKTIASNTDGfhiGVEGVITYDGITPEEIKKHYrgdvvynaetdVHFPHLTVG-ETLDFA 162
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279  593 RSLQ--ENIAYGLTQKPTMEEITAAAVKsgahsfISGLPQGYDTEVG-EAGSQLSGGQRQAVALARALIRKPCVLILDDA 669
Cdd:TIGR00956  163 ARCKtpQNRPDGVSREEYAKHIADVYMA------TYGLSHTRNTKVGnDFVRGVSGGERKRVSIAEASLGGAKIQCWDNA 236
                          170
                   ....*....|....*....
gi 2468698279  670 TSALDANSQLQVEQLLYES 688
Cdd:TIGR00956  237 TRGLDSATALEFIRALKTS 255
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
502-731 1.42e-07

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


Pssm-ID: 131681 [Multi-domain]  Cd Length: 500  Bit Score: 54.83  E-value: 1.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYPNRPDVLVLQGLTFTLRPGEVTALVGPNGSGKS-TVAALLQNLYQPTEGQLLLDGKPL----PQY---- 572
Cdd:TIGR02633 257 ILEARNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTeLVQALFGAYPGKFEGNVFINGKPVdirnPAQaira 336
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 573 ------EHRYLHRQVAAVGQEPQVFGRSLQE-----NIAYGLTQKPTMEEITAAAVKSgAHSFisgLPQGydtevgeags 641
Cdd:TIGR02633 337 giamvpEDRKRHGIVPILGVGKNITLSVLKSfcfkmRIDAAAELQIIGSAIQRLKVKT-ASPF---LPIG---------- 402
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 642 QLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYespELYSRSVLLITQHLSLVEQ---ADHILF---- 714
Cdd:TIGR02633 403 RLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLIN---QLAQEGVAIIVVSSELAEVlglSDRVLVigeg 479
                         250
                  ....*....|....*...
gi 2468698279 715 -LEGGTIREGGTHQQLME 731
Cdd:TIGR02633 480 kLKGDFVNHALTQEQVLA 497
ycf16 CHL00131
sulfate ABC transporter protein; Validated
517-737 1.74e-07

sulfate ABC transporter protein; Validated


Pssm-ID: 214372 [Multi-domain]  Cd Length: 252  Bit Score: 53.11  E-value: 1.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 517 DVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQN--LYQPTEGQLLLDGKPLPQY--EHRYlHRQVAAVGQEP-QVF 591
Cdd:CHL00131   19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLepEERA-HLGIFLAFQYPiEIP 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 592 GRSLQE--NIAYGLTQK----PTMEEITAAAVKSGAHSFISGLPQGYDTEVGEAgsqLSGGQRQAVALARALIRKPCVLI 665
Cdd:CHL00131   98 GVSNADflRLAYNSKRKfqglPELDPLEFLEIINEKLKLVGMDPSFLSRNVNEG---FSGGEKKRNEILQMALLDSELAI 174
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2468698279 666 LDDATSALDANSQLQVEQ---LLYESpelySRSVLLITQHLSLVE--QADHILFLEGGTIREGGTHQ--QLMEKKGCYW 737
Cdd:CHL00131  175 LDETDSGLDIDALKIIAEginKLMTS----ENSIILITHYQRLLDyiKPDYVHVMQNGKIIKTGDAElaKELEKKGYDW 249
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
533-721 1.77e-07

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 53.72  E-value: 1.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 533 VTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHR-YL---HRQVAAVGQEPQVFGR-SLQENIAYGLtqKP 607
Cdd:PRK11144   26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGiCLppeKRRIGYVFQDARLFPHyKVRGNLRYGM--AK 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 608 TMEEITAAAVKS-GAHSFISGLPqgydtevgeagSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLy 686
Cdd:PRK11144  104 SMVAQFDKIVALlGIEPLLDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYL- 171
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2468698279 687 espELYSRSV----LLITQHL-SLVEQADHILFLEGGTIR 721
Cdd:PRK11144  172 ---ERLAREInipiLYVSHSLdEILRLADRVVVLEQGKVK 208
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
461-731 3.90e-07

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 53.39  E-value: 3.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 461 LLSIYPRVQKAVGssEKIFEyldrtprcppsglltplhleglvqFQDVSFAYPNRPDVLVLQGLTFTLRPGEVTALVGPN 540
Cdd:PRK13549  244 LTALYPREPHTIG--EVILE------------------------VRNLTAWDPVNPHIKRVDDVSFSLRRGEILGIAGLV 297
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 541 GSGKSTVAALLQNLYQ-PTEGQLLLDGKPL----PQY----------EHRYLHRQVA--AVGQE------PQVFGRSLqe 597
Cdd:PRK13549  298 GAGRTELVQCLFGAYPgRWEGEIFIDGKPVkirnPQQaiaqgiamvpEDRKRDGIVPvmGVGKNitlaalDRFTGGSR-- 375
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 598 nIAYGLTQKPTMEEITAAAVKSgAHSFisgLPQGydtevgeagsQLSGGQRQAVALARALIRKPCVLILDDATSALDANS 677
Cdd:PRK13549  376 -IDDAAELKTILESIQRLKVKT-ASPE---LAIA----------RLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGA 440
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2468698279 678 QLQVEQLLYespELYSR--SVLLITQHLSLV-EQADHILFLEGGTIR-----EGGTHQQLME 731
Cdd:PRK13549  441 KYEIYKLIN---QLVQQgvAIIVISSELPEVlGLSDRVLVMHEGKLKgdlinHNLTQEQVME 499
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
506-699 4.58e-07

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 53.42  E-value: 4.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 506 QDVSFAYPNRpdVLVlQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKplpqYEHRYLHRQVAAVG 585
Cdd:PRK11147  323 ENVNYQIDGK--QLV-KDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTK----LEVAYFDQHRAELD 395
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 586 QEpqvfgRSLQENIAYGltqkptMEEITAAAVKSGAHSFISGL---PQGYDTEVgeagSQLSGGQRQAVALARALIRKPC 662
Cdd:PRK11147  396 PE-----KTVMDNLAEG------KQEVMVNGRPRHVLGYLQDFlfhPKRAMTPV----KALSGGERNRLLLARLFLKPSN 460
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2468698279 663 VLILDDATSALDansqlqVE--QLLYESPELYSRSVLLI 699
Cdd:PRK11147  461 LLILDEPTNDLD------VEtlELLEELLDSYQGTVLLV 493
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
506-718 6.16e-07

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


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 53.19  E-value: 6.16e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279  506 QDVSFAYPNRPDVLV-LQGLTFTLRPGEVTALVGPNGSGKSTvaaLLQNLYQP------TEGQLLLDGKPLPQyehrylh 578
Cdd:TIGR00956  763 RNLTYEVKIKKEKRViLNNVDGWVKPGTLTALMGASGAGKTT---LLNVLAERvttgviTGGDRLVNGRPLDS------- 832
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279  579 rqvaavgqepqvfgrSLQENIAYGLTQKPTMEEIT-------AAAVKSGAHSFIS-------------GLPQGYDTEVGE 638
Cdd:TIGR00956  833 ---------------SFQRSIGYVQQQDLHLPTSTvreslrfSAYLRQPKSVSKSekmeyveevikllEMESYADAVVGV 897
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279  639 AGSQLSGGQRQAVALARALIRKPCVLI-LDDATSALDANSQLQVEQLLYESPElYSRSVLLITQHLS--LVEQADHILFL 715
Cdd:TIGR00956  898 PGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLAD-HGQAILCTIHQPSaiLFEEFDRLLLL 976

                   ...
gi 2468698279  716 EGG 718
Cdd:TIGR00956  977 QKG 979
ABC_6TM_T1SS_like cd18555
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ...
203-478 7.18e-07

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


Pssm-ID: 349999 [Multi-domain]  Cd Length: 294  Bit Score: 51.36  E-value: 7.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 203 AIPFFTGRLTDWILQDGsadtftrNLTLMSILTIASAVLeFVGDGIYNNTMG--------HVHSHLQGEVFGAVLRQETE 274
Cdd:cd18555    20 LIPILTQYVIDNVIVPG-------NLNLLNVLGIGILIL-FLLYGLFSFLRGyiiiklqtKLDKSLMSDFFEHLLKLPYS 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 275 FFQQNQTGNITSRVtEDTSTLSDSLSENLSL----FLWYLVrglcLLGIMLWGSVSLTMVTLVTLPLLFL----LPKKVg 346
Cdd:cd18555    92 FFENRSSGDLLFRA-NSNVYIRQILSNQVISliidLLLLVI----YLIYMLYYSPLLTLIVLLLGLLIVLllllTRKKI- 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 347 kwYQLLEVQVREsLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYA-VNSWTTSISgMLLKVG 425
Cdd:cd18555   166 --KKLNQEEIVA-QTKVQSYLTETLYGIETIKSLGSEKNIYKKWENLFKKQLKAFKKKERLSNiLNSISSSIQ-FIAPLL 241
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2468698279 426 ILYIGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18555   242 ILWIGAYLVINGELTLGELIAFSSLAGSFLTPIVSLINSYNQFILLKSYLERL 294
PLN03073 PLN03073
ABC transporter F family; Provisional
525-690 1.34e-06

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 51.78  E-value: 1.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 525 TFTLRPGEVTALVGPNGSGKSTvaaLLQNLYQ------PTEGQLL---------------------LDGKPLPQYEHRYL 577
Cdd:PLN03073  197 SVTLAFGRHYGLVGRNGTGKTT---FLRYMAMhaidgiPKNCQILhveqevvgddttalqcvlntdIERTQLLEEEAQLV 273
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 578 HRQvaAVGQEPQVFGRSLQENIAyGLTQKPT----------MEEITAAAVKSGAHSFISGLPQGYDTEVgEAGSQLSGGQ 647
Cdd:PLN03073  274 AQQ--RELEFETETGKGKGANKD-GVDKDAVsqrleeiykrLELIDAYTAEARAASILAGLSFTPEMQV-KATKTFSGGW 349
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2468698279 648 RQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPE 690
Cdd:PLN03073  350 RMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPK 392
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
503-735 2.08e-06

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 411426 [Multi-domain]  Cd Length: 907  Bit Score: 51.28  E-value: 2.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPnrpDVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYEHRylhrqvA 582
Cdd:NF033858    2 ARLEGVSHRYG---KTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHR------R 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 583 AVGQE----PQVFGR------SLQENIA-----YGLTQ---KPTMEEITAAavkSGAHSFISgLPQGydtevgeagsQLS 644
Cdd:NF033858   73 AVCPRiaymPQGLGKnlyptlSVFENLDffgrlFGQDAaerRRRIDELLRA---TGLAPFAD-RPAG----------KLS 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 645 GGQRQAVALARALIRKPCVLILDDATSALDANSQLQ----VEQLLYESPELysrSVLLITQHLSLVEQADHILFLEGGTI 720
Cdd:NF033858  139 GGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQfwelIDRIRAERPGM---SVLVATAYMEEAERFDWLVAMDAGRV 215
                         250
                  ....*....|....*
gi 2468698279 721 REGGTHQQLMEKKGC 735
Cdd:NF033858  216 LATGTPAELLARTGA 230
ABC_6TM_PrtD_LapB_HlyB_like cd18783
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ...
203-478 2.51e-06

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


Pssm-ID: 350056 [Multi-domain]  Cd Length: 294  Bit Score: 49.82  E-value: 2.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 203 AIPFFTGRLTDWILQDGSADTFTRnLTLMSILTIA-SAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQNQT 281
Cdd:cd18783    20 APPIFFQIVIDKVLVHQSYSTLYV-LTIGVVIALLfEGILGYLRRYLLLVATTRIDARLALRTFDRLLSLPIDFFERTPA 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 282 GNITSRVTEdTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGSVSLTMVTLVTLPLLFLLPKKVGKWYQLLEVQVRESLA 361
Cdd:cd18783    99 GVLTKHMQQ-IERIRQFLTGQLFGTLLDATSLLVFLPVLFFYSPTLALVVLAFSALIALIILAFLPPFRRRLQALYRAEG 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 362 KSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVayaVNSWTTSISG---MLLKVGILYIGGQLVTSGA 438
Cdd:cd18783   178 ERQAFLVETVHGIRTVKSLALEPRQRREWDERVARAIRARFAVGR---LSNWPQTLTGpleKLMTVGVIWVGAYLVFAGS 254
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 2468698279 439 VSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18783   255 LTVGALIAFNMLAGRVAGPLVQLAGLVQEYQEARLSVRML 294
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
521-687 3.29e-06

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 50.11  E-value: 3.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 521 LQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPLPQYE-HRYLHRQVAAVGQEPQVFG------- 592
Cdd:PRK10982  264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNaNEAINHGFALVTEERRSTGiyayldi 343
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 593 --RSLQENI-----AYGLTQKPTMEE-----ITAAAVKSGAHSfisglpqgydTEVGeagsQLSGGQRQAVALARALIRK 660
Cdd:PRK10982  344 gfNSLISNIrnyknKVGLLDNSRMKSdtqwvIDSMRVKTPGHR----------TQIG----SLSGGNQQKVIIGRWLLTQ 409
                         170       180
                  ....*....|....*....|....*..
gi 2468698279 661 PCVLILDDATSALDANSQLQVEQLLYE 687
Cdd:PRK10982  410 PEILMLDEPTRGIDVGAKFEIYQLIAE 436
PRK13546 PRK13546
teichoic acids export ABC transporter ATP-binding subunit TagH;
521-732 7.03e-06

teichoic acids export ABC transporter ATP-binding subunit TagH;


Pssm-ID: 184131 [Multi-domain]  Cd Length: 264  Bit Score: 48.27  E-value: 7.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 521 LQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLlldgkplpqyeHRYLHRQVAAV--GQEPQVFGrslQEN 598
Cdd:PRK13546   40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV-----------DRNGEVSVIAIsaGLSGQLTG---IEN 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 599 IAY-----GLTQKpTMEEITAAAVKSgahsfisglpqgydTEVGEAGSQ----LSGGQRQAVALARALIRKPCVLILDDA 669
Cdd:PRK13546  106 IEFkmlcmGFKRK-EIKAMTPKIIEF--------------SELGEFIYQpvkkYSSGMRAKLGFSINITVNPDILVIDEA 170
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2468698279 670 TSALDANSQLQVEQLLYESPElYSRSVLLITQHLSLVEQ-ADHILFLEGGTIREGGTHQQLMEK 732
Cdd:PRK13546  171 LSVGDQTFAQKCLDKIYEFKE-QNKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYGELDDVLPK 233
ABC_6TM_ABCC_D2 cd18580
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ...
202-481 7.21e-06

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: 48.27  E-value: 7.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 202 MAIPFFTGRLTDWILQ-------DGSADTFTRNLTLMSILTIASAVLEFVGDGIYNNTMG-----HVHSHLqgevFGAVL 269
Cdd:cd18580     8 LLLLAFLSQFSNIWLDwwssdwsSSPNSSSGYYLGVYAALLVLASVLLVLLRWLLFVLAGlrasrRLHDKL----LRSVL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 270 RQETEFFQQNQTGNITSRVTEDTSTLSDSLSENLSLFLWYLVRGLCLLGIMLWGS--VSLTMVTLVTLPLlfllpkKVGK 347
Cdd:cd18580    84 RAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSpyFLIVLPPLLVVYY------LLQR 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 348 WYQLLEVQVR--ESLAKS---SQVAiEALSAMPTVRSFANEEGEAQKFREKLQEiktlNQKeavAY----AVNSWTTSIS 418
Cdd:cd18580   158 YYLRTSRQLRrlESESRSplySHFS-ETLSGLSTIRAFGWQERFIEENLRLLDA----SQR---AFylllAVQRWLGLRL 229
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2468698279 419 GMLLKVGILYIGGQLVTSGAVSSGNLVTFVLYQ-MQFTQAVEVLLSIYPRVQKAVGSSEKIFEY 481
Cdd:cd18580   230 DLLGALLALVVALLAVLLRSSISAGLVGLALTYaLSLTGSLQWLVRQWTELETSMVSVERILEY 293
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
503-676 7.46e-06

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 49.35  E-value: 7.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 503 VQFQDVSFAYPNRpdvLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLdGKPLpqyehrylhrQVA 582
Cdd:PRK11819  325 IEAENLSKSFGDR---LLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV----------KLA 390
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 583 AVGQ-----EPQvfgRSLQENIAYGLtqkptmEEITAA--AVKS----GAHSFisglpQGYDTE--VGeagsQLSGGQRQ 649
Cdd:PRK11819  391 YVDQsrdalDPN---KTVWEEISGGL------DIIKVGnrEIPSrayvGRFNF-----KGGDQQkkVG----VLSGGERN 452
                         170       180
                  ....*....|....*....|....*..
gi 2468698279 650 AVALARALIRKPCVLILDDATSALDAN 676
Cdd:PRK11819  453 RLHLAKTLKQGGNVLLLDEPTNDLDVE 479
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
502-688 9.66e-06

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 48.86  E-value: 9.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 502 LVQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLqnlyqptegqllldgkplpqyehrylhrqv 581
Cdd:PRK10938  260 RIVLNNGVVSYNDRP---ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLI------------------------------ 306
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 582 aaVGQEPQ-------VFGR---------SLQENIAYgLTQKPTMEEITAAAVK----SGAHSFIsGLPQ----------- 630
Cdd:PRK10938  307 --TGDHPQgysndltLFGRrrgsgetiwDIKKHIGY-VSSSLHLDYRVSTSVRnvilSGFFDSI-GIYQavsdrqqklaq 382
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2468698279 631 ------GYDTEVGEAGSQ-LSGGQRQAVALARALIRKPCVLILDDATSALDA-NSQLQ---VEQLLYES 688
Cdd:PRK10938  383 qwldilGIDKRTADAPFHsLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPlNRQLVrrfVDVLISEG 451
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
525-716 1.00e-05

ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.


Pssm-ID: 213207 [Multi-domain]  Cd Length: 204  Bit Score: 47.22  E-value: 1.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 525 TFTLRPGeVTALVGPNGSGKSTV-AALLQNLY---QPTEGQLLLDGKPLPQYEHR---YLHRQVAA-----VGQEPQVFg 592
Cdd:cd03240    17 EIEFFSP-LTLIVGQNGAGKTTIiEALKYALTgelPPNSKGGAHDPKLIREGEVRaqvKLAFENANgkkytITRSLAIL- 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 593 rslqENIAY---GLTQKPTMEEITaaavksgahsfisglpqgydtevgeagsQLSGGQRQAV------ALARALIRKPCV 663
Cdd:cd03240    95 ----ENVIFchqGESNWPLLDMRG----------------------------RCSGGEKVLAsliirlALAETFGSNCGI 142
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2468698279 664 LILDDATSALDA-NSQLQVEQLLYESPELYSRSVLLITQHLSLVEQADHILFLE 716
Cdd:cd03240   143 LALDEPTTNLDEeNIEESLAEIIEERKSQKNFQLIVITHDEELVDAADHIYRVE 196
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
637-748 1.06e-05

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 48.19  E-value: 1.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 637 GEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLyESPELYSRSVLLITQHLSLVEQADHIL-FL 715
Cdd:NF000106  139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEV-RSMVRDGATVLLTTQYMEEAEQLAHELtVI 217
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2468698279 716 EGGTIREGGTHQQLMEKKGCYWAMVQaPADAPE 748
Cdd:NF000106  218 DRGRVIADGKVDELKTKVGGRTLQIR-PAHAAE 249
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
526-674 1.29e-05

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 411426 [Multi-domain]  Cd Length: 907  Bit Score: 48.58  E-value: 1.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 526 FTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGKPlpqyehrylhrqVAA--------VGQEPQVFgrSL-- 595
Cdd:NF033858  287 FRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQP------------VDAgdiatrrrVGYMSQAF--SLyg 352
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 596 ----QENIA-----YGLTqkptmEEITAAAVKSGAHSFisGLpqgydTEVGEA-GSQLSGGQRQAVALARALIRKPCVLI 665
Cdd:NF033858  353 eltvRQNLElharlFHLP-----AAEIAARVAEMLERF--DL-----ADVADAlPDSLPLGIRQRLSLAVAVIHKPELLI 420

                  ....*....
gi 2468698279 666 LDDATSALD 674
Cdd:NF033858  421 LDEPTSGVD 429
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
526-730 2.23e-05

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 47.70  E-value: 2.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 526 FTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQL--------LLDGKPLPQY-EHRYLHRQVAAVGQEPQVFGRSLQ 596
Cdd:PRK10938   24 LTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERqsqfshitRLSFEQLQKLvSDEWQRNNTDMLSPGEDDTGRTTA 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 597 ENIAYGLTQKPTMEEItaaavksgAHSF-ISGLpqgydteVGEAGSQLSGGQRQAVALARALIRKPCVLILDDATSALDA 675
Cdd:PRK10938  104 EIIQDEVKDPARCEQL--------AQQFgITAL-------LDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDV 168
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2468698279 676 NSQLQVEQLLYESPELYSRSVLLITQHLSLVEQADHILFLEGGTIREGGTHQQLM 730
Cdd:PRK10938  169 ASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEIL 223
ABC_6TM_NHLM_bacteriocin cd18569
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; ...
268-478 2.43e-05

Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; This group includes the six-transmembrane helical domain (6-TMD) of the ABC subunit of NHLM (Nitrile Hydratase Leader Microcin) bacteriocin system, which contains ABC transporter (permease/ATP-binding fused protein) with a peptidase domain. ABC-transporter proteins in this group are predicted to be a subunit of a bacteriocin processing and export system, and they 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: 350013 [Multi-domain]  Cd Length: 294  Bit Score: 46.70  E-value: 2.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 268 VLRQETEFFQQNQTGNITSRV-TEDT--STLSDSLSE---NLSLFLWYLVrglcllgIMLWGSVSLTMVTLVTLPLLFLL 341
Cdd:cd18569    85 VLRLPVEFFSQRYAGDIASRVqSNDRvaNLLSGQLATtvlNLVMAVFYAL-------LMLQYDVPLTLIGIAIALLNLLV 157
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 342 PKKVGKWYQLL-EVQVRESlAKSSQVAIEALSAMPTVRSFANEEGeaqkFREKL--QEIKTLNQKEAVAyAVNSWTTSIS 418
Cdd:cd18569   158 LRLVSRKRVDLnRRLLQDS-GKLTGTTMSGLQMIETLKASGAESD----FFSRWagYQAKVLNAQQELG-RTNQLLGALP 231
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2468698279 419 GMLLKVG---ILYIGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEKI 478
Cdd:cd18569   232 TLLSALTnaaILGLGGLLVMDGALTIGMLVAFQSLMASFLAPVNSLVGLGGTLQEMRGDMERL 294
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
517-685 2.96e-05

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 47.25  E-value: 2.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 517 DVLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLqnlyqpTEGQLLLDGKPlpQYEHRYLhrqVAAVGQEP------QV 590
Cdd:PRK11147   15 DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKIL------NGEVLLDDGRI--IYEQDLI---VARLQQDPprnvegTV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 591 F----------GRSLQE--NIAYGLTQKPT------MEEITAAAVKSGAHSFIS---------GLPQgyDTEVgeagSQL 643
Cdd:PRK11147   84 YdfvaegieeqAEYLKRyhDISHLVETDPSeknlneLAKLQEQLDHHNLWQLENrinevlaqlGLDP--DAAL----SSL 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2468698279 644 SGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLL 685
Cdd:PRK11147  158 SGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFL 199
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
527-699 3.31e-05

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 47.11  E-value: 3.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 527 TLRPGEVTALVGPNGSGKSTVAALLQ-----NL---------------YQPTEGQ----LLLDG--KPL--PQYehrylh 578
Cdd:PRK13409   95 IPKEGKVTGILGPNGIGKTTAVKILSgelipNLgdyeeepswdevlkrFRGTELQnyfkKLYNGeiKVVhkPQY------ 168
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 579 rqvaaVGQEPQVFgrslqeniaygltqKPTMEEITAAAVKSGAHSFIS---GLPQGYDTEVgeagSQLSGGQRQAVALAR 655
Cdd:PRK13409  169 -----VDLIPKVF--------------KGKVRELLKKVDERGKLDEVVerlGLENILDRDI----SELSGGELQRVAIAA 225
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2468698279 656 ALIRKPCVLILDDATSALDANSQLQVEQLLYESPElySRSVLLI 699
Cdd:PRK13409  226 ALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAE--GKYVLVV 267
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
637-725 6.76e-05

excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273184 [Multi-domain]  Cd Length: 925  Bit Score: 46.54  E-value: 6.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 637 GEAGSQLSGGQRQAVALARALIRK---PCVLILDDATSAL---DANSQLQVEQLLYESpelySRSVLLITQHLSLVEQAD 710
Cdd:TIGR00630 824 GQPATTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLhfdDIKKLLEVLQRLVDK----GNTVVVIEHNLDVIKTAD 899
                          90
                  ....*....|....*..
gi 2468698279 711 HILFL--EGGTirEGGT 725
Cdd:TIGR00630 900 YIIDLgpEGGD--GGGT 914
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
531-717 9.81e-05

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


Pssm-ID: 213189 [Multi-domain]  Cd Length: 177  Bit Score: 43.71  E-value: 9.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 531 GEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDGkPLPQYEHRYLhrqvaavgqepqvfgrslqeniaygltqkptme 610
Cdd:cd03222    25 GEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDG-ITPVYKPQYI--------------------------------- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 611 eitaaavksgahsfisglpqgydtevgeagsQLSGGQRQAVALARALIRKPCVLILDDATSALDANSQLQVEQLLYESPE 690
Cdd:cd03222    71 -------------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSE 119
                         170       180
                  ....*....|....*....|....*...
gi 2468698279 691 LYSRSVLLITQHLSLVEQ-ADHILFLEG 717
Cdd:cd03222   120 EGKKTALVVEHDLAVLDYlSDRIHVFEG 147
ABC_6TM_YOR1_D2_like cd18606
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ...
268-481 1.04e-04

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: 44.77  E-value: 1.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 268 VLRQETEFFQQNQTGNITSRVTEDTSTLSDSLSENLSLFLWYLVR-----GLCL---------LGIMLWGSVSLTMVtlv 333
Cdd:cd18606    78 VLRAPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYTLSSiigtfILIIiylpwfaiaLPPLLVLYYFIANY--- 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 334 tlpllfllpkkvgkwYQ--LLEVQVRESLAKSSQVA--IEALSAMPTVRSFaneeGEAQKFREKLQE-IKTLNQKEAVAY 408
Cdd:cd18606   155 ---------------YRasSRELKRLESILRSFVYAnfSESLSGLSTIRAY----GAQDRFIKKNEKlIDNMNRAYFLTI 215
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2468698279 409 AVNSW----TTSISGML-LKVGILYIGGQLVTSGAvSSGNLVTFVLyqmQFTQAVEVLLSIYPRVQKAVGSSEKIFEY 481
Cdd:cd18606   216 ANQRWlairLDLLGSLLvLIVALLCVTRRFSISPS-STGLVLSYVL---QITQVLSWLVRQFAEVENNMNSVERLLHY 289
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
490-688 1.78e-04

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 44.78  E-value: 1.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 490 PSGLLTPLhleglVQFQDVSFAYPNRpdvLVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQL-LLDGKP 568
Cdd:PRK10636  305 PESLPNPL-----LKMEKVSAGYGDR---IILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIK 376
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 569 L---PQYEHRYLHRQVAAVGQ----EPQVFGRSLQENIaygltqkptmeeitaaavksGAHSFisglpQGydTEVGEAGS 641
Cdd:PRK10636  377 LgyfAQHQLEFLRADESPLQHlarlAPQELEQKLRDYL--------------------GGFGF-----QG--DKVTEETR 429
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2468698279 642 QLSGGQRQAVALARALIRKPCVLILDDATSALDansqLQVEQLLYES 688
Cdd:PRK10636  430 RFSGGEKARLVLALIVWQRPNLLLLDEPTNHLD----LDMRQALTEA 472
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
587-724 2.57e-04

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 44.82  E-value: 2.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279  587 EPQVFGRSLQENIAYGLTQKPTMEEITAAAvksgaHSFI-SGLpqGYdTEVGEAGSQLSGGQRQAVALARALI---RKPC 662
Cdd:PRK00635  1651 EGKHFGQLLQTPIEEVAETFPFLKKIQKPL-----QALIdNGL--GY-LPLGQNLSSLSLSEKIAIKIAKFLYlppKHPT 1722
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2468698279  663 VLILDDATSALDANSQLQVEQLLYESPELySRSVLLITQHLSLVEQADHILFLEGGTIREGG 724
Cdd:PRK00635  1723 LFLLDEIATSLDNQQKSALLVQLRTLVSL-GHSVIYIDHDPALLKQADYLIEMGPGSGKTGG 1783
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
503-560 2.62e-04

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 44.11  E-value: 2.62e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2468698279 503 VQFQDVSFAYPNRPdvlVLQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEG 560
Cdd:PRK15064  320 LEVENLTKGFDNGP---LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSG 374
ABC_6TM_VMR1_D2_like cd18604
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ...
233-482 3.01e-04

Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.


Pssm-ID: 350048 [Multi-domain]  Cd Length: 297  Bit Score: 43.23  E-value: 3.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 233 ILTIASAVLEFVGDGIYnnTMG------HVHSHLQGEVFGAVLRqeteFFQQNQTGNITSRVTEDTSTLSDSLSENLSLF 306
Cdd:cd18604    51 LISLLSVLLGTLRYLLF--FFGslrasrKLHERLLHSVLRAPLR----WLDTTPVGRILNRFSKDIETIDSELADSLSSL 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 307 LWYLVRGLCLLG-------IMLWGSVSLTMVTLVtlpllfllpkkVGKWYqlLEVQ--VR--ESLAKS---SQVAiEALS 372
Cdd:cd18604   125 LESTLSLLVILIaivvvspAFLLPAVVLAALYVY-----------IGRLY--LRASreLKrlESVARSpilSHFG-ETLA 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 373 AMPTVRSFANEEgeaqKFREKLQE-IKTLNQKEAVAYAVNSW----TTSISGML-LKVGILyiggqLVTSGAVSSGnLVT 446
Cdd:cd18604   191 GLVTIRAFGAEE----RFIEEMLRrIDRYSRAFRYLWNLNRWlsvrIDLLGALFsFATAAL-----LVYGPGIDAG-LAG 260
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 2468698279 447 FVL-YQMQFTQAVEVLLSIYPRVQKAVGSSEKIFEYL 482
Cdd:cd18604   261 FSLsFALGFSSAILWLVRSYNELELDMNSVERIQEYL 297
UvrA COG0178
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
627-736 4.30e-04

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


Pssm-ID: 223256 [Multi-domain]  Cd Length: 935  Bit Score: 43.73  E-value: 4.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 627 GLpqGYDTeVGEAGSQLSGGQRQAVALARALIRK---PCVLILDDATSAL---DansqlqVEQLLYESPELYSR--SVLL 698
Cdd:COG0178   810 GL--GYIK-LGQPATTLSGGEAQRVKLAKELSKRstgKTLYILDEPTTGLhfdD------IKKLLEVLHRLVDKgnTVIV 880
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2468698279 699 ITQHLSLVEQADHILFL------EGGTIREGGTHQQLMEKKGCY 736
Cdd:COG0178   881 IEHNLDVIKTADWIIDLgpeggdGGGEIVASGTPEEVAKVKASY 924
ABC_6TM_ATM1_ABCB7 cd18582
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ...
263-465 4.31e-04

Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1/ABCB7 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.


Pssm-ID: 350026 [Multi-domain]  Cd Length: 292  Bit Score: 42.87  E-value: 4.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 263 EVFGAVLRQETEFFQQNQTGNITS---RVTEDTSTLSDSLSENL----------SLFLWYLVrGLCLLGIMLwGSVSL-- 327
Cdd:cd18582    76 RVFRHLHSLSLRFHLSRKTGALSRaieRGTRGIEFLLRFLLFNIlptilelllvCGILWYLY-GWSYALITL-VTVALyv 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 328 --TMvtlvtlpllfllpkKVGKWYQLLEVQVRESLAKSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEA 405
Cdd:cd18582   154 afTI--------------KVTEWRTKFRREMNEADNEANAKAVDSLLNYETVKYFNNEEYEAERYDKALAKYEKAAVKSQ 219
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2468698279 406 VAYAVNSWTTSI---SGMllkVGILYIGGQLVTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIY 465
Cdd:cd18582   220 TSLALLNIGQALiisLGL---TAIMLLAAQGVVAGTLTVGDFVLVNTYLLQLYQPLNFLGFVY 279
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
641-727 4.87e-04

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 43.60  E-value: 4.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 641 SQLSGGQRQAVALARALI-------RKPC-VLILDDATSALDANSQLQVEQLLYESPELySRSVLLITQHLSLVEQADHI 712
Cdd:COG0419   814 KTLSGGERFLASLALRLAlsdllqgRARLeLLFLDEPFGTLDEERLEKLAEILEELLSD-GRQIIIISHVEELKERADVR 892
                          90
                  ....*....|....*
gi 2468698279 713 LFLEggtiREGGTHQ 727
Cdd:COG0419   893 IRVK----KDGGRSR 903
AAA_29 pfam13555
P-loop containing region of AAA domain;
522-551 2.06e-03

P-loop containing region of AAA domain;


Pssm-ID: 433304 [Multi-domain]  Cd Length: 61  Bit Score: 36.81  E-value: 2.06e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2468698279 522 QGLTFTLRPGEVTALVGPNGSGKST----VAALL 551
Cdd:pfam13555  13 DGHTIPIDPRGNTLLTGPSGSGKSTlldaIQTLL 46
tagH PRK13545
teichoic acids export protein ATP-binding subunit; Provisional
521-566 2.87e-03

teichoic acids export protein ATP-binding subunit; Provisional


Pssm-ID: 184130 [Multi-domain]  Cd Length: 549  Bit Score: 41.03  E-value: 2.87e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2468698279 521 LQGLTFTLRPGEVTALVGPNGSGKSTVAALLQNLYQPTEGQLLLDG 566
Cdd:PRK13545   40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG 85
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
636-718 2.88e-03

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 41.35  E-value: 2.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279  636 VGEAGSQLSGGQRQAVALARALI---RKPCVLILDDATSALDANSqlqVEQLLY--ESPELYSRSVLLITQHLSLVEQAD 710
Cdd:PRK00635   803 LGRPLSSLSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLHTHD---IKALIYvlQSLTHQGHTVVIIEHNMHVVKVAD 879
                           90
                   ....*....|
gi 2468698279  711 HILFL--EGG 718
Cdd:PRK00635   880 YVLELgpEGG 889
AAA_23 pfam13476
AAA domain;
497-555 5.77e-03

AAA domain;


Pssm-ID: 433240 [Multi-domain]  Cd Length: 190  Bit Score: 38.63  E-value: 5.77e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 497 LHLEGLVQFQDVsfaypnrpdvlvlqglTFTLRPGeVTALVGPNGSGKST-VAALLQNLY 555
Cdd:pfam13476   1 LTIENFRSFRDQ----------------TIDFSKG-LTLITGPNGSGKTTiLDAIKLALY 43
ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 cd18560
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ...
205-472 7.26e-03

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: 39.13  E-value: 7.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 205 PFFTGRLTDWILQDGSADTFT--RNLTLMSILTIASAVLEFVGDGIYNNTMGHVHSHLQGEVFGAVLRQETEFFQQNQTG 282
Cdd:cd18560    16 PLFLGRAVNALTLAKVKDLESavTLILLYALLRFSSKLLKELRSLLYRRVQQNAYRELSLKTFAHLHSLSLDWHLSKKTG 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 283 NITSRVTEDTstlsDSLSENLSLFLWYLVRGL--CLLGIMLW---GSVSLTMVTLVTLPLLFLLPKKVGKWyqllEVQVR 357
Cdd:cd18560    96 EVVRIMDRGT----ESANTLLSYLVFYLVPTLleLIVVSVVFafhFGAWLALIVFLSVLLYGVFTIKVTEW----RTKFR 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 358 ESLAK----SSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEIKTLNQKEAVAYAVNSWTTSISGMLLKVGILYIGGQL 433
Cdd:cd18560   168 RAANKkdneAHDIAVDSLLNFETVKYFTNEKYEVDRYGEAVKEYQKSSVKVQASLSLLNVGQQLIIQLGLTLGLLLAGYR 247
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 2468698279 434 VTSGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAV 472
Cdd:cd18560   248 VVDGGLSVGDFVAVNTYIFQLFQPLNFLGTIYRMIIQSL 286
ABC_6TM_HMT1 cd18583
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents ...
362-477 8.86e-03

Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents the HMT1 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster. HMT1 is closely related to 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.


Pssm-ID: 350027 [Multi-domain]  Cd Length: 290  Bit Score: 38.66  E-value: 8.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2468698279 362 KSSQVAIEALSAMPTVRSFANEEGEAQKFREKLQEiktlnqKEAVAYAVNSWTTSISG---MLLKVGIL---YIGGQLVT 435
Cdd:cd18583   174 EERSILTESLLNWETVKYFNREPYEKERYREAVKN------YQKAERKYLFSLNLLNAvqsLILTLGLLagcFLAAYQVS 247
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2468698279 436 SGAVSSGNLVTFVLYQMQFTQAVEVLLSIYPRVQKAVGSSEK 477
Cdd:cd18583   248 QGQATVGDFVTLLTYWAQLSGPLNFFATLYRSIQSDLIDAER 289
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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