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Conserved domains on  [gi|8928549|sp|O75027|]
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RecName: Full=Iron-sulfur clusters transporter ABCB7, mitochondrial; AltName: Full=ATP-binding cassette sub-family B member 7, mitochondrial; AltName: Full=ATP-binding cassette transporter 7; Short=ABC transporter 7 protein; Flags: Precursor

Protein Classification

ABCB family ABC transporter ATP-binding protein/permease( domain architecture ID 11474391)

ABCB family ABC transporter ATP-binding protein/permease ontains both the ATPase catalytic subunit and transmembrane (TM) component of an ATP transporter complex responsible for coupling the energy of ATP hydrolysis to the import of one or more from a variety of substrates; such as mitochondrial iron-sulfur clusters transporter ATM1

CATH:  3.40.50.300|1.20.1560.10
EC:  7.-.-.-
Gene Ontology:  GO:0140359|GO:0042626|GO:0005524|GO:0016887
PubMed:  24638992|25750732
SCOP:  4003976
TCDB:  3.A.1.210

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
 125-711 0e+00

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


:

Pssm-ID: 444078 [Multi-domain]  Cd Length: 605  Bit Score: 883.39  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  125 LSYVWPKDRPDLRARVAISLGFLGGAKAMNIVVPFMFKYAVDslnqmsgnmlNLSDAPNTVATMATAVLIGYGVSRAGAA 204
Cdd:COG5265  23 LLLLLLPPYLRRRRRALAALLLLLLAAALALVVPPLLKDAID----------ALLSGAAALLVVPVGLLLAYGLLRLLSV 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  205 FFNEVRNAVFGKVAQNSIRRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGISFVLSALVFNLLPIMFEVMLVSGV 284
Cdd:COG5265  93 LFGELRDALFARVTQRAVRRLALEVFRHLHALSLRFHLERQTGGLSRDIERGTKGIEFLLRFLLFNILPTLLEIALVAGI 172

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  285 LYYKCGAQFALVTLGTLGTYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNERYEAQRYDGFLKTYE 364
Cdd:COG5265 173 LLVKYDWWFALITLVTVVLYIAFTVVVTEWRTKFRREMNEADSEANTRAVDSLLNYETVKYFGNEAREARRYDEALARYE 252

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  365 TASLKSTSTLAMLNFGQSAIFSVGLTAIMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDMNTL 444
Cdd:COG5265 253 RAAVKSQTSLALLNFGQALIIALGLTAMMLMAAQGVVAGTMTVGDFVLVNAYLIQLYIPLNFLGFVYREIRQALADMERM 332

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  445 FTLLKVDTQIKDKVMASPLQITPqtATVAFDNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEP 524
Cdd:COG5265 333 FDLLDQPPEVADAPDAPPLVVGG--GEVRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDV 410

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  525 QKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNLLYGNISASPEEVYAVAKLAGLHDAILRMPHGYDTQVGE 604
Cdd:COG5265 411 TSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGE 490

                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  605 RGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKV 684
Cdd:COG5265 491 RGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRI 570

                       570       580
                ....*....|....*....|....*..
gi 8928549  685 AERGTHHGLLANpHSIYSEMWHTQSSR 711
Cdd:COG5265 571 VERGTHAELLAQ-GGLYAQMWARQQEE 596
 
Name Accession Description Interval E-value
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
 125-711 0e+00

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


Pssm-ID: 444078 [Multi-domain]  Cd Length: 605  Bit Score: 883.39  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  125 LSYVWPKDRPDLRARVAISLGFLGGAKAMNIVVPFMFKYAVDslnqmsgnmlNLSDAPNTVATMATAVLIGYGVSRAGAA 204
Cdd:COG5265  23 LLLLLLPPYLRRRRRALAALLLLLLAAALALVVPPLLKDAID----------ALLSGAAALLVVPVGLLLAYGLLRLLSV 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  205 FFNEVRNAVFGKVAQNSIRRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGISFVLSALVFNLLPIMFEVMLVSGV 284
Cdd:COG5265  93 LFGELRDALFARVTQRAVRRLALEVFRHLHALSLRFHLERQTGGLSRDIERGTKGIEFLLRFLLFNILPTLLEIALVAGI 172

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  285 LYYKCGAQFALVTLGTLGTYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNERYEAQRYDGFLKTYE 364
Cdd:COG5265 173 LLVKYDWWFALITLVTVVLYIAFTVVVTEWRTKFRREMNEADSEANTRAVDSLLNYETVKYFGNEAREARRYDEALARYE 252

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  365 TASLKSTSTLAMLNFGQSAIFSVGLTAIMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDMNTL 444
Cdd:COG5265 253 RAAVKSQTSLALLNFGQALIIALGLTAMMLMAAQGVVAGTMTVGDFVLVNAYLIQLYIPLNFLGFVYREIRQALADMERM 332

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  445 FTLLKVDTQIKDKVMASPLQITPqtATVAFDNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEP 524
Cdd:COG5265 333 FDLLDQPPEVADAPDAPPLVVGG--GEVRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDV 410

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  525 QKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNLLYGNISASPEEVYAVAKLAGLHDAILRMPHGYDTQVGE 604
Cdd:COG5265 411 TSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGE 490

                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  605 RGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKV 684
Cdd:COG5265 491 RGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRI 570

                       570       580
                ....*....|....*....|....*..
gi 8928549  685 AERGTHHGLLANpHSIYSEMWHTQSSR 711
Cdd:COG5265 571 VERGTHAELLAQ-GGLYAQMWARQQEE 596
ABC_6TM_ATM1_ABCB7 cd18582
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ...
 143-444 2.87e-167

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: 483.15  E-value: 2.87e-167
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  143 SLGFLGGAKAMNIVVPFMFKYAVDSLnqmsgnmlnlSDAPNTVATMATAVLIGYGVSRAGAAFFNEVRNAVFGKVAQNSI 222
Cdd:cd18582   1 ALLLLVLAKLLNVAVPFLLKYAVDAL----------SAPASALLAVPLLLLLAYGLARILSSLFNELRDALFARVSQRAV 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  223 RRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGISFVLSALVFNLLPIMFEVMLVSGVLYYKCGAQFALVTLGTLG 302
Cdd:cd18582  71 RRLALRVFRHLHSLSLRFHLSRKTGALSRAIERGTRGIEFLLRFLLFNILPTILELLLVCGILWYLYGWSYALITLVTVA 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  303 TYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNERYEAQRYDGFLKTYETASLKSTSTLAMLNFGQS 382
Cdd:cd18582 151 LYVAFTIKVTEWRTKFRREMNEADNEANAKAVDSLLNYETVKYFNNEEYEAERYDKALAKYEKAAVKSQTSLALLNIGQA 230

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 8928549  383 AIFSVGLTAIMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDMNTL 444
Cdd:cd18582 231 LIISLGLTAIMLLAAQGVVAGTLTVGDFVLVNTYLLQLYQPLNFLGFVYREIRQSLIDMEKL 292
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
 128-695 6.41e-102

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: 324.75  E-value: 6.41e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    128 VWPKDRPDLRARVAISLGFLGGAKAMNIVVPFMfKYAVDSLnqmsgnmLNLSDaPNTVATMAtAVLIGYGVSRAGAAFFN 207
Cdd:TIGR02203   5 LWSYVRPYKAGLVLAGVAMILVAATESTLAALL-KPLLDDG-------FGGRD-RSVLWWVP-LVVIGLAVLRGICSFVS 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    208 evrNAVFGKVAQNSIRRIAKNVFLHLHNLDLGFHLSRQTGALskaIDRGTRGISFVLSALVFNLLPIMFEVMLVSGVLYY 287
Cdd:TIGR02203  75 ---TYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTL---LSRITFDSEQVASAATDAFIVLVRETLTVIGLFIV 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    288 KCGAQFALvTLGTLGTYTAFTVAVTRWRTRFR---IEMNKADNDAGNAAIDSLLNYETVKYFNNERYEAQRYDGFLKTYE 364
Cdd:TIGR02203 149 LLYYSWQL-TLIVVVMLPVLSILMRRVSKRLRrisKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNR 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    365 TASLKSTSTLAMLNFGQSAIFSVGLTAIMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDMNTL 444
Cdd:TIGR02203 228 RLAMKMTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESL 307

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    445 FTLLkvDTQikDKVMASPLQITPQTATVAFDNVHFEYI-EGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYE 523
Cdd:TIGR02203 308 FTLL--DSP--PEKDTGTRAIERARGDVEFRNVTFRYPgRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYE 383

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    524 PQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNLLYGNIS-ASPEEVYAVAKLAGLHDAILRMPHGYDTQV 602
Cdd:TIGR02203 384 PDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTEqADRAEIERALAAAYAQDFVDKLPLGLDTPI 463

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    603 GERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQG 682
Cdd:TIGR02203 464 GENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDG 543

                         570
                  ....*....|...
gi 8928549    683 KVAERGTHHGLLA 695
Cdd:TIGR02203 544 RIVERGTHNELLA 556
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
223-695 6.19e-95

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 306.89  E-value: 6.19e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   223 RRIA--KNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGISFV--------LSALV--FNLLPIMFEVmlvsgvlyykcG 290
Cdd:PRK13657  87 RRLAvlTEYFERIIQLPLAWHSQRGSGRALHTLLRGTDALFGLwlefmrehLATLValVVLLPLALFM-----------N 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   291 AQFALVTLGTLGTYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNERYEAQRYDGFLKTYETASLKS 370
Cdd:PRK13657 156 WRLSLVLVVLGIVYTLITTLVMRKTKDGQAAVEEHYHDLFAHVSDAIGNVSVVQSYNRIEAETQALRDIADNLLAAQMPV 235

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   371 TSTLAMLNFGQSAIFSVGLTAIMVLASQGIVAGTLTVGDLVMVNG---LLFQ-LSLPLNFLGTVYRETRQalidMNTLFT 446
Cdd:PRK13657 236 LSWWALASVLNRAASTITMLAILVLGAALVQKGQLRVGEVVAFVGfatLLIGrLDQVVAFINQVFMAAPK----LEEFFE 311

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   447 LLKVDTQIKDKVMASPLQITpqTATVAFDNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQK 526
Cdd:PRK13657 312 VEDAVPDVRDPPGAIDLGRV--KGAVEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQS 389

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   527 GSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNLLYGNISASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERG 606
Cdd:PRK13657 390 GRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERG 469

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   607 LKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAE 686
Cdd:PRK13657 470 RQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVE 549


                 ....*....
gi 8928549   687 RGTHHGLLA 695
Cdd:PRK13657 550 SGSFDELVA 558
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 488-637 3.66e-42

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


Pssm-ID: 394964 [Multi-domain]  Cd Length: 150  Bit Score: 150.11  E-value: 3.66e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    488 LSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLF-HNTIYYNL 566
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 8928549    567 LYGnisASPEEVYAVAKLAGLHDAI--LRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATS 637
Cdd:pfam00005  81 RLG---LLLKGLSKREKDARAEEALekLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
483-679 6.34e-14

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 70.73  E-value: 6.34e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   483 EGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGqniqdvsleslRRAVGVVPQdavlfhnti 562
Cdd:NF040873   3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQ--------- 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   563 yynllygnISASPEEVYA-VAKLAGL----HDAILRMPHGYDTQVGERGLK--------------LSGGEKQRVAIARAI 623
Cdd:NF040873  63 --------RSEVPDSLPLtVRDLVAMgrwaRRGLWRRLTRDDRAAVDDALErvgladlagrqlgeLSGGQRQRALLAQGL 134

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 8928549   624 LKDPPVILYDEATSSLDSITEETILGAMKDVV-KHRTSIFIAHRLSTVVDADEIIVL 679
Cdd:NF040873 135 AQEADLLLLDEPTTGLDAESRERIIALLAEEHaRGATVVVVTHDLELVRRADPCVLL 191
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 498-680 8.44e-11

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 60.85  E-value: 8.44e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549     498 GKKVAIVGGSGSGKSTIVRLLFRFYEPQKGS-IYLAGQNIQDVSLESLRravgvvpqdavlfhntiyynllygnisaspe 576
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPGGGvIYIDGEDILEEVLDQLL------------------------------- 50

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549     577 evyavaklaglhdailrmphgyDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVK 656
Cdd:smart00382  51 ----------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLL 108

                          170       180       190
                   ....*....|....*....|....*....|.
gi 8928549     657 HRTS-------IFIAHRLSTVVDADEIIVLD 680
Cdd:smart00382 109 LLLKseknltvILTTNDEKDLGPALLRRRFD 139
GguA NF040905
sugar ABC transporter ATP-binding protein;
484-686 4.46e-09

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 59.42  E-value: 4.46e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   484 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLL-----FRFYEpqkGSIYLAGQ-----NIQDvsleSLRRAVGVVPQ 553
Cdd:NF040905  13 GVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLsgvypHGSYE---GEILFDGEvcrfkDIRD----SEALGIVIIHQ 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   554 D-AVLFHNTIYYNLLYGNISASP-----EEVYAVAK--LA--GLHDAilrmPhgyDTQVGERGLklsgGEKQRVAIARAI 623
Cdd:NF040905  86 ElALIPYLSIAENIFLGNERAKRgvidwNETNRRARelLAkvGLDES----P---DTLVTDIGV----GKQQLVEIAKAL 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 8928549   624 LKDPPVILYDEATSSL---DSiteETILGAMKDVVKHR-TSIFIAHRLSTVVD-ADEIIVLDQGKVAE 686
Cdd:NF040905 155 SKDVKLLILDEPTAALneeDS---AALLDLLLELKAQGiTSIIISHKLNEIRRvADSITVLRDGRTIE 219
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
603-688 4.29e-04

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 43.19  E-value: 4.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   603 GERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVD--ADEIIVLD 680
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEqlAHELTVID 218


                 ....*...
gi 8928549   681 QGKVAERG 688
Cdd:NF000106 219 RGRVIADG 226
 
Name Accession Description Interval E-value
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
 125-711 0e+00

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


Pssm-ID: 444078 [Multi-domain]  Cd Length: 605  Bit Score: 883.39  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  125 LSYVWPKDRPDLRARVAISLGFLGGAKAMNIVVPFMFKYAVDslnqmsgnmlNLSDAPNTVATMATAVLIGYGVSRAGAA 204
Cdd:COG5265  23 LLLLLLPPYLRRRRRALAALLLLLLAAALALVVPPLLKDAID----------ALLSGAAALLVVPVGLLLAYGLLRLLSV 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  205 FFNEVRNAVFGKVAQNSIRRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGISFVLSALVFNLLPIMFEVMLVSGV 284
Cdd:COG5265  93 LFGELRDALFARVTQRAVRRLALEVFRHLHALSLRFHLERQTGGLSRDIERGTKGIEFLLRFLLFNILPTLLEIALVAGI 172

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  285 LYYKCGAQFALVTLGTLGTYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNERYEAQRYDGFLKTYE 364
Cdd:COG5265 173 LLVKYDWWFALITLVTVVLYIAFTVVVTEWRTKFRREMNEADSEANTRAVDSLLNYETVKYFGNEAREARRYDEALARYE 252

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  365 TASLKSTSTLAMLNFGQSAIFSVGLTAIMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDMNTL 444
Cdd:COG5265 253 RAAVKSQTSLALLNFGQALIIALGLTAMMLMAAQGVVAGTMTVGDFVLVNAYLIQLYIPLNFLGFVYREIRQALADMERM 332

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  445 FTLLKVDTQIKDKVMASPLQITPqtATVAFDNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEP 524
Cdd:COG5265 333 FDLLDQPPEVADAPDAPPLVVGG--GEVRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDV 410

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  525 QKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNLLYGNISASPEEVYAVAKLAGLHDAILRMPHGYDTQVGE 604
Cdd:COG5265 411 TSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGE 490

                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  605 RGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKV 684
Cdd:COG5265 491 RGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRI 570

                       570       580
                ....*....|....*....|....*..
gi 8928549  685 AERGTHHGLLANpHSIYSEMWHTQSSR 711
Cdd:COG5265 571 VERGTHAELLAQ-GGLYAQMWARQQEE 596
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
116-710 1.56e-180

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 528.20  E-value: 1.56e-180
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  116 DTRKIIKAMLSYVWPkdrpdLRARVAISLGFLGGAKAMNIVVPFMFKYAVDSLnqmsgnmlnLSDAPNTVATMATAVLIG 195
Cdd:COG1132   4 SPRKLLRRLLRYLRP-----YRGLLILALLLLLLSALLELLLPLLLGRIIDAL---------LAGGDLSALLLLLLLLLG 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  196 YGVSRAGAAFFnevRNAVFGKVAQNSIRRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGISFVLSALVFNLLPIM 275
Cdd:COG1132  70 LALLRALLSYL---QRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSV 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  276 FEVMLVSGVLYYKcGAQFALVTLGTLGTYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNERYEAQR 355
Cdd:COG1132 147 VTLIGALVVLFVI-DWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELER 225

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  356 YDGFLKTYETASLKSTSTLAMLNFGQSAIFSVGLTAIMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRETR 435
Cdd:COG1132 226 FREANEELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQ 305

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  436 QALIDMNTLFTLLKVDTQIKDKvmASPLQITPQTATVAFDNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIV 515
Cdd:COG1132 306 RALASAERIFELLDEPPEIPDP--PGAVPLPPVRGEIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLV 383

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  516 RLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNLLYGNISASPEEVYAVAKLAGLHDAILRMP 595
Cdd:COG1132 384 NLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALP 463

                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  596 HGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADE 675
Cdd:COG1132 464 DGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADR 543

                       570       580       590
                ....*....|....*....|....*....|....*
gi 8928549  676 IIVLDQGKVAERGTHHGLLANpHSIYSEMWHTQSS 710
Cdd:COG1132 544 ILVLDDGRIVEQGTHEELLAR-GGLYARLYRLQFG 577
ABC_6TM_ATM1_ABCB7 cd18582
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ...
 143-444 2.87e-167

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: 483.15  E-value: 2.87e-167
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  143 SLGFLGGAKAMNIVVPFMFKYAVDSLnqmsgnmlnlSDAPNTVATMATAVLIGYGVSRAGAAFFNEVRNAVFGKVAQNSI 222
Cdd:cd18582   1 ALLLLVLAKLLNVAVPFLLKYAVDAL----------SAPASALLAVPLLLLLAYGLARILSSLFNELRDALFARVSQRAV 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  223 RRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGISFVLSALVFNLLPIMFEVMLVSGVLYYKCGAQFALVTLGTLG 302
Cdd:cd18582  71 RRLALRVFRHLHSLSLRFHLSRKTGALSRAIERGTRGIEFLLRFLLFNILPTILELLLVCGILWYLYGWSYALITLVTVA 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  303 TYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNERYEAQRYDGFLKTYETASLKSTSTLAMLNFGQS 382
Cdd:cd18582 151 LYVAFTIKVTEWRTKFRREMNEADNEANAKAVDSLLNYETVKYFNNEEYEAERYDKALAKYEKAAVKSQTSLALLNIGQA 230

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 8928549  383 AIFSVGLTAIMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDMNTL 444
Cdd:cd18582 231 LIISLGLTAIMLLAAQGVVAGTLTVGDFVLVNTYLLQLYQPLNFLGFVYREIRQSLIDMEKL 292
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
 472-708 1.37e-143

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: 420.48  E-value: 1.37e-143
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  472 VAFDNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVV 551
Cdd:cd03253   1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  552 PQDAVLFHNTIYYNLLYGNISASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVIL 631
Cdd:cd03253  81 PQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILL 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 8928549  632 YDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLLAnPHSIYSEMWHTQ 708
Cdd:cd03253 161 LDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLA-KGGLYAEMWKAQ 236
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
 71-708 3.37e-140

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


Pssm-ID: 441875 [Multi-domain]  Cd Length: 711  Bit Score: 428.87  E-value: 3.37e-140
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   71 KGNSGQFLDAAKALQVWPLIEKRTCWHGHAgggLHTDPKEGLKDVDTRKI-IKAMLSYVWPkDRPDLRArvAISLGFLGG 149
Cdd:COG2274  96 DGDKVTIADPATGRRKLSLEEFAESWTGVA---LLLEPTPEFDKRGEKPFgLRWFLRLLRR-YRRLLLQ--VLLASLLIN 169

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  150 AkaMNIVVPFMFKYAVDSLnqMSGNMLNlsdapnTVATMATAVLIGYGVSragaAFFNEVRNAVFGKVAQNSIRRIAKNV 229
Cdd:COG2274 170 L--LALATPLFTQVVIDRV--LPNQDLS------TLWVLAIGLLLALLFE----GLLRLLRSYLLLRLGQRIDLRLSSRF 235

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  230 FLHLHNLDLGFHLSRQTGALSKAIdRGTRGI-SFVLSALVFNLLPIMFevMLVSGVL--YYkcGAQFALVTLGTLGTYTA 306
Cdd:COG2274 236 FRHLLRLPLSFFESRSVGDLASRF-RDVESIrEFLTGSLLTALLDLLF--VLIFLIVlfFY--SPPLALVVLLLIPLYVL 310

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  307 FTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNERYEAQRYDGFLKTYETASLKSTSTLAMLNFGQSAIFS 386
Cdd:COG2274 311 LGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQ 390

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  387 VGLTAIMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDMNTLFTLLkvDTQIKDKVMASPLQIT 466
Cdd:COG2274 391 LATVALLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDIL--DLPPEREEGRSKLSLP 468

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  467 PQTATVAFDNVHFEYIE-GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLR 545
Cdd:COG2274 469 RLKGDIELENVSFRYPGdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLR 548

                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  546 RAVGVVPQDAVLFHNTIYYNLLYGNISASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILK 625
Cdd:COG2274 549 RQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLR 628

                       570       580       590       600       610       620       630       640
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  626 DPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLLANpHSIYSEMW 705
Cdd:COG2274 629 NPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLAR-KGLYAELV 707


                ...
gi 8928549  706 HTQ 708
Cdd:COG2274 708 QQQ 710
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
 128-695 6.41e-102

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: 324.75  E-value: 6.41e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    128 VWPKDRPDLRARVAISLGFLGGAKAMNIVVPFMfKYAVDSLnqmsgnmLNLSDaPNTVATMAtAVLIGYGVSRAGAAFFN 207
Cdd:TIGR02203   5 LWSYVRPYKAGLVLAGVAMILVAATESTLAALL-KPLLDDG-------FGGRD-RSVLWWVP-LVVIGLAVLRGICSFVS 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    208 evrNAVFGKVAQNSIRRIAKNVFLHLHNLDLGFHLSRQTGALskaIDRGTRGISFVLSALVFNLLPIMFEVMLVSGVLYY 287
Cdd:TIGR02203  75 ---TYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTL---LSRITFDSEQVASAATDAFIVLVRETLTVIGLFIV 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    288 KCGAQFALvTLGTLGTYTAFTVAVTRWRTRFR---IEMNKADNDAGNAAIDSLLNYETVKYFNNERYEAQRYDGFLKTYE 364
Cdd:TIGR02203 149 LLYYSWQL-TLIVVVMLPVLSILMRRVSKRLRrisKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNR 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    365 TASLKSTSTLAMLNFGQSAIFSVGLTAIMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDMNTL 444
Cdd:TIGR02203 228 RLAMKMTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESL 307

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    445 FTLLkvDTQikDKVMASPLQITPQTATVAFDNVHFEYI-EGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYE 523
Cdd:TIGR02203 308 FTLL--DSP--PEKDTGTRAIERARGDVEFRNVTFRYPgRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYE 383

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    524 PQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNLLYGNIS-ASPEEVYAVAKLAGLHDAILRMPHGYDTQV 602
Cdd:TIGR02203 384 PDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTEqADRAEIERALAAAYAQDFVDKLPLGLDTPI 463

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    603 GERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQG 682
Cdd:TIGR02203 464 GENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDG 543

                         570
                  ....*....|...
gi 8928549    683 KVAERGTHHGLLA 695
Cdd:TIGR02203 544 RIVERGTHNELLA 556
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
 472-705 9.34e-102

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: 312.24  E-value: 9.34e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  472 VAFDNVHFEYI-EGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGV 550
Cdd:cd03251   1 VEFKNVTFRYPgDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  551 VPQDAVLFHNTIYYNLLYGNISASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVI 630
Cdd:cd03251  81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 8928549  631 LYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLLANpHSIYSEMW 705
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQ-GGVYAKLH 234
MsbA_rel TIGR02204
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ...
 125-695 9.60e-102

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: 324.73  E-value: 9.60e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    125 LSYVWPKDRPdLRARVAISLGFLGGAKAMNIVVPFMFKYAVD-SLNQMSGNMLNLSDAPNTVATMATAVLIG---YGVSR 200
Cdd:TIGR02204   6 LAALWPFVRP-YRGRVLAALVALLITAAATLSLPYAVRLMIDhGFSKDSSGLLNRYFAFLLVVALVLALGTAarfYLVTW 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    201 AGAAFFNEVRNAVFGkvaqnsirriaknvflHLHNLDLGFHLSRQTGALskaIDRGTRGISFVLSALVFNL-LPIMFEVM 279
Cdd:TIGR02204  85 LGERVVADIRRAVFA----------------HLISLSPSFFDKNRSGEV---VSRLTTDTTLLQSVIGSSLsMALRNALM 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    280 LVSGV-LYYKCGAQFALVTLGTLGTYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNERYEAQRYDG 358
Cdd:TIGR02204 146 CIGGLiMMFITSPKLTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGG 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    359 FLKTYETASLKSTSTLAMLNfgQSAIFSV--GLTAIMVLASQGIVAGTLTVGDL-------VMVNGLLFQLSlplnflgT 429
Cdd:TIGR02204 226 AVEKAYEAARQRIRTRALLT--AIVIVLVfgAIVGVLWVGAHDVIAGKMSAGTLgqfvfyaVMVAGSIGTLS-------E 296

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    430 VYRETRQALIDMNTLFTLLKVDTQIKdkVMASPLQI-TPQTATVAFDNVHFEYIE--GQKVLSGISFEVPAGKKVAIVGG 506
Cdd:TIGR02204 297 VWGELQRAAGAAERLIELLQAEPDIK--APAHPKTLpVPLRGEIEFEQVNFAYPArpDQPALDGLNLTVRPGETVALVGP 374

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    507 SGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNLLYGNISASPEEVYAVAKLAG 586
Cdd:TIGR02204 375 SGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAH 454

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    587 LHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHR 666
Cdd:TIGR02204 455 AHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHR 534

                         570       580
                  ....*....|....*....|....*....
gi 8928549    667 LSTVVDADEIIVLDQGKVAERGTHHGLLA 695
Cdd:TIGR02204 535 LATVLKADRIVVMDQGRIVAQGTHAELIA 563
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
 139-696 2.09e-100

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


Pssm-ID: 444012 [Multi-domain]  Cd Length: 563  Bit Score: 320.55  E-value: 2.09e-100
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  139 RVAISLGFLGGAkaMNIVVPFMFKYAVDSLnqMSGNmLNLSDAPNTVATMATAVLIgygvsRAGAAFFNEVRNAVFGKVA 218
Cdd:COG4988  20 ALAVLLGLLSGL--LIIAQAWLLASLLAGL--IIGG-APLSALLPLLGLLLAVLLL-----RALLAWLRERAAFRAAARV 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  219 QNSIRRiakNVFLHLHNLDLGFHLSRQTGALSKAIdrgTRGISfVLSALVFNLLPIMFEVMLVSGVLyykcgaqfaLVTL 298
Cdd:COG4988  90 KRRLRR---RLLEKLLALGPAWLRGKSTGELATLL---TEGVE-ALDGYFARYLPQLFLAALVPLLI---------LVAV 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  299 GTLGTYTAFTVAVT---------------------RWRTRFRIemnkadndaGNAAIDSLLNYETVKYFNNERYEAQRYD 357
Cdd:COG4988 154 FPLDWLSGLILLVTapliplfmilvgkgaakasrrQWRALARL---------SGHFLDRLRGLTTLKLFGRAKAEAERIA 224

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  358 GFLKTYETASLKstsTLAMlNFGQSA----IFSVGLTAIMVLASQGIVAGTLTVGDLVMVngLLfqLS----LPLNFLGT 429
Cdd:COG4988 225 EASEDFRKRTMK---VLRV-AFLSSAvlefFASLSIALVAVYIGFRLLGGSLTLFAALFV--LL--LApeffLPLRDLGS 296

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  430 VYRETRQALIDMNTLFTLLkvDTQIKDKVMASPLQITPQTATVAFDNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGS 509
Cdd:COG4988 297 FYHARANGIAAAEKIFALL--DAPEPAAPAGTAPLPAAGPPSIELEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGA 374

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  510 GKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNLLYGNISASPEEVYAVAKLAGLHD 589
Cdd:COG4988 375 GKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDE 454

                       490       500       510       520       530       540       550       560
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  590 AILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLST 669
Cdd:COG4988 455 FVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLAL 534

                       570       580
                ....*....|....*....|....*..
gi 8928549  670 VVDADEIIVLDQGKVAERGTHHGLLAN 696
Cdd:COG4988 535 LAQADRILVLDDGRIVEQGTHEELLAK 561
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
 470-695 1.09e-99

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


Pssm-ID: 213221 [Multi-domain]  Cd Length: 229  Bit Score: 306.84  E-value: 1.09e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  470 ATVAFDNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVG 549
Cdd:cd03254   1 GEIEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  550 VVPQDAVLFHNTIYYNLLYGNISASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPV 629
Cdd:cd03254  81 VVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKI 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 8928549  630 ILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLLA 695
Cdd:cd03254 161 LILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLA 226
ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 cd18560
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ...
 143-444 1.10e-98

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: 306.84  E-value: 1.10e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  143 SLGFLGGAKAMNIVVPFMFKYAVDSLnqmsgnmlnlSDAPNTVATMATAVLIGYGVSRAGAAFFNEVRNAVFGKVAQNSI 222
Cdd:cd18560   1 SLLLLILGKACNVLAPLFLGRAVNAL----------TLAKVKDLESAVTLILLYALLRFSSKLLKELRSLLYRRVQQNAY 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  223 RRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGISFVLSALVFNLLPIMFEVMLVSGVLYYKCGAQFALVTLGTLG 302
Cdd:cd18560  71 RELSLKTFAHLHSLSLDWHLSKKTGEVVRIMDRGTESANTLLSYLVFYLVPTLLELIVVSVVFAFHFGAWLALIVFLSVL 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  303 TYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNERYEAQRYDGFLKTYETASLKSTSTLAMLNFGQS 382
Cdd:cd18560 151 LYGVFTIKVTEWRTKFRRAANKKDNEAHDIAVDSLLNFETVKYFTNEKYEVDRYGEAVKEYQKSSVKVQASLSLLNVGQQ 230

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 8928549  383 AIFSVGLTAIMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDMNTL 444
Cdd:cd18560 231 LIIQLGLTLGLLLAGYRVVDGGLSVGDFVAVNTYIFQLFQPLNFLGTIYRMIIQSLTDMENL 292
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
 472-708 1.55e-98

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: 304.08  E-value: 1.55e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  472 VAFDNVHFEYIE--GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVG 549
Cdd:cd03249   1 IEFKNVSFRYPSrpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  550 VVPQDAVLFHNTIYYNLLYGNISASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPV 629
Cdd:cd03249  81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 8928549  630 ILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLLANpHSIYSEMWHTQ 708
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQ-KGVYAKLVKAQ 238
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
223-695 6.19e-95

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 306.89  E-value: 6.19e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   223 RRIA--KNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGISFV--------LSALV--FNLLPIMFEVmlvsgvlyykcG 290
Cdd:PRK13657  87 RRLAvlTEYFERIIQLPLAWHSQRGSGRALHTLLRGTDALFGLwlefmrehLATLValVVLLPLALFM-----------N 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   291 AQFALVTLGTLGTYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNERYEAQRYDGFLKTYETASLKS 370
Cdd:PRK13657 156 WRLSLVLVVLGIVYTLITTLVMRKTKDGQAAVEEHYHDLFAHVSDAIGNVSVVQSYNRIEAETQALRDIADNLLAAQMPV 235

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   371 TSTLAMLNFGQSAIFSVGLTAIMVLASQGIVAGTLTVGDLVMVNG---LLFQ-LSLPLNFLGTVYRETRQalidMNTLFT 446
Cdd:PRK13657 236 LSWWALASVLNRAASTITMLAILVLGAALVQKGQLRVGEVVAFVGfatLLIGrLDQVVAFINQVFMAAPK----LEEFFE 311

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   447 LLKVDTQIKDKVMASPLQITpqTATVAFDNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQK 526
Cdd:PRK13657 312 VEDAVPDVRDPPGAIDLGRV--KGAVEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQS 389

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   527 GSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNLLYGNISASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERG 606
Cdd:PRK13657 390 GRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERG 469

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   607 LKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAE 686
Cdd:PRK13657 470 RQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVE 549


                 ....*....
gi 8928549   687 RGTHHGLLA 695
Cdd:PRK13657 550 SGSFDELVA 558
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
 259-706 1.66e-91

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


Pssm-ID: 444011 [Multi-domain]  Cd Length: 569  Bit Score: 297.45  E-value: 1.66e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  259 GISFVLSALVFNLLPIMFEVMLVSGVLyykcgaqfalVTLGTLGTYTAFTVAVTRWRTRFRIemnkadndagnAAIDSLL 338
Cdd:COG4987 145 AAVAFLAFFSPALALVLALGLLLAGLL----------LPLLAARLGRRAGRRLAAARAALRA-----------RLTDLLQ 203

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  339 NYETVKYFNNERYEAQRYDGFLKTYETASLKSTSTLAMLNFGQSAIFSVGLTAIMVLASQGIVAGTLTVGDLVMVngLLF 418
Cdd:COG4987 204 GAAELAAYGALDRALARLDAAEARLAAAQRRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPLLALL--VLA 281

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  419 QLSL--PLNFLGTVYRETRQALIDMNTLFTLLKVDTQIKDKVMASPLqitPQTATVAFDNVHFEY-IEGQKVLSGISFEV 495
Cdd:COG4987 282 ALALfeALAPLPAAAQHLGRVRAAARRLNELLDAPPAVTEPAEPAPA---PGGPSLELEDVSFRYpGAGRPVLDGLSLTL 358

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  496 PAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNLLYGNISASP 575
Cdd:COG4987 359 PPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATD 438

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  576 EEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVV 655
Cdd:COG4987 439 EELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEAL 518

                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|.
gi 8928549  656 KHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLLANpHSIYSEMWH 706
Cdd:COG4987 519 AGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQ-NGRYRQLYQ 568
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
213-708 7.59e-87

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 285.37  E-value: 7.59e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   213 VFGKVAQNsIRRiakNVFLHLHNLDLGFHLSRQTGAL-------SKAIDRGTRG--ISFVL-SALVFNLLPIMFevmlvs 282
Cdd:PRK11176  92 VSGKVVMT-MRR---RLFGHMMGMPVSFFDKQSTGTLlsritydSEQVASSSSGalITVVReGASIIGLFIMMF------ 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   283 gvlYYKCgaQFALVtLGTLGTYTAFTVAVTRwrTRFRIEMNKADNDAG---NAAIDSLLNYETVKYFNNERYEAQRYDGF 359
Cdd:PRK11176 162 ---YYSW--QLSLI-LIVIAPIVSIAIRVVS--KRFRNISKNMQNTMGqvtTSAEQMLKGHKEVLIFGGQEVETKRFDKV 233

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   360 LKTYETASLKSTSTLAMLNFGQSAIFSVGLTAIMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALI 439
Cdd:PRK11176 234 SNRMRQQGMKMVSASSISDPIIQLIASLALAFVLYAASFPSVMDTLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMA 313

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   440 DMNTLFTLLKVDTQiKDKvmaSPLQITPQTATVAFDNVHFEYIEGQK-VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLL 518
Cdd:PRK11176 314 ACQTLFAILDLEQE-KDE---GKRVIERAKGDIEFRNVTFTYPGKEVpALRNINFKIPAGKTVALVGRSGSGKSTIANLL 389

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   519 FRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNLLYG-NISASPEEVYAVAKLAGLHDAILRMPHG 597
Cdd:PRK11176 390 TRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYArTEQYSREQIEEAARMAYAMDFINKMDNG 469

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   598 YDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEII 677
Cdd:PRK11176 470 LDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEIL 549

                        490       500       510
                 ....*....|....*....|....*....|.
gi 8928549   678 VLDQGKVAERGTHHGLLANpHSIYSEMWHTQ 708
Cdd:PRK11176 550 VVEDGEIVERGTHAELLAQ-NGVYAQLHKMQ 579
ABC_6TM_ABCB6 cd18581
Six-transmembrane helical domain of the ATP-binding cassette subfamily B member 6, ...
 144-441 1.25e-82

Six-transmembrane helical domain of the ATP-binding cassette subfamily B member 6, mitochondrial; This group represents the ABCB6 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. 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, ABCB6 (ABC transporter subfamily B, member 6) is closely related to yeast ATM1 and human ABCB7, 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: 350025 [Multi-domain]  Cd Length: 300  Bit Score: 264.88  E-value: 1.25e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  144 LGFLGGAKAMNIVVPFMFKYAVDSLnqmsgnmlnLSDAPNTVATMATAVLIGY-------GVSRAGAAFFNEVRNAVFGK 216
Cdd:cd18581   2 LLLLAAGRVVNVLVPILYKKIVDSL---------TPDSADSPLAFPWALILLYvflkflqGGGSGSVGLLSNLRSFLWIP 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  217 VAQNSIRRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGISFVLSALVFNLLPIMFEVMLVSGVLYYKCGAQFALV 296
Cdd:cd18581  73 VQQFTTREISVKLFAHLHSLSLRWHLSRKTGEVLRVMDRGTSSINSLLSYVLFNIGPTIADIIIAIIYFAIAFNPWFGLI 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  297 TLGTLGTYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNERYEAQRYDGFLKTYETASLKSTSTLAM 376
Cdd:cd18581 153 VFVTMALYLILTIIITEWRTKFRREMNKLDNEKRAKAVDSLLNFETVKYYNAERFEVERYRRAIDDYQVAEWKSNASLNL 232

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 8928549  377 LNFGQSAIFSVGLTAIMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDM 441
Cdd:cd18581 233 LNTAQNLIITIGLLAGSLLCAYFVVEGKLTVGDFVLFLTYIIQLYAPLNFFGTYYRMIQQSFIDM 297
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
 223-704 4.53e-79

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 268.13  E-value: 4.53e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    223 RRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGT----RGISFVLSALVFNLlpimfeVMLVsGVLYYKC--GAQFALV 296
Cdd:TIGR00958 234 LRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTqtmsRSLSLNVNVLLRNL------VMLL-GLLGFMLwlSPRLTMV 306

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    297 TLGTLGTYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNERYEAQRYDGFLKtyETASLKSTSTLA- 375
Cdd:TIGR00958 307 TLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALE--ETLQLNKRKALAy 384

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    376 MLNFGQSAIFSVGL-TAIMVLASQGIVAGTLTVGDLVMVngLLFQLSL--PLNFLGTVYRETRQALIDMNTLFTLLKVDT 452
Cdd:TIGR00958 385 AGYLWTTSVLGMLIqVLVLYYGGQLVLTGKVSSGNLVSF--LLYQEQLgeAVRVLSYVYSGMMQAVGASEKVFEYLDRKP 462

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    453 QIKDKVMASPLqitPQTATVAFDNVHFEYIE--GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIY 530
Cdd:TIGR00958 463 NIPLTGTLAPL---NLEGLIEFQDVSFSYPNrpDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVL 539

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    531 LAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNLLYGNISASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLS 610
Cdd:TIGR00958 540 LDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLS 619

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    611 GGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKdvVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTH 690
Cdd:TIGR00958 620 GGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRS--RASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTH 697

                         490
                  ....*....|....
gi 8928549    691 HGLLANPhSIYSEM 704
Cdd:TIGR00958 698 KQLMEDQ-GCYKHL 710
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
 472-683 4.10e-78

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: 248.07  E-value: 4.10e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  472 VAFDNVHFEYIEG-QKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGV 550
Cdd:cd03228   1 IEFKNVSFSYPGRpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  551 VPQDAVLFHNTIYYNLlygnisaspeevyavaklaglhdailrmphgydtqvgerglkLSGGEKQRVAIARAILKDPPVI 630
Cdd:cd03228  81 VPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPIL 118

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 8928549  631 LYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGK 683
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
 472-708 2.41e-77

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: 248.56  E-value: 2.41e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  472 VAFDNVHFEY-IEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGV 550
Cdd:cd03252   1 ITFEHVRFRYkPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  551 VPQDAVLFHNTIYYNLLYGNISASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVI 630
Cdd:cd03252  81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 8928549  631 LYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLLANpHSIYSEMWHTQ 708
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAE-NGLYAYLYQLQ 237
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
 472-689 1.37e-71

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: 232.77  E-value: 1.37e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  472 VAFDNVHFEYIEGQK-VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGV 550
Cdd:cd03244   3 IEFKNVSLRYRPNLPpVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISI 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  551 VPQDAVLFHNTIYYNL-LYGniSASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPV 629
Cdd:cd03244  83 IPQDPVLFSGTIRSNLdPFG--EYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  630 ILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGT 689
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
 182-706 1.61e-70

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: 244.65  E-value: 1.61e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    182 PNTVATMATAVLIGYGVSRAGAAFFNEVRNAVFGKVAQNSIRRIAKNVFLHLHNLDLGFHLSRQTGALskaIDRGTRGIS 261
Cdd:TIGR01193 188 PHKMMGTLGIISIGLIIAYIIQQILSYIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGEI---VSRFTDASS 264

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    262 FV--LSALVFNLLPIMFEVMLVSGVLYYKcGAQFALVTLGTLGTYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLN 339
Cdd:TIGR01193 265 IIdaLASTILSLFLDMWILVIVGLFLVRQ-NMLLFLLSLLSIPVYAVIIILFKRTFNKLNHDAMQANAVLNSSIIEDLNG 343

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    340 YETVKYFNNERYEAQRYDGFLKTYetasLKSTSTLAMLNFGQSAIFSV-GLTAIMVL---ASQGIVAGTLTVGDLVMVNG 415
Cdd:TIGR01193 344 IETIKSLTSEAERYSKIDSEFGDY----LNKSFKYQKADQGQQAIKAVtKLILNVVIlwtGAYLVMRGKLTLGQLITFNA 419

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    416 LLFQLSLPLNFLGTVYRETRQALIDMNTLFTLLKVDTQIKDKVMASPLqiTPQTATVAFDNVHFEYIEGQKVLSGISFEV 495
Cdd:TIGR01193 420 LLSYFLTPLENIINLQPKLQAARVANNRLNEVYLVDSEFINKKKRTEL--NNLNGDIVINDVSYSYGYGSNILSDISLTI 497

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    496 PAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNLLYGNI-SAS 574
Cdd:TIGR01193 498 KMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGAKeNVS 577

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    575 PEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDv 654
Cdd:TIGR01193 578 QDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLN- 656

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|..
gi 8928549    655 VKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLLaNPHSIYSEMWH 706
Cdd:TIGR01193 657 LQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELL-DRNGFYASLIH 707
NHLM_micro_ABC1 TIGR03796
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ...
 223-695 1.69e-70

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


Pssm-ID: 274788 [Multi-domain]  Cd Length: 710  Bit Score: 244.47  E-value: 1.69e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    223 RRIAKNVFLHLHNLDLGFHLSRQTGALSKAI---DRGTRGISFVLSALVFNLLPIMFEVMLVsgVLYykcGAQFALVTLG 299
Cdd:TIGR03796 227 VGMSARFLWHILRLPVRFFAQRHAGDIASRVqlnDQVAEFLSGQLATTALDAVMLVFYALLM--LLY---DPVLTLIGIA 301

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    300 TlgtyTAFTVAVTRWRTRFRIEMN-KADNDAG---NAAIDSLLNYETVKYFNNERYEAQRYDGflktYETASLKSTSTLA 375
Cdd:TIGR03796 302 F----AAINVLALQLVSRRRVDANrRLQQDAGkltGVAISGLQSIETLKASGLESDFFSRWAG----YQAKLLNAQQELG 373

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    376 MLNfgqsAIFSV------GLTAIMVLASQG--IVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDMNTLFTL 447
Cdd:TIGR03796 374 VLT----QILGVlptlltSLNSALILVVGGlrVMEGQLTIGMLVAFQSLMSSFLEPVNNLVGFGGTLQELEGDLNRLDDV 449

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    448 LK--VDTQIKDKVMASPLQITPQ--TATVAFDNVHFEY-IEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFY 522
Cdd:TIGR03796 450 LRnpVDPLLEEPEGSAATSEPPRrlSGYVELRNITFGYsPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLY 529

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    523 EPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNLLYGNISASPEEVYAVAKLAGLHDAILRMPHGYDTQV 602
Cdd:TIGR03796 530 QPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLWDPTIPDADLVRACKDAAIHDVITSRPGGYDAEL 609

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    603 GERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILgamkDVVKHR--TSIFIAHRLSTVVDADEIIVLD 680
Cdd:TIGR03796 610 AEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIID----DNLRRRgcTCIIVAHRLSTIRDCDEIIVLE 685

                         490
                  ....*....|....*
gi 8928549    681 QGKVAERGTHHGLLA 695
Cdd:TIGR03796 686 RGKVVQRGTHEELWA 700
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
 472-684 2.37e-69

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


Pssm-ID: 213212 [Multi-domain]  Cd Length: 220  Bit Score: 226.70  E-value: 2.37e-69
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  472 VAFDNVHFEYIEGQ-KVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGV 550
Cdd:cd03245   3 IEFRNVSFSYPNQEiPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGY 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  551 VPQDAVLFHNTIYYNLLYGNISASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVI 630
Cdd:cd03245  83 VPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPIL 162

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 8928549  631 LYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKV 684
Cdd:cd03245 163 LLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
ABC_6TM_HMT1 cd18583
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents ...
 147-444 8.23e-67

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: 222.79  E-value: 8.23e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  147 LGGAKAMNIVVPFMFKYAVDSLNQMSGNMlnlsdapntvatMATAVLIgYGVSR--AGAAFFNEVRNAVFGKVAQNSIRR 224
Cdd:cd18583   5 LLAERVLNVLVPRQLGIIVDSLSGGSGKS------------PWKEIGL-YVLLRflQSGGGLGLLRSWLWIPVEQYSYRA 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  225 IAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTrGISFVLSALVFNLLPIMFEVMLVSGVLYYKCGAQFALVTLGTLGTY 304
Cdd:cd18583  72 LSTAAFNHVMNLSMDFHDSKKSGEVLKAIEQGS-SINDLLEQILFQIVPMIIDLVIAIVYLYYLFDPYMGLIVAVVMVLY 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  305 TAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNERYEAQRYDGFLKTYETASLKSTSTLAMLNFGQSAI 384
Cdd:cd18583 151 VWSTIKLTSWRTKLRRDMIDADREERSILTESLLNWETVKYFNREPYEKERYREAVKNYQKAERKYLFSLNLLNAVQSLI 230

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  385 FSVGLTAIMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDMNTL 444
Cdd:cd18583 231 LTLGLLAGCFLAAYQVSQGQATVGDFVTLLTYWAQLSGPLNFFATLYRSIQSDLIDAERL 290
chvA TIGR01192
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ...
 386-693 3.11e-66

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


Pssm-ID: 130260 [Multi-domain]  Cd Length: 585  Bit Score: 230.16  E-value: 3.11e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    386 SVGLTAIMVLASQGIVAGTLTVGDLVMVNG----LLFQLSLPLNFLGTVYrETRQALIDmntlFTLLKVDTQIKDKVMAS 461
Cdd:TIGR01192 251 TISMMCILVIGTVLVIKGELSVGEVIAFIGfanlLIGRLDQMSGFITQIF-EARAKLED----FFDLEDSVFQREEPADA 325

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    462 PlQITPQTATVAFDNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSL 541
Cdd:TIGR01192 326 P-ELPNVKGAVEFRHITFEFANSSQGVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTR 404

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    542 ESLRRAVGVVPQDAVLFHNTIYYNLLYGNISASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIAR 621
Cdd:TIGR01192 405 ESLRKSIATVFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIAR 484

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 8928549    622 AILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGL 693
Cdd:TIGR01192 485 AILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQEL 556
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
 465-684 3.33e-65

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: 216.18  E-value: 3.33e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  465 ITPQT--ATVAFDNVHFEYIE--GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS 540
Cdd:cd03248   3 LAPDHlkGIVKFQNVTFAYPTrpDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYE 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  541 LESLRRAVGVVPQDAVLFHNTIYYNLLYGNISASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIA 620
Cdd:cd03248  83 HKYLHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIA 162

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 8928549  621 RAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKV 684
Cdd:cd03248 163 RALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
400-708 3.01e-61

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


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 216.12  E-value: 3.01e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   400 IVAGTLTVGDL---VMVNGLLFQLSLPLNFLGTVYRETRQALIDMNTLFTLLKVdtqIKDKVMASPlqitPQTATVAFDN 476
Cdd:PRK10789 246 VVNGSLTLGQLtsfVMYLGLMIWPMLALAWMFNIVERGSAAYSRIRAMLAEAPV---VKDGSEPVP----EGRGELDVNI 318

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   477 VHFEYIEGQK-VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDA 555
Cdd:PRK10789 319 RQFTYPQTDHpALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTP 398

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   556 VLFHNTIYYNLLYGNISASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEA 635
Cdd:PRK10789 399 FLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDA 478

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 8928549   636 TSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLLANPhSIYSEMWHTQ 708
Cdd:PRK10789 479 LSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQS-GWYRDMYRYQ 550
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
 139-679 1.81e-60

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: 212.92  E-value: 1.81e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    139 RVAISLGFLGGAkaMNIVVPFMFKYAVDSLNQMSGNMLNLSDAPNTVATMATA-VLIGYG----VSRAGAAFFNEVRNAV 213
Cdd:TIGR02857   6 ALLALLGVLGAL--LIIAQAWLLARVVDGLISAGEPLAELLPALGALALVLLLrALLGWLqeraAARAAAAVKSQLRERL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    214 FGKVAQNSIRRIAKnvflhlhnldlgfhlsRQTGALSKAIDRGTRGisfvLSALVFNLLPIMFEVMLVSGVLYYKCGAQ- 292
Cdd:TIGR02857  84 LEAVAALGPRWLQG----------------RPSGELATLALEGVEA----LDGYFARYLPQLVLAVIVPLAILAAVFPQd 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    293 --FALVTLGTLGTYTAFtVAVTRWRTRFRIEMN-KADNDAGNAAIDSLLNYETVKYFNNERYEAQRydgfLKTYETASLK 369
Cdd:TIGR02857 144 wiSGLILLLTAPLIPIF-MILIGWAAQAAARKQwAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAA----IRRSSEEYRE 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    370 ST-STLAMlNFGQSAIF------SVGLTAIMVlasqGIvagTLTVGDLVMVNGLLFQL-----SLPLNFLGTVYRETRQA 437
Cdd:TIGR02857 219 RTmRVLRI-AFLSSAVLelfatlSVALVAVYI----GF---RLLAGDLDLATGLFVLLlapefYLPLRQLGAQYHARADG 290

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    438 LIDMNTLFTLLKVDTQI----KDKVMASPLQITpqtatvaFDNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKST 513
Cdd:TIGR02857 291 VAAAEALFAVLDAAPRPlagkAPVTAAPASSLE-------FSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKST 363

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    514 IVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNLLYGNISASPEEVYAVAKLAGLHDAILR 593
Cdd:TIGR02857 364 LLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAA 443

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    594 MPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDA 673
Cdd:TIGR02857 444 LPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALA 523


                  ....*.
gi 8928549    674 DEIIVL 679
Cdd:TIGR02857 524 DRIVVL 529
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
 464-696 7.32e-60

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 212.38  E-value: 7.32e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   464 QITPQTATVAFDNVHFEYIEG-QKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLE 542
Cdd:PRK11160 331 TAAADQVSLTLNNVSFTYPDQpQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEA 410

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   543 SLRRAVGVVPQDAVLFHNTIYYNLLYGNISASPEEVYAVAKLAGLhDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARA 622
Cdd:PRK11160 411 ALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGL-EKLLEDDKGLNAWLGEGGRQLSGGEQRRLGIARA 489

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 8928549   623 ILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLLAN 696
Cdd:PRK11160 490 LLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQ 563
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
350-708 3.64e-59

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


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 210.73  E-value: 3.64e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   350 RYEAQRYDGFLkTYETASLKSTSTLA--MLNFGQSAifsvgltaimvlasqgivAGTLTVGDLVMVNGLLFQLSLPLNFL 427
Cdd:PRK10790 241 RMQTLRLDGFL-LRPLLSLFSALILCglLMLFGFSA------------------SGTIEVGVLYAFISYLGRLNEPLIEL 301

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   428 GTVYRETRQALIDMNTLFTLlkvdtqikdkvMASPLQ------ITPQTATVAFDNVHFEYIEGQKVLSGISFEVPAGKKV 501
Cdd:PRK10790 302 TTQQSMLQQAVVAGERVFEL-----------MDGPRQqygnddRPLQSGRIDIDNVSFAYRDDNLVLQNINLSVPSRGFV 370

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   502 AIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNLLYG-NISAspEEVYA 580
Cdd:PRK10790 371 ALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGrDISE--EQVWQ 448

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   581 VAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTS 660
Cdd:PRK10790 449 ALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTL 528

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 8928549   661 IFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLLANpHSIYSEMWHTQ 708
Cdd:PRK10790 529 VVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAA-QGRYWQMYQLQ 575
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
 355-667 9.49e-55

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: 197.20  E-value: 9.49e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    355 RYDGFLKTYETASLKST----STLAMLNFGQSA-IFSVGLTAIMVL--ASQGIVAGTLTVGDLVMVngLLFQLSL--PLN 425
Cdd:TIGR02868 211 ALPAALAQVEEADRELTraerRAAAATALGAALtLLAAGLAVLGALwaGGPAVADGRLAPVTLAVL--VLLPLAAfeAFA 288

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    426 FLGTVYRETRQALIDMNTLFTLLKVDTQIKDKVMASPLQITPQTATVAFDNVHFEYIEGQKVLSGISFEVPAGKKVAIVG 505
Cdd:TIGR02868 289 ALPAAAQQLTRVRAAAERIVEVLDAAGPVAEGSAPAAGAVGLGKPTLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILG 368

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    506 GSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNLLYGNISASPEEVYAVAKLA 585
Cdd:TIGR02868 369 PSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERV 448

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    586 GLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAH 665
Cdd:TIGR02868 449 GLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITH 528


                  ..
gi 8928549    666 RL 667
Cdd:TIGR02868 529 HL 530
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
 293-685 1.12e-54

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


Pssm-ID: 443660 [Multi-domain]  Cd Length: 563  Bit Score: 197.66  E-value: 1.12e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  293 FALVTLGTLGTYTAFTVAvTRWRTRFRI-EMNKADNDAGNAAIDSLLNYETVkyfnneryEA------------QRYDGF 359
Cdd:COG4618 157 LGLLALVGALVLVALALL-NERLTRKPLkEANEAAIRANAFAEAALRNAEVI--------EAmgmlpalrrrwqRANARA 227

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  360 LKTYETASLKSTSTLAML----NFGQSAIFSVGltAIMVLASQ----GIVAGTLTVG------DLVMVNGLLFQlslpln 425
Cdd:COG4618 228 LALQARASDRAGGFSALSkflrLLLQSAVLGLG--AYLVIQGEitpgAMIAASILMGralapiEQAIGGWKQFV------ 299

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  426 flgtvyrETRQALIDMNTLFTLLKVDtqikDKVMASPlqiTPQtATVAFDNVHFEYIEGQK-VLSGISFEVPAGKKVAIV 504
Cdd:COG4618 300 -------SARQAYRRLNELLAAVPAE----PERMPLP---RPK-GRLSVENLTVVPPGSKRpILRGVSFSLEPGEVLGVI 364

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  505 GGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYynllyGNIS----ASPEEVYA 580
Cdd:COG4618 365 GPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIA-----ENIArfgdADPEKVVA 439

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  581 VAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTS 660
Cdd:COG4618 440 AAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGAT 519

                       410       420
                ....*....|....*....|....*.
gi 8928549  661 IF-IAHRLSTVVDADEIIVLDQGKVA 685
Cdd:COG4618 520 VVvITHRPSLLAAVDKLLVLRDGRVQ 545
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
 467-689 1.53e-53

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: 183.77  E-value: 1.53e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  467 PQTATVAFDNVHFEYI-EGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLR 545
Cdd:cd03369   2 PEHGEIEVENLSVRYApDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLR 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  546 RAVGVVPQDAVLFHNTIYYNL-LYGNIsaSPEEVYAVAKlaglhdailrmphgydtqVGERGLKLSGGEKQRVAIARAIL 624
Cdd:cd03369  82 SSLTIIPQDPTLFSGTIRSNLdPFDEY--SDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALL 141

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 8928549  625 KDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGT 689
Cdd:cd03369 142 KRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
 418-697 3.62e-52

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 191.21  E-value: 3.62e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   418 FQlslPLNFLGTVYRETRQALIDMNTLFTLLKVDTQikdkvmasplqiTPQTATVAFDNVHFEYIEGQ---------KVL 488
Cdd:PRK11174 301 YQ---PLRDLGTFYHAKAQAVGAAESLVTFLETPLA------------HPQQGEKELASNDPVTIEAEdleilspdgKTL 365

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   489 SG-ISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYePQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNLL 567
Cdd:PRK11174 366 AGpLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVL 444

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   568 YGNISASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETI 647
Cdd:PRK11174 445 LGNPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLV 524

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 8928549   648 LGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLLANP 697
Cdd:PRK11174 525 MQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAG 574
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
 472-697 2.77e-51

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


Pssm-ID: 440739 [Multi-domain]  Cd Length: 230  Bit Score: 178.29  E-value: 2.77e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  472 VAFDNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVV 551
Cdd:COG1122   1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  552 PQDAV--LFHNTIYYNLLYG--NISASPEE----VYAVAKLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARAI 623
Cdd:COG1122  81 FQNPDdqLFAPTVEEDVAFGpeNLGLPREEirerVEEALELVGLEHLADRPPH-----------ELSGGQKQRVAIAGVL 149

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 8928549  624 LKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIA-HRLSTVVD-ADEIIVLDQGKVAERGTHHGLLANP 697
Cdd:COG1122 150 AMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVtHDLDLVAElADRVIVLDDGRIVADGTPREVFSDY 225
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
 472-688 3.03e-49

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: 170.96  E-value: 3.03e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  472 VAFDNVHFEYIE-GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSlESLRRAVGV 550
Cdd:cd03247   1 LSINNVSFSYPEqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  551 VPQDAVLFHNTIYYNLlygnisaspeevyavaklaglhdailrmphgydtqvgerGLKLSGGEKQRVAIARAILKDPPVI 630
Cdd:cd03247  80 LNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPIV 120

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 8928549  631 LYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERG 688
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
 474-698 8.88e-48

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: 168.83  E-value: 8.88e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  474 FDNVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS---LESLRRAVGV 550
Cdd:cd03261   3 LRGLTKSF-GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSeaeLYRLRRRMGM 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  551 VPQDAVLF-HNTIYYNL---LYGNISASPEEVYAVA--KLA--GLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARA 622
Cdd:cd03261  82 LFQSGALFdSLTVFENVafpLREHTRLSEEEIREIVleKLEavGLRGAEDLYPA-----------ELSGGMKKRVALARA 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  623 ILKDPPVILYDEATSSLDSIT----EETILgAMKDVVKHrTSIFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGLLANP 697
Cdd:cd03261 151 LALDPELLLYDEPTAGLDPIAsgviDDLIR-SLKKELGL-TSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRASD 228


                .
gi 8928549  698 H 698
Cdd:cd03261 229 D 229
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
 472-701 1.02e-47

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


Pssm-ID: 440740 [Multi-domain]  Cd Length: 514  Bit Score: 177.02  E-value: 1.02e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  472 VAFDNVHFEY----IEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS---LESL 544
Cdd:COG1123 261 LEVRNLSKRYpvrgKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLREL 340

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  545 RRAVGVVPQD--AVLF-HNTIYYNL-----LYGNISAS--PEEVYAVAKLAGLHDAIL-RMPHGydtqvgerglkLSGGE 613
Cdd:COG1123 341 RRRVQMVFQDpySSLNpRMTVGDIIaeplrLHGLLSRAerRERVAELLERVGLPPDLAdRYPHE-----------LSGGQ 409

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  614 KQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLSTVVD-ADEIIVLDQGKVAERGTH 690
Cdd:COG1123 410 RQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELglTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPT 489

                       250
                ....*....|.
gi 8928549  691 HGLLANPHSIY 701
Cdd:COG1123 490 EEVFANPQHPY 500
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
474-684 3.26e-47

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 166.53  E-value: 3.26e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  474 FDNVHFEyIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQ 553
Cdd:COG4619   3 LEGLSFR-VGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVPQ 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  554 DAVLFHNTIYYNLL----YGNISASPEEVYAVAKLAGLHDAILrmphgyDTQVGErglkLSGGEKQRVAIARAILKDPPV 629
Cdd:COG4619  82 EPALWGGTVRDNLPfpfqLRERKFDRERALELLERLGLPPDIL------DKPVER----LSGGERQRLALIRALLLQPDV 151

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 8928549  630 ILYDEATSSLDSITEETILGAMKDVVKH--RTSIFIAH------RLstvvdADEIIVLDQGKV 684
Cdd:COG4619 152 LLLDEPTSALDPENTRRVEELLREYLAEegRAVLWVSHdpeqieRV-----ADRVLTLEAGRL 209
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
 472-698 5.51e-47

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


Pssm-ID: 440744 [Multi-domain]  Cd Length: 241  Bit Score: 167.08  E-value: 5.51e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  472 VAFDNVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS---LESLRRAV 548
Cdd:COG1127   6 IEVRNLTKSF-GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekeLYELRRRI 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  549 GVVPQDAVLFHN-TIYYNLLYG---NISASPEEVYAVA--KLA--GLHDAILRMPhgydtqvGErglkLSGGEKQRVAIA 620
Cdd:COG1127  85 GMLFQGGALFDSlTVFENVAFPlreHTDLSEAEIRELVleKLElvGLPGAADKMP-------SE----LSGGMRKRVALA 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  621 RAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGLLANP 697
Cdd:COG1127 154 RALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELglTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLASD 233


                .
gi 8928549  698 H 698
Cdd:COG1127 234 D 234
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
472-686 3.60e-45

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 161.37  E-value: 3.60e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  472 VAFDNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS---LESLRRAV 548
Cdd:COG2884   2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrreIPYLRRRI 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  549 GVVPQDA-VLFHNTIYYNLLY-----GnisASPEE----VYAVAKLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVA 618
Cdd:COG2884  82 GVVFQDFrLLPDRTVYENVALplrvtG---KSRKEirrrVREVLDLVGLSDKAKALPH-----------ELSGGEQQRVA 147

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 8928549  619 IARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIA-HRLSTVvdaDE----IIVLDQGKVAE 686
Cdd:COG2884 148 IARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIAtHDLELV---DRmpkrVLELEDGRLVR 217
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
 475-702 6.43e-45

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


Pssm-ID: 440741 [Multi-domain]  Cd Length: 248  Bit Score: 161.51  E-value: 6.43e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  475 DNVHFEY---IEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVV 551
Cdd:COG1124   5 RNLSVSYgqgGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMV 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  552 PQDAVL-FH--NTIYYNL-----LYGnISASPEEVYAVAKLAGLHDAIL-RMPHgydtqvgerglKLSGGEKQRVAIARA 622
Cdd:COG1124  85 FQDPYAsLHprHTVDRILaeplrIHG-LPDREERIAELLEQVGLPPSFLdRYPH-----------QLSGGQRQRVAIARA 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  623 ILKDPPVILYDEATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLStVVD--ADEIIVLDQGKVAERGTHHGLLANPH 698
Cdd:COG1124 153 LILEPELLLLDEPTSALDVSVQAEILNLLKDLREERglTYLFVSHDLA-VVAhlCDRVAVMQNGRIVEELTVADLLAGPK 231


                ....
gi 8928549  699 SIYS 702
Cdd:COG1124 232 HPYT 235
PLN03130 PLN03130
ABC transporter C family member; Provisional
 415-739 1.08e-44

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 174.16  E-value: 1.08e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    415 GLLfqLSLPLNFLGTVYRETRQALIDMNTLFTLLKVDTQIkDKVMASPLQIT--------PQTATVAFDNVHFEY-IEGQ 485
Cdd:PLN03130 1176 GLL--LSYALNITSLLTAVLRLASLAENSLNAVERVGTYI-DLPSEAPLVIEnnrpppgwPSSGSIKFEDVVLRYrPELP 1252

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    486 KVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYN 565
Cdd:PLN03130 1253 PVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFN 1332

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    566 LLYGNiSASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEE 645
Cdd:PLN03130 1333 LDPFN-EHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDA 1411

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    646 TILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLLANPHSIYSEMwhTQSSRVQNHDNPKWEA--K 723
Cdd:PLN03130 1412 LIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFSKM--VQSTGAANAQYLRSLVfgG 1489

                         330
                  ....*....|....*.
gi 8928549    724 KENISKEEERKKLQEE 739
Cdd:PLN03130 1490 DEDRLAREESKALDGQ 1505
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
 474-683 2.99e-44

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: 158.40  E-value: 2.99e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  474 FDNVHFEYIEG-QKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVP 552
Cdd:cd03225   2 LKNLSFSYPDGaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVF 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  553 QDA--VLFHNTIYYNLLYG--NISASPEEVYAVAKLA----GLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARAIL 624
Cdd:cd03225  82 QNPddQFFGPTVEEEVAFGleNLGLPEEEIEERVEEAlelvGLEGLRDRSPF-----------TLSGGQKQRVAIAGVLA 150

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 8928549  625 KDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIA-HRLSTVVD-ADEIIVLDQGK 683
Cdd:cd03225 151 MDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVtHDLDLLLElADRVIVLEDGK 211
PLN03232 PLN03232
ABC transporter C family member; Provisional
 371-728 4.08e-44

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 172.08  E-value: 4.08e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    371 TSTLAMLNFGQSAiFSVGLTAIMVLasqgIVAGTLTVGDLVmvNGLLFQLSLPLNFLGTVYRETRqaLIDMNTLFTLLKV 450
Cdd:PLN03232 1151 TATFAVLRNGNAE-NQAGFASTMGL----LLSYTLNITTLL--SGVLRQASKAENSLNSVERVGN--YIDLPSEATAIIE 1221

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    451 DTQikdkvmasPLQITPQTATVAFDNVHFEYIEG-QKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSI 529
Cdd:PLN03232 1222 NNR--------PVSGWPSRGSIKFEDVHLRYRPGlPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRI 1293

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    530 YLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNLlygnisaSPEEVYAVAKL------AGLHDAILRMPHGYDTQVG 603
Cdd:PLN03232 1294 MIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNI-------DPFSEHNDADLwealerAHIKDVIDRNPFGLDAEVS 1366

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    604 ERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGK 683
Cdd:PLN03232 1367 EGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQ 1446

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 8928549    684 VAERGTHHGLLANPHSIYSEMWH-TQSSRVQNHDNPKWEAKKENIS 728
Cdd:PLN03232 1447 VLEYDSPQELLSRDTSAFFRMVHsTGPANAQYLSNLVFERRENGMS 1492
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
 476-688 2.12e-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: 156.51  E-value: 2.12e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  476 NVHF-EYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS---LESLRRAVGVV 551
Cdd:cd03257   8 SVSFpTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIRRKEIQMV 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  552 PQDAVLFHN---TIYYNL---LYGNISASPEEVYAVAKLA-----GLHDAILRM-PHgydtqvgerglKLSGGEKQRVAI 619
Cdd:cd03257  88 FQDPMSSLNprmTIGEQIaepLRIHGKLSKKEARKEAVLLllvgvGLPEEVLNRyPH-----------ELSGGQRQRVAI 156

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 8928549  620 ARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLSTVVD-ADEIIVLDQGKVAERG 688
Cdd:cd03257 157 ARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELglTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
 475-684 8.08e-43

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: 152.76  E-value: 8.08e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  475 DNVHFEYIEGQK-VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQ 553
Cdd:cd03246   4 ENVSFRYPGAEPpVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQ 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  554 DAVLFHNTIyynllYGNIsaspeevyavaklaglhdailrmphgydtqvgerglkLSGGEKQRVAIARAILKDPPVILYD 633
Cdd:cd03246  84 DDELFSGSI-----AENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLD 121

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 8928549  634 EATSSLDSITEETILGAMKDV-VKHRTSIFIAHRLSTVVDADEIIVLDQGKV 684
Cdd:cd03246 122 EPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
 484-688 1.06e-42

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


Pssm-ID: 213226 [Multi-domain]  Cd Length: 213  Bit Score: 153.83  E-value: 1.06e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  484 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLEslRRAVGVVPQDAVLF-HNTI 562
Cdd:cd03259  12 SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMVFQDYALFpHLTV 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  563 YYNLLYG-NISASPEE-----VYAVAKLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARAILKDPPVILYDEAT 636
Cdd:cd03259  90 AENIAFGlKLRGVPKAeirarVRELLELVGLEGLLNRYPH-----------ELSGGQQQRVALARALAREPSLLLLDEPL 158

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 8928549  637 SSLDSITEETILGAMKDVVK--HRTSIFIAHRLSTVVD-ADEIIVLDQGKVAERG 688
Cdd:cd03259 159 SALDAKLREELREELKELQRelGITTIYVTHDQEEALAlADRIAVMNEGRIVQVG 213
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
 472-699 1.26e-42

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


Pssm-ID: 213262 [Multi-domain]  Cd Length: 242  Bit Score: 154.77  E-value: 1.26e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  472 VAFDNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVV 551
Cdd:cd03295   1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  552 PQDAVLF-HNTIYYNL-LYGNISASPEE-----VYAVAKLAGLHDAIL--RMPHgydtqvgerglKLSGGEKQRVAIARA 622
Cdd:cd03295  81 IQQIGLFpHMTVEENIaLVPKLLKWPKEkirerADELLALVGLDPAEFadRYPH-----------ELSGGQQQRVGVARA 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  623 ILKDPPVILYDEATSSLDSITEETILGAMKDVVK--HRTSIFIAHRL-STVVDADEIIVLDQGKVAERGTHHGLLANPHS 699
Cdd:cd03295 150 LAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILRSPAN 229
PTZ00243 PTZ00243
ABC transporter; Provisional
 460-704 1.54e-42

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 167.26  E-value: 1.54e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    460 ASPLQITP---QTATVAFDNVHFEYIEGQK-VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQN 535
Cdd:PTZ00243 1294 ASPTSAAPhpvQAGSLVFEGVQMRYREGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGRE 1373

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    536 IQDVSLESLRRAVGVVPQDAVLFHNTIYYNlLYGNISASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQ 615
Cdd:PTZ00243 1374 IGAYGLRELRRQFSMIPQDPVLFDGTVRQN-VDPFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQ 1452

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    616 RVAIARAILK-DPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLL 694
Cdd:PTZ00243 1453 LMCMARALLKkGSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELV 1532

                         250
                  ....*....|
gi 8928549    695 ANPHSIYSEM 704
Cdd:PTZ00243 1533 MNRQSIFHSM 1542
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 488-637 3.66e-42

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


Pssm-ID: 394964 [Multi-domain]  Cd Length: 150  Bit Score: 150.11  E-value: 3.66e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    488 LSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLF-HNTIYYNL 566
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 8928549    567 LYGnisASPEEVYAVAKLAGLHDAI--LRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATS 637
Cdd:pfam00005  81 RLG---LLLKGLSKREKDARAEEALekLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
 472-688 4.03e-42

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: 152.72  E-value: 4.03e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  472 VAFDNVHFEYIEGQkVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYE-----PQKGSIYLAGQNI--QDVSLESL 544
Cdd:cd03260   1 IELRDLNVYYGDKH-ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIydLDVDVLEL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  545 RRAVGVVPQDAVLFHNTIYYNLLYG-------NISASPEEVYAVAKLAGLHDAILRMPHGydtqvgergLKLSGGEKQRV 617
Cdd:cd03260  80 RRRVGMVFQKPNPFPGSIYDNVAYGlrlhgikLKEELDERVEEALRKAALWDEVKDRLHA---------LGLSGGQQQRL 150

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 8928549  618 AIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAH------RLstvvdADEIIVLDQGKVAERG 688
Cdd:cd03260 151 CLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHnmqqaaRV-----ADRTAFLLNGRLVEFG 222
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
472-695 2.44e-41

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 150.98  E-value: 2.44e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  472 VAFDNVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLEsLRRAVGVV 551
Cdd:COG1131   1 IEVRGLTKRY-GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAE-VRRRIGYV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  552 PQDAVLFHN-TIYYNL-----LYG-NISASPEEVYAVAKLAGLHDAIlrmphgyDTQVGerglKLSGGEKQRVAIARAIL 624
Cdd:COG1131  79 PQEPALYPDlTVRENLrffarLYGlPRKEARERIDELLELFGLTDAA-------DRKVG----TLSGGMKQRLGLALALL 147

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 8928549  625 KDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIA-HRLSTVVD-ADEIIVLDQGKVAERGTHHGLLA 695
Cdd:COG1131 148 HDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLStHYLEEAERlCDRVAIIDKGRIVADGTPDELKA 220
ECF_ATPase_1 TIGR04520
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
 472-689 2.70e-41

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: 151.81  E-value: 2.70e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    472 VAFDNVHFEYIEGQK-VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS-LESLRRAVG 549
Cdd:TIGR04520   1 IEVENVSFSYPESEKpALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEEnLWEIRKKVG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    550 VVPQ--DAVLFHNTIYYNLLYG--NISASPEE----VYAVAKLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVAIAR 621
Cdd:TIGR04520  81 MVFQnpDNQFVGATVEDDVAFGleNLGVPREEmrkrVDEALKLVGMEDFRDREPH-----------LLSGGQKQRVAIAG 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    622 AILKDPPVILYDEATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLSTVVDADEIIVLDQGKVAERGT 689
Cdd:TIGR04520 150 VLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEgiTVISITHDMEEAVLADRVIVMNKGKIVAEGT 219
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
 472-697 3.27e-41

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: 150.42  E-value: 3.27e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  472 VAFDNVHFEYIEGQK---VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS---LESLR 545
Cdd:cd03258   2 IELKNVSKVFGDTGGkvtALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSgkeLRKAR 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  546 RAVGVVPQdavlfhntiYYNLL-----YGNI-----------SASPEEVYAVAKLAGLHDAIlrmpHGYDTQvgerglkL 609
Cdd:cd03258  82 RRIGMIFQ---------HFNLLssrtvFENValpleiagvpkAEIEERVLELLELVGLEDKA----DAYPAQ-------L 141

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  610 SGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLSTVVD-ADEIIVLDQGKVAE 686
Cdd:cd03258 142 SGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELglTIVLITHEMEVVKRiCDRVAVMEKGEVVE 221

                       250
                ....*....|.
gi 8928549  687 RGTHHGLLANP 697
Cdd:cd03258 222 EGTVEEVFANP 232
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
 472-697 5.33e-41

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


Pssm-ID: 440740 [Multi-domain]  Cd Length: 514  Bit Score: 157.76  E-value: 5.33e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  472 VAFDNVHFEYIEGQK-VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQ---KGSIYLAGQNIQDVSLESLRRA 547
Cdd:COG1123   5 LEVRDLSVRYPGGDVpAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  548 VGVVPQD--AVLFHNTIYYNLLYG--NISASPEE----VYAVAKLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVAI 619
Cdd:COG1123  85 IGMVFQDpmTQLNPVTVGDQIAEAleNLGLSRAEararVLELLEAVGLERRLDRYPH-----------QLSGGQRQRVAI 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  620 ARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGLLAN 696
Cdd:COG1123 154 AMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILAA 233


                .
gi 8928549  697 P 697
Cdd:COG1123 234 P 234
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
 418-702 8.90e-41

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: 161.65  E-value: 8.90e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549     418 FQLSLPLNFLGTVYRETRQALIDMNTLFTLLKVDTQIKDKVMAS-PLQITPQTATVAFDNVHFEYIEGQK-VLSGISFEV 495
Cdd:TIGR00957 1230 LQVTFYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPWQIQETaPPSGWPPRGRVEFRNYCLRYREDLDlVLRHINVTI 1309

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549     496 PAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNL-LYGniSAS 574
Cdd:TIGR00957 1310 HGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLdPFS--QYS 1387

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549     575 PEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDV 654
Cdd:TIGR00957 1388 DEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQ 1467

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 8928549     655 VKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLLANPHSIYS 702
Cdd:TIGR00957 1468 FEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYS 1515
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
 472-699 1.00e-40

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


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 149.37  E-value: 1.00e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  472 VAFDNVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQD--VSLESLRRAVG 549
Cdd:COG1126   2 IEIENLHKSF-GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDskKDINKLRRKVG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  550 VVPQDAVLF-HNTIYYNLLYGNISA---SPEEVYAVAK--LA--GLHDAILRMPHgydtqvgerglKLSGGEKQRVAIAR 621
Cdd:COG1126  81 MVFQQFNLFpHLTVLENVTLAPIKVkkmSKAEAEERAMelLErvGLADKADAYPA-----------QLSGGQQQRVAIAR 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  622 AILKDPPVILYDEATSSLD--SITEetILGAMKDVVK-HRTSIFIAHRLS---TVvdADEIIVLDQGKVAERGTHHGLLA 695
Cdd:COG1126 150 ALAMEPKVMLFDEPTSALDpeLVGE--VLDVMRDLAKeGMTMVVVTHEMGfarEV--ADRVVFMDGGRIVEEGPPEEFFE 225


                ....
gi 8928549  696 NPHS 699
Cdd:COG1126 226 NPQH 229
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
 474-683 1.37e-40

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


Pssm-ID: 213196 [Multi-domain]  Cd Length: 178  Bit Score: 146.95  E-value: 1.37e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  474 FDNVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLES--LRRAVGVV 551
Cdd:cd03229   3 LKNVSKRY-GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRRIGMV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  552 PQDAVLF-HNTIYYNLLYGnisaspeevyavaklaglhdailrmphgydtqvgerglkLSGGEKQRVAIARAILKDPPVI 630
Cdd:cd03229  82 FQDFALFpHLTVLENIALG---------------------------------------LSGGQQQRVALARALAMDPDVL 122

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 8928549  631 LYDEATSSLDSITEETILGAMKDVVKH--RTSIFIAHRLSTVVD-ADEIIVLDQGK 683
Cdd:cd03229 123 LLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARlADRVVVLRDGK 178
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
472-686 6.25e-40

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 146.73  E-value: 6.25e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  472 VAFDNVHFEYIEGQ---KVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS---LESLR 545
Cdd:COG1136   5 LELRNLTKSYGTGEgevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSereLARLR 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  546 R-AVGVVPQdavlFHN-----TIYYN----LLYGNISAS--PEEVYAVAKLAGLHDAILRMPHgydtqvgerglKLSGGE 613
Cdd:COG1136  85 RrHIGFVFQ----FFNllpelTALENvalpLLLAGVSRKerRERARELLERVGLGDRLDHRPS-----------QLSGGQ 149

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 8928549  614 KQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVK--HRTSIFIAHRLSTVVDADEIIVLDQGKVAE 686
Cdd:COG1136 150 QQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRelGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
 177-703 7.31e-40

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 159.04  E-value: 7.31e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    177 NLSDAPNTVATMATAVLIGYGVSRAGAAFFNevrNAVFGKVAQNSIRRIAKNVFLHlhnlDLGF--HLSRQTGALSKAID 254
Cdd:PTZ00265  860 NLEANSNKYSLYILVIAIAMFISETLKNYYN---NVIGEKVEKTMKRRLFENILYQ----EISFfdQDKHAPGLLSAHIN 932

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    255 RGtrgISFVLSALVFNLLPIMFEVML--VSGVL-YYKCGAQFALVTlgtlGTYTAFT-VAVTRWRTRFRIEMNKAD-NDA 329
Cdd:PTZ00265  933 RD---VHLLKTGLVNNIVIFTHFIVLflVSMVMsFYFCPIVAAVLT----GTYFIFMrVFAIRARLTANKDVEKKEiNQP 1005

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    330 GNAAI----------------DSLLNYETVKYFNNERYEAQRYDGFLKTYETASLKSTSTLAML-NFGQSAIFSVGLTAI 392
Cdd:PTZ00265 1006 GTVFAynsddeifkdpsfliqEAFYNMNTVIIYGLEDYFCNLIEKAIDYSNKGQKRKTLVNSMLwGFSQSAQLFINSFAY 1085

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    393 MvLASQGIVAGTLTVGDLVMVnglLFQLSLPLNFLGTVYR---ETRQALIDMNTLFTLL--KVDTQIKDKVMASPLQITP 467
Cdd:PTZ00265 1086 W-FGSFLIRRGTILVDDFMKS---LFTFLFTGSYAGKLMSlkgDSENAKLSFEKYYPLIirKSNIDVRDNGGIRIKNKND 1161

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    468 QTATVAFDNVHFEYIEGQKV--LSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYE---------------------- 523
Cdd:PTZ00265 1162 IKGKIEIMDVNFRYISRPNVpiYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqd 1241

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    524 --------------------------------PQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNLLYGNI 571
Cdd:PTZ00265 1242 yqgdeeqnvgmknvnefsltkeggsgedstvfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKE 1321

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    572 SASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAM 651
Cdd:PTZ00265 1322 DATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTI 1401

                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 8928549    652 KDVVKH--RTSIFIAHRLSTVVDADEIIVLDQGK-----VAERGTHHGLLANPHSIYSE 703
Cdd:PTZ00265 1402 VDIKDKadKTIITIAHRIASIKRSDKIVVFNNPDrtgsfVQAHGTHEELLSVQDGVYKK 1460
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
 469-689 1.16e-39

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 147.44  E-value: 1.16e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   469 TATVAFDNVHFEYIEGQK-VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRA 547
Cdd:PRK13632   5 SVMIKVENVSFSYPNSENnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKK 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   548 VGVVPQ--DAVLFHNTIYYNLLYG--NISASPEE----VYAVAKLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVAI 619
Cdd:PRK13632  85 IGIIFQnpDNQFIGATVEDDIAFGleNKKVPPKKmkdiIDDLAKKVGMEDYLDKEPQ-----------NLSGGQKQRVAI 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 8928549   620 ARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLSTVVDADEIIVLDQGKVAERGT 689
Cdd:PRK13632 154 ASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEAILADKVIVFSEGKLIAQGK 225
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
 467-733 1.54e-39

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 157.88  E-value: 1.54e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    467 PQTATVAFDNVHFEYIEGQKV--LSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLA-GQNIQDVSLES 543
Cdd:PTZ00265  378 KDIKKIQFKNVRFHYDTRKDVeiYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdSHNLKDINLKW 457

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    544 LRRAVGVVPQDAVLFHNTIYYNLLYG----------------NISASPE------------------------------- 576
Cdd:PTZ00265  458 WRSKIGVVSQDPLLFSNSIKNNIKYSlyslkdlealsnyyneDGNDSQEnknkrnscrakcagdlndmsnttdsneliem 537

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    577 ----------EVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEET 646
Cdd:PTZ00265  538 rknyqtikdsEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYL 617

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    647 ILGAMKDVV--KHRTSIFIAHRLSTVVDADEIIVL------------------------------DQGK----------- 683
Cdd:PTZ00265  618 VQKTINNLKgnENRITIIIAHRLSTIRYANTIFVLsnrergstvdvdiigedptkdnkennnknnKDDNnnnnnnnnnki 697

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 8928549    684 ------VAERGTHHGLLANPHSIYSEMWHTQ---SSRVQNHDNPKWEAKKENISKEEER 733
Cdd:PTZ00265  698 nnagsyIIEQGTHDALMKNKNGIYYTMINNQkvsSKKSSNNDNDKDSDMKSSAYKDSER 756
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
 474-683 5.42e-39

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: 141.61  E-value: 5.42e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  474 FDNVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQ 553
Cdd:cd00267   2 IENLSFRY-GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  554 davlfhntiyynllygnisaspeevyavaklaglhdailrmphgydtqvgerglkLSGGEKQRVAIARAILKDPPVILYD 633
Cdd:cd00267  81 -------------------------------------------------------LSGGQRQRVALARALLLNPDLLLLD 105

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 8928549  634 EATSSLDSITEETILGAMKDVVKH-RTSIFIAHRLSTVVDA-DEIIVLDQGK 683
Cdd:cd00267 106 EPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAELAaDRVIVLKDGK 157
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
 472-684 1.72e-38

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


Pssm-ID: 213222 [Multi-domain]  Cd Length: 218  Bit Score: 142.24  E-value: 1.72e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  472 VAFDNVHFEYIEG---QKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS---LESLR 545
Cdd:cd03255   1 IELKNLSKTYGGGgekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSekeLAAFR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  546 RA-VGVVPQdavlFHN-----TIYYN-----LLYGNISASPEE-VYAVAKLAGLHDAILRMPHgydtqvgerglKLSGGE 613
Cdd:cd03255  81 RRhIGFVFQ----SFNllpdlTALENvelplLLAGVPKKERRErAEELLERVGLGDRLNHYPS-----------ELSGGQ 145

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 8928549  614 KQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLSTVVDADEIIVLDQGKV 684
Cdd:cd03255 146 QQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAgtTIVVVTHDPELAEYADRIIELRDGKI 218
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
 472-683 3.28e-38

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: 141.07  E-value: 3.28e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  472 VAFDNVHFEYIEGQ----KVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQniqdvsleslrra 547
Cdd:cd03250   1 ISVEDASFTWDSGEqetsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------- 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  548 VGVVPQDAVLFHNTIYYNLLYGnisaSP--EEVY-AVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAIL 624
Cdd:cd03250  68 IAYVSQEPWIQNGTIRENILFG----KPfdEERYeKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVY 143

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 8928549  625 KDPPVILYDEATSSLDS-----ITEETILGAMKDvvkHRTSIFIAHRLSTVVDADEIIVLDQGK 683
Cdd:cd03250 144 SDADIYLLDDPLSAVDAhvgrhIFENCILGLLLN---NKTRILVTHQLQLLPHADQIVVLDNGR 204
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
 487-699 6.45e-37

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: 138.62  E-value: 6.45e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  487 VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLEslRRAVGVVPQDAVLF-HNTIYYN 565
Cdd:cd03299  14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFpHMTVYKN 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  566 LLYG------NISASPEEVYAVAKLAGLHDAILRMPhgydtqvgergLKLSGGEKQRVAIARAILKDPPVILYDEATSSL 639
Cdd:cd03299  92 IAYGlkkrkvDKKEIERKVLEIAEMLGIDHLLNRKP-----------ETLSGGEQQRVAIARALVVNPKILLLDEPFSAL 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 8928549  640 DSITEETILGAMKDVVKHR--TSIFIAHRLSTV-VDADEIIVLDQGKVAERGTHHGLLANPHS 699
Cdd:cd03299 161 DVRTKEKLREELKKIRKEFgvTVLHVTHDFEEAwALADKVAIMLNGKLIQVGKPEEVFKKPKN 223
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
 475-688 1.78e-36

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: 135.26  E-value: 1.78e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  475 DNVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQd 554
Cdd:cd03214   3 ENLSVGY-GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ- 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  555 avlfhntiyynllygnisaspeevyaVAKLAGLHDAILRmphGYDTqvgerglkLSGGEKQRVAIARAILKDPPVILYDE 634
Cdd:cd03214  81 --------------------------ALELLGLAHLADR---PFNE--------LSGGERQRVLLARALAQEPPILLLDE 123

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 8928549  635 ATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLSTVVD-ADEIIVLDQGKVAERG 688
Cdd:cd03214 124 PTSHLDIAHQIELLELLRRLARERgkTVVMVLHDLNLAARyADRVILLKDGRIVAQG 180
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
 468-703 1.98e-36

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 140.62  E-value: 1.98e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  468 QTATVAFDNVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLEslRRA 547
Cdd:COG3842   2 AMPALELENVSKRY-GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE--KRN 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  548 VGVVPQDAVLF-HNTIYYNLLYG---------NISASPEEVYAVAKLAGLHDailRMPHgydtqvgerglKLSGGEKQRV 617
Cdd:COG3842  79 VGMVFQDYALFpHLTVAENVAFGlrmrgvpkaEIRARVAELLELVGLEGLAD---RYPH-----------QLSGGQQQRV 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  618 AIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHR--TSIFIAHrlstvvD-------ADEIIVLDQGKVAERG 688
Cdd:COG3842 145 ALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELgiTFIYVTH------DqeealalADRIAVMNDGRIEQVG 218

                       250
                ....*....|....*
gi 8928549  689 ThhgllanPHSIYSE 703
Cdd:COG3842 219 T-------PEEIYER 226
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
 472-687 2.23e-36

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: 136.45  E-value: 2.23e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  472 VAFDNVHFEYIEGQ---KVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSleslrRAV 548
Cdd:cd03293   1 LEVRNVSKTYGGGGgavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG-----PDR 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  549 GVVPQDAVLF-HNTIYYNLLYG----NISASP--EEVYAVAKLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVAIAR 621
Cdd:cd03293  76 GYVFQQDALLpWLTVLDNVALGlelqGVPKAEarERAEELLELVGLSGFENAYPH-----------QLSGGMRQRVALAR 144

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 8928549  622 AILKDPPVILYDEATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLSTVVD-ADEIIVLDQ--GKVAER 687
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETgkTVLLVTHDIDEAVFlADRVVVLSArpGRIVAE 215
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
 472-684 2.48e-36

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: 136.12  E-value: 2.48e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  472 VAFDNVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNI--QDVSLESLRRAVG 549
Cdd:cd03262   1 IEIKNLHKSF-GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKVG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  550 VVPQDAVLF-HNTIYYNLLYGNISA---SPEEVYAVA----KLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVAIAR 621
Cdd:cd03262  80 MVFQQFNLFpHLTVLENITLAPIKVkgmSKAEAEERAlellEKVGLADKADAYPA-----------QLSGGQQQRVAIAR 148

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 8928549  622 AILKDPPVILYDEATSSLDSITEETILGAMKDVVK-HRTSIFIAHRLSTVVD-ADEIIVLDQGKV 684
Cdd:cd03262 149 ALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEeGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
 476-697 3.34e-36

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


Pssm-ID: 440213 [Multi-domain]  Cd Length: 320  Bit Score: 139.03  E-value: 3.34e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  476 NVHFEYIEGQ-KVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQ---KGSIYLAGQNIQDVSLESLR----RA 547
Cdd:COG0444   8 KVYFPTRRGVvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKLSEKELRkirgRE 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  548 VGVVPQD-----------------AVLFHNtiyynllygniSASPEEVYAVA----KLAGLHDAILRM---PHgydtQvg 603
Cdd:COG0444  88 IQMIFQDpmtslnpvmtvgdqiaePLRIHG-----------GLSKAEARERAiellERVGLPDPERRLdryPH----E-- 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  604 erglkLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVK-HRTS-IFIAHRLSTVVD-ADEIIVLD 680
Cdd:COG0444 151 -----LSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQReLGLAiLFITHDLGVVAEiADRVAVMY 225

                       250
                ....*....|....*..
gi 8928549  681 QGKVAERGTHHGLLANP 697
Cdd:COG0444 226 AGRIVEEGPVEELFENP 242
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
 475-689 5.39e-36

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


Pssm-ID: 440737 [Multi-domain]  Cd Length: 254  Bit Score: 136.33  E-value: 5.39e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  475 DNVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQ- 553
Cdd:COG1120   5 ENLSVGY-GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVPQe 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  554 ----------DAVLFHNTIYYNLLYGNISASPEEVYAVAKLAGLHDaiLRmphgyDTQVGErglkLSGGEKQRVAIARAI 623
Cdd:COG1120  84 ppapfgltvrELVALGRYPHLGLFGRPSAEDREAVEEALERTGLEH--LA-----DRPVDE----LSGGERQRVLIARAL 152

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 8928549  624 LKDPPVILYDEATSSLDSITEETILGAMKDVVKH--RTSIFIAHRLSTVVD-ADEIIVLDQGKVAERGT 689
Cdd:COG1120 153 AQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARErgRTVVMVLHDLNLAARyADRLVLLKDGRIVAQGP 221
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
 472-684 1.85e-35

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


Pssm-ID: 213259 [Multi-domain]  Cd Length: 214  Bit Score: 133.69  E-value: 1.85e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  472 VAFDNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDV---SLESLRRAV 548
Cdd:cd03292   1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLrgrAIPYLRRKI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  549 GVVPQDA-VLFHNTIYYNLLYGN--ISASPEE----VYAVAKLAGLHDAILRMPHGydtqvgerglkLSGGEKQRVAIAR 621
Cdd:cd03292  81 GVVFQDFrLLPDRNVYENVAFALevTGVPPREirkrVPAALELVGLSHKHRALPAE-----------LSGGEQQRVAIAR 149

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 8928549  622 AILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDA--DEIIVLDQGKV 684
Cdd:cd03292 150 AIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTtrHRVIALERGKL 214
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
 467-686 2.05e-35

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 134.45  E-value: 2.05e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  467 PQTATVAFDNVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVsleslRR 546
Cdd:COG1121   2 MMMPAIELENLTVSY-GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-----RR 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  547 AVGVVPQdavlfHNTIYYNL-----------LYGNISASP-------EEVYAVAKLAGLHDaiLRmphgyDTQVGErglk 608
Cdd:COG1121  76 RIGYVPQ-----RAEVDWDFpitvrdvvlmgRYGRRGLFRrpsradrEAVDEALERVGLED--LA-----DRPIGE---- 139

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  609 LSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKH-RTSIFIAHRLSTVVD-ADEIIVLDQGKVAE 686
Cdd:COG1121 140 LSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREgKTILVVTHDLGAVREyFDRVLLLNRGLVAH 219
PhnC COG3638
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ...
 472-684 2.85e-35

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


Pssm-ID: 442855 [Multi-domain]  Cd Length: 249  Bit Score: 134.03  E-value: 2.85e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  472 VAFDNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS---LESLRRAV 548
Cdd:COG3638   3 LELRNLSKRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRgraLRRLRRRI 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  549 GVVPQDavlfHN-----TIYYNLLYGNISA-----------SPEEV-YAVAKLA--GLHDAILRmphgydtqvgeRGLKL 609
Cdd:COG3638  83 GMIFQQ----FNlvprlSVLTNVLAGRLGRtstwrsllglfPPEDReRALEALErvGLADKAYQ-----------RADQL 147

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 8928549  610 SGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLSTVVD-ADEIIVLDQGKV 684
Cdd:COG3638 148 SGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDgiTVVVNLHQVDLARRyADRIIGLRDGRV 225
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
 484-684 2.94e-35

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: 131.37  E-value: 2.94e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  484 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDvSLESLRRAVGVVPQDAVLfhntiY 563
Cdd:cd03230  12 KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYLPEEPSL-----Y 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  564 YNLlygnisaSPEEVyavaklaglhdailrmphgydtqvgergLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSIT 643
Cdd:cd03230  86 ENL-------TVREN----------------------------LKLSGGMKQRLALAQALLHDPELLILDEPTSGLDPES 130

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 8928549  644 EETILGAMKDVVKHRTSIFIA-HRLSTVVD-ADEIIVLDQGKV 684
Cdd:cd03230 131 RREFWELLRELKKEGKTILLSsHILEEAERlCDRVAILNNGRI 173
ABC_membrane pfam00664
ABC transporter transmembrane region; This family represents a unit of six transmembrane ...
 140-424 3.08e-35

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


Pssm-ID: 459896 [Multi-domain]  Cd Length: 274  Bit Score: 135.08  E-value: 3.08e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    140 VAISLGFLGGAKAMNIVVPFMFKYAVDSLNQmsgnmlNLSDAPNTVATMATAVLIGYgvsrAGAAFFNEVRNAVFGKVAQ 219
Cdd:pfam00664   1 LILAILLAILSGAISPAFPLVLGRILDVLLP------DGDPETQALNVYSLALLLLG----LAQFILSFLQSYLLNHTGE 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    220 NSIRRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGISFVLSALVFNLLPIMFEVMLVSGVLYYKcGAQFALVTLG 299
Cdd:pfam00664  71 RLSRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYY-GWKLTLVLLA 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    300 TLGTYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNERYEAQRYDGFLKTYETASLKSTSTLAMLNF 379
Cdd:pfam00664 150 VLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFG 229

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 8928549    380 GQSAIFSVGLTAIMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPL 424
Cdd:pfam00664 230 ITQFIGYLSYALALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
472-699 1.21e-34

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 135.21  E-value: 1.21e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  472 VAFDNVHFEYIEGQK---VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS---LESLR 545
Cdd:COG1135   2 IELENLSKTFPTKGGpvtALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSereLRAAR 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  546 RAVGVVPQdavlfHntiyYNLL-----YGNIsASPEEVYAVAK---------------LAGLHDAilrmphgYDTQvger 605
Cdd:COG1135  82 RKIGMIFQ-----H----FNLLssrtvAENV-ALPLEIAGVPKaeirkrvaellelvgLSDKADA-------YPSQ---- 140

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  606 glkLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLSTVVD-ADEIIVLDQG 682
Cdd:COG1135 141 ---LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELglTIVLITHEMDVVRRiCDRVAVLENG 217

                       250
                ....*....|....*..
gi 8928549  683 KVAERGTHHGLLANPHS 699
Cdd:COG1135 218 RIVEQGPVLDVFANPQS 234
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
 472-702 4.33e-34

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 131.41  E-value: 4.33e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   472 VAFDNVHFEYIEGQK-VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGV 550
Cdd:PRK13648   8 IVFKNVSFQYQSDASfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   551 VPQ--DAVLFHNTIYYNLLYG--NISASPEEVYAVAKLAgLHDAILRMPHGYDTQvgerglKLSGGEKQRVAIARAILKD 626
Cdd:PRK13648  88 VFQnpDNQFVGSIVKYDVAFGleNHAVPYDEMHRRVSEA-LKQVDMLERADYEPN------ALSGGQKQRVAIAGVLALN 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 8928549   627 PPVILYDEATSSLDSITEETILGAMKDV--VKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGThhgllanPHSIYS 702
Cdd:PRK13648 161 PSVIILDEATSMLDPDARQNLLDLVRKVksEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGT-------PTEIFD 231
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
 491-697 4.64e-34

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


Pssm-ID: 131197 [Multi-domain]  Cd Length: 354  Bit Score: 133.70  E-value: 4.64e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    491 ISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQD----VSLESLRRAVGVVPQDAVLF-HNTIYYN 565
Cdd:TIGR02142  16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgIFLPPEKRRIGYVFQEARLFpHLSVRGN 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    566 LLYGNISASPEEVYAVaklaglHDAILRMpHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEE 645
Cdd:TIGR02142  96 LRYGMKRARPSERRIS------FERVIEL-LGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKY 168

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 8928549    646 TILGAMKDVVKHRT--SIFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGLLANP 697
Cdd:TIGR02142 169 EILPYLERLHAEFGipILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWASP 223
ABC_6TM_exporters cd07346
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ...
 140-441 7.12e-34

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


Pssm-ID: 349983 [Multi-domain]  Cd Length: 292  Bit Score: 131.52  E-value: 7.12e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  140 VAISLGFLGGAKAMNIVVPFMFKYAVDSLnqmsgnmlnLSDAPNTVATMATAVLIGYGVSRAGAAFFnevRNAVFGKVAQ 219
Cdd:cd07346   1 LLLALLLLLLATALGLALPLLTKLLIDDV---------IPAGDLSLLLWIALLLLLLALLRALLSYL---RRYLAARLGQ 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  220 NSIRRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGISFVLSALVFNLLPIMFEVMLVSGVLYYKcGAQFALVTLG 299
Cdd:cd07346  69 RVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYL-NWKLTLVALL 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  300 TLgtytAFTVAVTRW-----RTRFRIEMNKADNDAGNAAiDSLLNYETVKYFNNERYEAQRYDGFLKTYETASLKSTSTL 374
Cdd:cd07346 148 LL----PLYVLILRYfrrriRKASREVRESLAELSAFLQ-ESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLS 222

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 8928549  375 AMLNFGQSAIFSVGLTAIMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDM 441
Cdd:cd07346 223 ALFSPLIGLLTALGTALVLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASL 289
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
 474-689 3.56e-33

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


Pssm-ID: 213223 [Multi-domain]  Cd Length: 241  Bit Score: 128.07  E-value: 3.56e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  474 FDNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNI---QDVSLESLRRAVGV 550
Cdd:cd03256   3 VENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDInklKGKALRQLRRQIGM 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  551 VPQDavlfHN-----TIYYNLLYGNISASPeevyavaklagLHDAILRMPHGYDTQ--------VG------ERGLKLSG 611
Cdd:cd03256  83 IFQQ----FNlierlSVLENVLSGRLGRRS-----------TWRSLFGLFPKEEKQralaalerVGlldkayQRADQLSG 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  612 GEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLSTVVD-ADEIIVLDQGKVAERG 688
Cdd:cd03256 148 GQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEgiTVIVSLHQVDLAREyADRIVGLKDGRIVFDG 227


                .
gi 8928549  689 T 689
Cdd:cd03256 228 P 228
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
 466-686 3.82e-33

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


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 128.28  E-value: 3.82e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  466 TPQTATVAFDNVHFEYIEGQK---VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIqdvslE 542
Cdd:COG1116   2 SAAAPALELRGVSKRFPTGGGgvtALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPV-----T 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  543 SLRRAVGVVPQDAVLF-HNTIYYNLLYG--NISASPEEVYAVA----KLAGLHDAILRMPHgydtQvgerglkLSGGEKQ 615
Cdd:COG1116  77 GPGPDRGVVFQEPALLpWLTVLDNVALGleLRGVPKAERRERArellELVGLAGFEDAYPH----Q-------LSGGMRQ 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  616 RVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVK--HRTSIFIAH------RLstvvdADEIIVLDQ--GKVA 685
Cdd:COG1116 146 RVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQetGKTVLFVTHdvdeavFL-----ADRVVVLSArpGRIV 220


                .
gi 8928549  686 E 686
Cdd:COG1116 221 E 221
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
475-689 5.14e-33

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 128.59  E-value: 5.14e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   475 DNVHFEYIEGQK-VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQ 553
Cdd:PRK13635   9 EHISFRYPDAATyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGMVFQ 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   554 --DAVLFHNTIYYNLLYG--NISASPEE----VYAVAKLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARAILK 625
Cdd:PRK13635  89 npDNQFVGATVQDDVAFGleNIGVPREEmverVDQALRQVGMEDFLNREPH-----------RLSGGQKQRVAIAGVLAL 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 8928549   626 DPPVILYDEATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLSTVVDADEIIVLDQGKVAERGT 689
Cdd:PRK13635 158 QPDIIILDEATSMLDPRGRREVLETVRQLKEQKgiTVLSITHDLDEAAQADRVIVMNKGEILEEGT 223
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
 475-684 5.21e-33

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


Pssm-ID: 213193 [Multi-domain]  Cd Length: 205  Bit Score: 126.22  E-value: 5.21e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  475 DNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIqdvSLESLRRAVGVVPQD 554
Cdd:cd03226   3 ENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI---KAKERRKSIGYVMQD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  555 A--VLFHNTIYYNLLYGN--ISASPEEVYAVAKLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARAILKDPPVI 630
Cdd:cd03226  80 VdyQLFTDSVREELLLGLkeLDAGNEQAETVLKDLDLYALKERHPL-----------SLSGGQKQRLAIAAALLSGKDLL 148

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 8928549  631 LYDEATSSLDSITEETILGAMKDVVKHRTSIF-IAHR---LSTVvdADEIIVLDQGKV 684
Cdd:cd03226 149 IFDEPTSGLDYKNMERVGELIRELAAQGKAVIvITHDyefLAKV--CDRVLLLANGAI 204
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
 484-697 7.43e-33

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 127.56  E-value: 7.43e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   484 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNI--------QDVSLESLRRAVGVVPQDA 555
Cdd:PRK11264  15 GQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtarslsqQKGLIRQLRQHVGFVFQNF 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   556 VLF-HNTIYYNLLYGNISASPE----------EVYAVAKLAGLHDAILRmphgydtqvgerglKLSGGEKQRVAIARAIL 624
Cdd:PRK11264  95 NLFpHRTVLENIIEGPVIVKGEpkeeatararELLAKVGLAGKETSYPR--------------RLSGGQQQRVAIARALA 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 8928549   625 KDPPVILYDEATSSLDSITEETILGAMKDVVKH-RTSIFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGLLANP 697
Cdd:PRK11264 161 MRPEVILFDEPTSALDPELVGEVLNTIRQLAQEkRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFADP 235
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
 474-685 1.58e-32

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: 125.34  E-value: 1.58e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  474 FDNVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVsleslRRAVGVVPQ 553
Cdd:cd03235   2 VEDLTVSY-GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGYVPQ 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  554 -------------DAVLFHNTIYYNLLYGNISASPEEVYAVAKLAGLHDAILRmphgydtQVGErglkLSGGEKQRVAIA 620
Cdd:cd03235  76 rrsidrdfpisvrDVVLMGLYGHKGLFRRLSKADKAKVDEALERVGLSELADR-------QIGE----LSGGQQQRVLLA 144

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 8928549  621 RAILKDPPVILYDEATSSLDSITEETILGAMKDVVKH-RTSIFIAHRLSTVVD-ADEIIVLDQGKVA 685
Cdd:cd03235 145 RALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREgMTILVVTHDLGLVLEyFDRVLLLNRTVVA 211
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
 472-703 1.72e-32

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


Pssm-ID: 213267 [Multi-domain]  Cd Length: 232  Bit Score: 125.81  E-value: 1.72e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  472 VAFDNVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDvsLESLRRAVGVV 551
Cdd:cd03300   1 IELENVSKFY-GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITN--LPPHKRPVNTV 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  552 PQDAVLF-HNTIYYNLLYG------NISASPEEVYAVAKLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARAIL 624
Cdd:cd03300  78 FQNYALFpHLTVFENIAFGlrlkklPKAEIKERVAEALDLVQLEGYANRKPS-----------QLSGGQQQRVAIARALV 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  625 KDPPVILYDEATSSLDSITEETILGAMKDVvkHR----TSIFIAHRLS-TVVDADEIIVLDQGKVAERGThhgllanPHS 699
Cdd:cd03300 147 NEPKVLLLDEPLGALDLKLRKDMQLELKRL--QKelgiTFVFVTHDQEeALTMSDRIAVMNKGKIQQIGT-------PEE 217


                ....
gi 8928549  700 IYSE 703
Cdd:cd03300 218 IYEE 221
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
 491-701 2.11e-32

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: 126.60  E-value: 2.11e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  491 ISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESL----RRAVGVVPQDAVLF-HNTIYYN 565
Cdd:cd03294  43 VSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLpHRTVLEN 122

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  566 LLYG-NISASPEEV-YAVA----KLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARAILKDPPVILYDEATSSL 639
Cdd:cd03294 123 VAFGlEVQGVPRAErEERAaealELVGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMDEAFSAL 191

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 8928549  640 DSiteeTILGAMKDVV------KHRTSIFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGLLANPHSIY 701
Cdd:cd03294 192 DP----LIRREMQDELlrlqaeLQKTIVFITHDLDEALRlGDRIAIMKDGRLVQVGTPEEILTNPANDY 256
cbiO PRK13637
energy-coupling factor transporter ATPase;
475-689 6.25e-32

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 125.93  E-value: 6.25e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   475 DNVHFEYIEG----QKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQD--VSLESLRRAV 548
Cdd:PRK13637   6 ENLTHIYMEGtpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDkkVKLSDIRKKV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   549 GVVPQ--DAVLFHNTIYYNLLYG--NISASPEE----VYAVAKLAGLHdailrmphgYDTQVGERGLKLSGGEKQRVAIA 620
Cdd:PRK13637  86 GLVFQypEYQLFEETIEKDIAFGpiNLGLSEEEienrVKRAMNIVGLD---------YEDYKDKSPFELSGGQKRRVAIA 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 8928549   621 RAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLSTVVD-ADEIIVLDQGKVAERGT 689
Cdd:PRK13637 157 GVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYnmTIILVSHSMEDVAKlADRIIVMNKGKCELQGT 228
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
 486-701 1.39e-31

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


Pssm-ID: 443332 [Multi-domain]  Cd Length: 533  Bit Score: 129.80  E-value: 1.39e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  486 KVLSGISFEVPAGKKVAIVGGSGSGKST----IVRLLfrfyePQKGSIYLAGQNIQDVS---LESLRRAVGVVPQD---- 554
Cdd:COG4172 300 KAVDGVSLTLRRGETLGLVGESGSGKSTlglaLLRLI-----PSEGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDpfgs 374

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  555 ---------------AVLFhntiyynllygnISASPEEVYA-VAKL---AGLH-DAILRMPHgydtqvgerglKLSGGEK 614
Cdd:COG4172 375 lsprmtvgqiiaeglRVHG------------PGLSAAERRArVAEAleeVGLDpAARHRYPH-----------EFSGGQR 431

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  615 QRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLStVVDA--DEIIVLDQGKVAERGTH 690
Cdd:COG4172 432 QRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHglAYLFISHDLA-VVRAlaHRVMVMKDGKVVEQGPT 510

                       250
                ....*....|.
gi 8928549  691 HGLLANPHSIY 701
Cdd:COG4172 511 EQVFDAPQHPY 521
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
 491-688 1.70e-31

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: 122.40  E-value: 1.70e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  491 ISFEVPAGKkVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQD----VSLESLRRAVGVVPQDAVLF-HNTIYYN 565
Cdd:cd03297  17 IDFDLNEEV-TGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDsrkkINLPPQQRKIGLVFQQYALFpHLNVREN 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  566 LLYGNISASPEE----VYAVAKLAGLhdailrmphgydTQVGERG-LKLSGGEKQRVAIARAILKDPPVILYDEATSSLD 640
Cdd:cd03297  96 LAFGLKRKRNREdrisVDELLDLLGL------------DHLLNRYpAQLSGGEKQRVALARALAAQPELLLLDEPFSALD 163

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 8928549  641 SITEETILGAMKDVVK--HRTSIFIAHRLSTVVD-ADEIIVLDQGKVAERG 688
Cdd:cd03297 164 RALRLQLLPELKQIKKnlNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
 486-703 2.20e-31

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


Pssm-ID: 443658 [Multi-domain]  Cd Length: 329  Bit Score: 125.23  E-value: 2.20e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  486 KVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS---LESLRRAVGVVPQD--AVLfhN 560
Cdd:COG4608  32 KAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSgreLRPLRRRMQMVFQDpyASL--N 109

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  561 ---TIyynllyGNISASPEEVYAVAKLAGLHDAILRM--------------PHgydtqvgerglKLSGGEKQRVAIARAI 623
Cdd:COG4608 110 prmTV------GDIIAEPLRIHGLASKAERRERVAELlelvglrpehadryPH-----------EFSGGQRQRIGIARAL 172

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  624 LKDPPVILYDEATSSLD-SItEETILGAMKDVVKHR--TSIFIAHRLStVVD--ADEIIVLDQGKVAERGTHHGLLANPH 698
Cdd:COG4608 173 ALNPKLIVCDEPVSALDvSI-QAQVLNLLEDLQDELglTYLFISHDLS-VVRhiSDRVAVMYLGKIVEIAPRDELYARPL 250


                ....*
gi 8928549  699 SIYSE 703
Cdd:COG4608 251 HPYTQ 255
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
 486-701 2.71e-31

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


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 125.64  E-value: 2.71e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  486 KVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIqDVSLESLRRAVGVVPQDAVLF-HNTIYY 564
Cdd:COG1118  16 TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDL-FTNLPPRERRVGFVFQHYALFpHMTVAE 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  565 NLLYG--NISASPEEVYAVA-------KLAGLHDailRMPHgydtqvgerglKLSGGEKQRVAIARAILKDPPVILYDEA 635
Cdd:COG1118  95 NIAFGlrVRPPSKAEIRARVeellelvQLEGLAD---RYPS-----------QLSGGQRQRVALARALAVEPEVLLLDEP 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 8928549  636 TSSLDSITEETILGAMKDVVK--HRTSIFIAH------RLstvvdADEIIVLDQGKVAERGTHHGLLANPHSIY 701
Cdd:COG1118 161 FGALDAKVRKELRRWLRRLHDelGGTTVFVTHdqeealEL-----ADRVVVMNQGRIEQVGTPDEVYDRPATPF 229
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
 459-648 4.26e-31

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


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 122.45  E-value: 4.26e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  459 MASPLQITPQTATVafDNVHFEYieGQK-VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYE--PQ---KGSIYLA 532
Cdd:COG1117   1 MTAPASTLEPKIEV--RNLNVYY--GDKqALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPGarvEGEILLD 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  533 GQNI--QDVSLESLRRAVGVVPQDAVLFHNTIYYNLLYGnisaspeevyavAKLAGLH-----DAI----LRmphgydtQ 601
Cdd:COG1117  77 GEDIydPDVDVVELRRRVGMVFQKPNPFPKSIYDNVAYG------------LRLHGIKskselDEIveesLR-------K 137

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 8928549  602 VG----------ERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSIT----EETIL 648
Cdd:COG1117 138 AAlwdevkdrlkKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPIStakiEELIL 198
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
 474-699 7.76e-31

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 124.14  E-value: 7.76e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   474 FDNVHFEYIEGQK---VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS---LESLRRA 547
Cdd:PRK11153   4 LKNISKVFPQGGRtihALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSekeLRKARRQ 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   548 VGVVPQdavlfHntiyYNLL-----YGNIsASPEEVYAVAK------------LAGL---HDAilrmphgYDTQvgergl 607
Cdd:PRK11153  84 IGMIFQ-----H----FNLLssrtvFDNV-ALPLELAGTPKaeikarvtelleLVGLsdkADR-------YPAQ------ 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   608 kLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVK--HRTSIFIAHRLStVVD--ADEIIVLDQGK 683
Cdd:PRK11153 141 -LSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRelGLTIVLITHEMD-VVKriCDRVAVIDAGR 218

                        250
                 ....*....|....*.
gi 8928549   684 VAERGTHHGLLANPHS 699
Cdd:PRK11153 219 LVEQGTVSEVFSHPKH 234
ABCC_SUR2 cd03288
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...
 487-702 1.92e-30

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


Pssm-ID: 213255 [Multi-domain]  Cd Length: 257  Bit Score: 120.78  E-value: 1.92e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  487 VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNL 566
Cdd:cd03288  36 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL 115

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  567 lYGNISASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEET 646
Cdd:cd03288 116 -DPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENI 194

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 8928549  647 ILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLLANPHSIYS 702
Cdd:cd03288 195 LQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVFA 250
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
 470-688 2.17e-30

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: 118.42  E-value: 2.17e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  470 ATVAFDNV-----HFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLL--FRFYEPQKGSIYLAGQNIqdvSLE 542
Cdd:cd03213   2 VTLSFRNLtvtvkSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPL---DKR 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  543 SLRRAVGVVPQDAVLF-HNTIYYNLLYgnisaspeevyaVAKLAGLhdailrmphgydtqvgerglklSGGEKQRVAIAR 621
Cdd:cd03213  79 SFRKIIGYVPQDDILHpTLTVRETLMF------------AAKLRGL----------------------SGGERKRVSIAL 124

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  622 AILKDPPVILYDEATSSLDSITEETILGAMKDVVK-HRTSIFIAHRLSTVV--DADEIIVLDQGKVAERG 688
Cdd:cd03213 125 ELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADtGRTIICSIHQPSSEIfeLFDKLLLLSQGRVIYFG 194
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
 475-696 5.12e-30

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


Pssm-ID: 213191 [Multi-domain]  Cd Length: 222  Bit Score: 118.31  E-value: 5.12e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  475 DNVHFEYIEGQkVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLES-LRRAVGVVPQ 553
Cdd:cd03224   4 ENLNAGYGKSQ-ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIGYVPE 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  554 DAVLFHN-TIYYNLLYG-------NISASPEEVYAV--------AKLAGLhdailrmphgydtqvgerglkLSGGEKQRV 617
Cdd:cd03224  83 GRRIFPElTVEENLLLGayarrraKRKARLERVYELfprlkerrKQLAGT---------------------LSGGEQQML 141

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  618 AIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFI----AHRLSTVvdADEIIVLDQGKVAERGTHHGL 693
Cdd:cd03224 142 AIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLveqnARFALEI--ADRAYVLERGRVVLEGTAAEL 219


                ...
gi 8928549  694 LAN 696
Cdd:cd03224 220 LAD 222
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
 420-730 1.09e-29

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


Pssm-ID: 188098 [Multi-domain]  Cd Length: 1522  Bit Score: 126.98  E-value: 1.09e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549     420 LSLPLNFLGTVYRETRQALIDMNTLFTLLKVDTQIKDKVMASPLQITPQTAtVAFDNVHFEYIEGQK-VLSGISFEVPAG 498
Cdd:TIGR00957  586 LRFPLNILPMVISSIVQASVSLKRLRIFLSHEELEPDSIERRTIKPGEGNS-ITVHNATFTWARDLPpTLNGITFSIPEG 664

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549     499 KKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGqniqdvsleslrrAVGVVPQDAVLFHNTIYYNLLYGNiSASPEEV 578
Cdd:TIGR00957  665 ALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-------------SVAYVPQQAWIQNDSLRENILFGK-ALNEKYY 730

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549     579 YAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITE----ETILGAMkDV 654
Cdd:TIGR00957  731 QQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGkhifEHVIGPE-GV 809

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 8928549     655 VKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLLANPHSIYSEMWHTQSSRVQNHDNPKWEAKKENISKE 730
Cdd:TIGR00957  810 LKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFLRTYAPDEQQGHLEDSWTALVSGEGKE 885
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
 476-738 1.55e-29

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: 118.42  E-value: 1.55e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  476 NVHFEYIE-GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQkGSIYLAGQNIQDVSLESLRRAVGVVPQD 554
Cdd:cd03289   7 DLTAKYTEgGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAFGVIPQK 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  555 AVLFHNTIYYNL-LYGniSASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYD 633
Cdd:cd03289  86 VFIFSGTFRKNLdPYG--KWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLD 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  634 EATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLLANPHSIYSEMWHTQSSRV- 712
Cdd:cd03289 164 EPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQAISPSDRLKLf 243

                       250       260
                ....*....|....*....|....*....
gi 8928549  713 -QNHDNPKWEAKKENIS--KEEERKKLQE 738
Cdd:cd03289 244 pRRNSSKSKRKPRPQIQalQEETEEEVQD 272
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
 470-689 1.67e-29

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


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 120.56  E-value: 1.67e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  470 ATVAFDNVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLEslRRAVG 549
Cdd:COG3839   2 ASLELENVSKSY-GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPK--DRNIA 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  550 VVPQDAVLF-HNTIYYNLLYG--NISASPEE----VYAVAKLAGLhDAIL-RMPhgydtqvgergLKLSGGEKQRVAIAR 621
Cdd:COG3839  79 MVFQSYALYpHMTVYENIAFPlkLRKVPKAEidrrVREAAELLGL-EDLLdRKP-----------KQLSGGQRQRVALGR 146

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 8928549  622 AILKDPPVILYDEATSSLDSITEETILGAMKDVvkHR----TSIFIAHrlstvvD-------ADEIIVLDQGKVAERGT 689
Cdd:COG3839 147 ALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRL--HRrlgtTTIYVTH------DqveamtlADRIAVMNDGRIQQVGT 217
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
472-699 2.73e-29

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 116.73  E-value: 2.73e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   472 VAFDNV--HFeyieGQ-KVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQD--VSLESLRR 546
Cdd:PRK09493   2 IEFKNVskHF----GPtQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDpkVDERLIRQ 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   547 AVGVVPQDAVLF-HNTIYYNLLYGNI---SASPEEVYAVAK--LA--GLHDailRMPHgYDTQvgerglkLSGGEKQRVA 618
Cdd:PRK09493  78 EAGMVFQQFYLFpHLTALENVMFGPLrvrGASKEEAEKQARelLAkvGLAE---RAHH-YPSE-------LSGGQQQRVA 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   619 IARAILKDPPVILYDEATSSLDSITEETILGAMKD---------VVKHRtsIFIAHRLSTvvdadEIIVLDQGKVAERGT 689
Cdd:PRK09493 147 IARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDlaeegmtmvIVTHE--IGFAEKVAS-----RLIFIDKGRIAEDGD 219

                        250
                 ....*....|
gi 8928549   690 HHGLLANPHS 699
Cdd:PRK09493 220 PQVLIKNPPS 229
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
 491-697 3.88e-29

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


Pssm-ID: 443319 [Multi-domain]  Cd Length: 358  Bit Score: 119.44  E-value: 3.88e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  491 ISFEVPAGKKVAIVGGSGSGKSTIVRL---LFRfyePQKGSIYLAGQNIQD----VSLESLRRAVGVVPQDAVLF-HNTI 562
Cdd:COG4148  18 VDFTLPGRGVTALFGPSGSGKTTLLRAiagLER---PDSGRIRLGGEVLQDsargIFLPPHRRRIGYVFQEARLFpHLSV 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  563 YYNLLYG----NISASPEEVYAVAKLAGLhDAIL-RMPHgydtqvgerglKLSGGEKQRVAIARAILKDPPVILYDEATS 637
Cdd:COG4148  95 RGNLLYGrkraPRAERRISFDEVVELLGI-GHLLdRRPA-----------TLSGGERQRVAIGRALLSSPRLLLMDEPLA 162

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 8928549  638 SLDSITEETILGAMKDvVKHRTSI---FIAH------RLstvvdADEIIVLDQGKVAERGTHHGLLANP 697
Cdd:COG4148 163 ALDLARKAEILPYLER-LRDELDIpilYVSHsldevaRL-----ADHVVLLEQGRVVASGPLAEVLSRP 225
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
 488-699 7.40e-29

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: 115.51  E-value: 7.40e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  488 LSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLEslRRAVGVVPQDAVLF-HNTIYYNL 566
Cdd:cd03296  18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVGFVFQHYALFrHMTVFDNV 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  567 LYG-------------NISASPEEVYAVAKLAGLHDailRMPHgydtqvgerglKLSGGEKQRVAIARAILKDPPVILYD 633
Cdd:cd03296  96 AFGlrvkprserppeaEIRAKVHELLKLVQLDWLAD---RYPA-----------QLSGGQRQRVALARALAVEPKVLLLD 161

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  634 EATSSLDS-ITEE--TILGAMKDVVkHRTSIFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGLLANPHS 699
Cdd:cd03296 162 EPFGALDAkVRKElrRWLRRLHDEL-HVTTVFVTHDQEEALEvADRVVVMNKGRIEQVGTPDEVYDHPAS 230
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
 486-697 8.43e-29

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 117.76  E-value: 8.43e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   486 KVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLE---SLRRAVGVVpqdavlFHNTi 562
Cdd:PRK11308  29 KALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEaqkLLRQKIQIV------FQNP- 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   563 yYNLL-----YGNISASP-------------EEVYAVAKLAGL---HDAilRMPHGYdtqvgerglklSGGEKQRVAIAR 621
Cdd:PRK11308 102 -YGSLnprkkVGQILEEPllintslsaaerrEKALAMMAKVGLrpeHYD--RYPHMF-----------SGGQRQRIAIAR 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   622 AILKDPPVILYDEATSSLDSITEETILGAMKDVVKH-RTS-IFIAHRLStVVD--ADEIIVLDQGKVAERGTHHGLLANP 697
Cdd:PRK11308 168 ALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQElGLSyVFISHDLS-VVEhiADEVMVMYLGRCVEKGTKEQIFNNP 246
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
 475-697 8.94e-29

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 116.37  E-value: 8.94e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   475 DNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQD 554
Cdd:PRK13647   8 EDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQD 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   555 A--VLFHNTIYYNLLYG--NISASPEE----VYAVAKLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARAILKD 626
Cdd:PRK13647  88 PddQVFSSTVWDDVAFGpvNMGLDKDEverrVEEALKAVRMWDFRDKPPY-----------HLSYGQKKRVAIAGVLAMD 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 8928549   627 PPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIA-HRLSTVVD-ADEIIVLDQGKVAERGTHHgLLANP 697
Cdd:PRK13647 157 PDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDLAAEwADQVIVLKEGRVLAEGDKS-LLTDE 228
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
 484-685 9.95e-29

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


Pssm-ID: 213183 [Multi-domain]  Cd Length: 163  Bit Score: 112.52  E-value: 9.95e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  484 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS-LESLRRAVGVVPQdavlfhnti 562
Cdd:cd03216  12 GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASpRDARRAGIAMVYQ--------- 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  563 yynllygnisaspeevyavaklaglhdailrmphgydtqvgerglkLSGGEKQRVAIARAILKDPPVILYDEATSSLDSI 642
Cdd:cd03216  83 ----------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPA 116

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 8928549  643 TEETILGAMKDVVKH-RTSIFIAHRLSTVVD-ADEIIVLDQGKVA 685
Cdd:cd03216 117 EVERLFKVIRRLRAQgVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
 495-688 1.04e-28

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: 114.13  E-value: 1.04e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  495 VPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIqdVSLESLRRAVGVVPQDAVLF-HNTIYYNLLYG---N 570
Cdd:cd03298  21 FAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDV--TAAPPADRPVSMLFQENNLFaHLTVEQNVGLGlspG 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  571 ISASPEEVYAVAKLA---GLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETI 647
Cdd:cd03298  99 LKLTAEDRQAIEVALarvGLAGLEKRLPG-----------ELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEM 167

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 8928549  648 LGAMKDVVKHR--TSIFIAHRLSTVVD-ADEIIVLDQGKVAERG 688
Cdd:cd03298 168 LDLVLDLHAETkmTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
474-697 2.60e-28

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 113.70  E-value: 2.60e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  474 FDNVHFEYieGQKVLSgISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIqdVSLESLRRAVGVVPQ 553
Cdd:COG3840   4 LDDLTYRY--GDFPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDL--TALPPAERPVSMLFQ 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  554 DAVLF-HNTIYYNLLYG---NISASPEEVYAVAKLA---GLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARAILKD 626
Cdd:COG3840  79 ENNLFpHLTVAQNIGLGlrpGLKLTAEQRAQVEQALervGLAGLLDRLPG-----------QLSGGQRQRVALARCLVRK 147

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 8928549  627 PPVILYDEATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGLLANP 697
Cdd:COG3840 148 RPILLLDEPFSALDPALRQEMLDLVDELCRERglTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDGE 221
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
 472-688 3.79e-28

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


Pssm-ID: 213268 [Multi-domain]  Cd Length: 213  Bit Score: 112.73  E-value: 3.79e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  472 VAFDNVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVslESLRRAVGVV 551
Cdd:cd03301   1 VELENVTKRF-GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDL--PPKDRDIAMV 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  552 PQDAVLF-HNTIYYNLLYG-NISASPEE-----VYAVAKLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARAIL 624
Cdd:cd03301  78 FQNYALYpHMTVYDNIAFGlKLRKVPKDeiderVREVAELLQIEHLLDRKPK-----------QLSGGQRQRVALGRAIV 146

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 8928549  625 KDPPVILYDEATSSLDSITEETILGAMKDVVKH--RTSIFIAH-RLSTVVDADEIIVLDQGKVAERG 688
Cdd:cd03301 147 REPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRlgTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
PLN03232 PLN03232
ABC transporter C family member; Provisional
 332-696 5.96e-28

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 121.24  E-value: 5.96e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    332 AAIDSLLNYETVKYFNNeRYEAQRYDGfLKTYETASLKSTSTLAMLNfgqsaifsvGLTAIMVLASQGIVagTLTVGDLV 411
Cdd:PLN03232  487 ASMDTVKCYAWEKSFES-RIQGIRNEE-LSWFRKAQLLSAFNSFILN---------SIPVVVTLVSFGVF--VLLGGDLT 553

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    412 MVNGL----LFQ-LSLPLNFLGTVYRETRQALIDMNTLFTLLKVDtqikDKVMASPLQITPQTATVAFDNVHFEYIE--G 484
Cdd:PLN03232  554 PARAFtslsLFAvLRSPLNMLPNLLSQVVNANVSLQRIEELLLSE----ERILAQNPPLQPGAPAISIKNGYFSWDSktS 629

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    485 QKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPqkgsiylagqnIQDVSLEsLRRAVGVVPQDAVLFHNTIYY 564
Cdd:PLN03232  630 KPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSH-----------AETSSVV-IRGSVAYVPQVSWIFNATVRE 697

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    565 NLLYGNISASPEEVYAVAKLAGLHDaiLRMPHGYD-TQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDS-I 642
Cdd:PLN03232  698 NILFGSDFESERYWRAIDVTALQHD--LDLLPGRDlTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAhV 775

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 8928549    643 TEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLLAN 696
Cdd:PLN03232  776 AHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKS 829
PLN03130 PLN03130
ABC transporter C family member; Provisional
 382-696 6.58e-28

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 121.00  E-value: 6.58e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    382 SAIFSVGLTAIMVLA---SQGIVagTLTVGDLVMVNGL----LFQ-LSLPLNFLGTVYRETRQALIDMNTLFTLLKVDtq 453
Cdd:PLN03130  523 SAFNSFILNSIPVLVtvvSFGVF--TLLGGDLTPARAFtslsLFAvLRFPLFMLPNLITQAVNANVSLKRLEELLLAE-- 598

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    454 ikDKVMASPLQITPQTATVAFDNVHFEY-IEGQK-VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYL 531
Cdd:PLN03130  599 --ERVLLPNPPLEPGLPAISIKNGYFSWdSKAERpTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV 676

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    532 agqniqdvslesLRRAVGVVPQDAVLFHNTIYYNLLYGNiSASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSG 611
Cdd:PLN03130  677 ------------IRGTVAYVPQVSWIFNATVRDNILFGS-PFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISG 743

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    612 GEKQRVAIARAILKDPPVILYDEATSSLDS-ITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTH 690
Cdd:PLN03130  744 GQKQRVSMARAVYSNSDVYIFDDPLSALDAhVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTY 823


                  ....*.
gi 8928549    691 HGLLAN 696
Cdd:PLN03130  824 EELSNN 829
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
 334-738 7.03e-27

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: 117.70  E-value: 7.03e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549     334 IDSLLNYETVKYFNNERYEAQRYDGFLKTYETASLKSTSTLAMLNFGQSAIFSVGLTAIMVLA------SQGIVAGTLTV 407
Cdd:TIGR01271 1068 ITSLKGLWTIRAFGRQSYFETLFHKALNLHTANWFLYLSTLRWFQMRIDIIFVFFFIAVTFIAigtnqdGEGEVGIILTL 1147

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549     408 GDLVM------------VNGLLFQLSLPLNFLGTVYRETR-QALIDMNTLFTLLKVDTQIKDKVMASPLQITPQTATVAF 474
Cdd:TIGR01271 1148 AMNILstlqwavnssidVDGLMRSVSRVFKFIDLPQEEPRpSGGGGKYQLSTVLVIENPHAQKCWPSGGQMDVQGLTAKY 1227

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549     475 DNvhfeyiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQkGSIYLAGQNIQDVSLESLRRAVGVVPQD 554
Cdd:TIGR01271 1228 TE------AGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTLQTWRKAFGVIPQK 1300

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549     555 AVLFHNTIYYNLlYGNISASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDE 634
Cdd:TIGR01271 1301 VFIFSGTFRKNL-DPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDE 1379

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549     635 ATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLLaNPHSIYSEMWhTQSSRVQ- 713
Cdd:TIGR01271 1380 PSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLL-NETSLFKQAM-SAADRLKl 1457

                          410       420       430
                   ....*....|....*....|....*....|
gi 8928549     714 ---NHDNPKWEAKKENIS--KEEERKKLQE 738
Cdd:TIGR01271 1458 fplHRRNSSKRKPQPKITalREEAEEEVQN 1487
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
455-703 9.40e-27

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 112.73  E-value: 9.40e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   455 KDKVMASPLQITPqtaTVAFDNVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQ 534
Cdd:PRK09452   1 SKKLNKQPSSLSP---LVELRGISKSF-DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQ 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   535 NIQDVSLEslRRAVGVVPQDAVLF-HNTIYYNLLYG---------NISASPEEVYAVAKLAGLHDailRMPHgydtqvge 604
Cdd:PRK09452  77 DITHVPAE--NRHVNTVFQSYALFpHMTVFENVAFGlrmqktpaaEITPRVMEALRMVQLEEFAQ---RKPH-------- 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   605 rglKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSiteeTILGAMKDVVKH--R----TSIFIAH----RLSTvvdAD 674
Cdd:PRK09452 144 ---QLSGGQQQRVAIARAVVNKPKVLLLDESLSALDY----KLRKQMQNELKAlqRklgiTFVFVTHdqeeALTM---SD 213

                        250       260
                 ....*....|....*....|....*....
gi 8928549   675 EIIVLDQGKVAERGThhgllanPHSIYSE 703
Cdd:PRK09452 214 RIVVMRDGRIEQDGT-------PREIYEE 235
cbiO PRK13644
energy-coupling factor transporter ATPase;
472-697 1.31e-26

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 110.08  E-value: 1.31e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   472 VAFDNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS-LESLRRAVGV 550
Cdd:PRK13644   2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVGI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   551 VPQ--DAVLFHNTIYYNLLYG--NISASPEEVYAVAKLA----GLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARA 622
Cdd:PRK13644  82 VFQnpETQFVGRTVEEDLAFGpeNLCLPPIEIRKRVDRAlaeiGLEKYRHRSPK-----------TLSGGQGQCVALAGI 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 8928549   623 ILKDPPVILYDEATSSLDSITEETILGAMKDV-VKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLLANP 697
Cdd:PRK13644 151 LTMEPECLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDV 226
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
 487-698 1.76e-26

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


Pssm-ID: 440179 [Multi-domain]  Cd Length: 236  Bit Score: 108.53  E-value: 1.76e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  487 VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESL-RRAVGVVPQDAVLFHN-TIYY 564
Cdd:COG0410  18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIaRLGIGYVPEGRRIFPSlTVEE 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  565 NLLYG--------NISASPEEVYAV--------AKLAGLhdailrmphgydtqvgerglkLSGGEKQRVAIARAILKDPP 628
Cdd:COG0410  98 NLLLGayarrdraEVRADLERVYELfprlkerrRQRAGT---------------------LSGGEQQMLAIGRALMSRPK 156

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 8928549  629 VILYDEATSSLD-SITEEtILGAMKDVVKHRTSIFI----AHRLSTVvdADEIIVLDQGKVAERGTHHGLLANPH 698
Cdd:COG0410 157 LLLLDEPSLGLApLIVEE-IFEIIRRLNREGVTILLveqnARFALEI--ADRAYVLERGRIVLEGTAAELLADPE 228
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
476-699 2.31e-26

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 108.90  E-value: 2.31e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   476 NVHFEYIEgQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDV-------------SLE 542
Cdd:PRK10619  10 DLHKRYGE-HEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlkvadknQLR 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   543 SLRRAVGVVPQDAVLF-HNTIYYNLLygnisASPEEVYAVAKLAGLHDAILRMPH-GYDTQV-GERGLKLSGGEKQRVAI 619
Cdd:PRK10619  89 LLRTRLTMVFQHFNLWsHMTVLENVM-----EAPIQVLGLSKQEARERAVKYLAKvGIDERAqGKYPVHLSGGQQQRVSI 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   620 ARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKH-RTSIFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGLLANP 697
Cdd:PRK10619 164 ARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEgKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLFGNP 243


                 ..
gi 8928549   698 HS 699
Cdd:PRK10619 244 QS 245
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
475-703 2.38e-26

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 109.41  E-value: 2.38e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   475 DNVHFEYIEGQK-----VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS-LESLRRAV 548
Cdd:PRK13633   8 KNVSYKYESNEEsteklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnLWDIRNKA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   549 GVVPQ--DAVLFHNTIYYNLLYG--NISASPEEV-----YAVAKLaGLHDAILRMPHgydtqvgerglKLSGGEKQRVAI 619
Cdd:PRK13633  88 GMVFQnpDNQIVATIVEEDVAFGpeNLGIPPEEIrervdESLKKV-GMYEYRRHAPH-----------LLSGGQKQRVAI 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   620 ARAILKDPPVILYDEATSSLDSITEETILGAMKDVVK--HRTSIFIAHRLSTVVDADEIIVLDQGKVAERGThhgllanP 697
Cdd:PRK13633 156 AGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKkyGITIILITHYMEEAVEADRIIVMDSGKVVMEGT-------P 228


                 ....*.
gi 8928549   698 HSIYSE 703
Cdd:PRK13633 229 KEIFKE 234
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
 471-704 3.48e-26

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


Pssm-ID: 443332 [Multi-domain]  Cd Length: 533  Bit Score: 113.63  E-value: 3.48e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  471 TVAFDNVHFEyiegQKVLSGISFEVPAGKKVAIVGGSGSGKS----TIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRR 546
Cdd:COG4172  13 SVAFGQGGGT----VEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRR 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  547 ----AVGVVPQDA----------------VLfhntiyynLLYGNISASPEEVYAVAKLA--GLHDAILRM---PHgydtq 601
Cdd:COG4172  89 irgnRIAMIFQEPmtslnplhtigkqiaeVL--------RLHRGLSGAAARARALELLErvGIPDPERRLdayPH----- 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  602 vgerglKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVK-HRTSI-FIAHRLSTVVD-ADEIIV 678
Cdd:COG4172 156 ------QLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQReLGMALlLITHDLGVVRRfADRVAV 229

                       250       260
                ....*....|....*....|....*.
gi 8928549  679 LDQGKVAERGTHHGLLANPHSIYSEM 704
Cdd:COG4172 230 MRQGEIVEQGPTAELFAAPQHPYTRK 255
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
 467-651 3.52e-26

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


Pssm-ID: 443338 [Multi-domain]  Cd Length: 233  Bit Score: 107.52  E-value: 3.52e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  467 PQTATVAFDNVHFEYIEGQK---VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLES 543
Cdd:COG4181   4 SSAPIIELRGLTKTVGTGAGeltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDA 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  544 L----RRAVGVVPQDavlFHntiyynlLYGNISASpEEVYAVAKLAGLHDA------IL-------RMPHgYDTQvgerg 606
Cdd:COG4181  84 RarlrARHVGFVFQS---FQ-------LLPTLTAL-ENVMLPLELAGRRDArararaLLervglghRLDH-YPAQ----- 146

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 8928549  607 lkLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAM 651
Cdd:COG4181 147 --LSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLL 189
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
 475-688 4.57e-26

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


Pssm-ID: 213231 [Multi-domain]  Cd Length: 211  Bit Score: 106.51  E-value: 4.57e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  475 DNVHFEYiEGQKVLSGISFEVPAGKkVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDvSLESLRRAVGVVPQD 554
Cdd:cd03264   4 ENLTKRY-GKKRALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGYLPQE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  555 AVLFHN-TIYYNLLY----GNISAS--PEEVYAVAKLAGLHDAilrmphgYDTQVGerglKLSGGEKQRVAIARAILKDP 627
Cdd:cd03264  81 FGVYPNfTVREFLDYiawlKGIPSKevKARVDEVLELVNLGDR-------AKKKIG----SLSGGMRRRVGIAQALVGDP 149

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 8928549  628 PVILYDEATSSLDSitEETI--LGAMKDVVKHRTSIFIAHRLSTVVD-ADEIIVLDQGKVAERG 688
Cdd:cd03264 150 SILIVDEPTAGLDP--EERIrfRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
 484-683 5.12e-26

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


Pssm-ID: 443308 [Multi-domain]  Cd Length: 206  Bit Score: 106.41  E-value: 5.12e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  484 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIY 563
Cdd:COG4133  14 ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYLGHADGLKPELTVR 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  564 YNL-----LYGnISASPEEVYAVAKLAGLHDAIlrmphgyDTQVGerglKLSGGEKQRVAIARAILKDPPVILYDEATSS 638
Cdd:COG4133  94 ENLrfwaaLYG-LRADREAIDEALEAVGLAGLA-------DLPVR----QLSAGQKRRVALARLLLSPAPLWLLDEPFTA 161

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 8928549  639 LDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGK 683
Cdd:COG4133 162 LDAAGVALLAELIAAHLARGGAVLLTTHQPLELAAARVLDLGDFK 206
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
 484-698 1.00e-25

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: 106.37  E-value: 1.00e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  484 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSL-ESLRRAVGVVPQDAVLFHN-T 561
Cdd:cd03219  12 GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPhEIARLGIGRTFQIPRLFPElT 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  562 IYYNLLYGNISASPEEVYAVAKLAGLHDA---------ILRMPHGYDTQVGErglkLSGGEKQRVAIARAILKDPPVILY 632
Cdd:cd03219  92 VLENVMVAAQARTGSGLLLARARREEREAreraeelleRVGLADLADRPAGE----LSYGQQRRLEIARALATDPKLLLL 167

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 8928549  633 DEATSSLdSITE-ETILGAMKDVVKHRTSI-FIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGLLANPH 698
Cdd:cd03219 168 DEPAAGL-NPEEtEELAELIRELRERGITVlLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRNNPR 235
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
 485-684 1.11e-25

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: 105.66  E-value: 1.11e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  485 QKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDvSLESLRRAVGVVPQDAVLFHN-TI- 562
Cdd:cd03263  15 KPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGYCPQFDALFDElTVr 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  563 ----YYNLLYG-NISASPEEVYAVAKLAGLHDAIlrmphgyDTQVGErglkLSGGEKQRVAIARAILKDPPVILYDEATS 637
Cdd:cd03263  94 ehlrFYARLKGlPKSEIKEEVELLLRVLGLTDKA-------NKRART----LSGGMKRKLSLAIALIGGPSVLLLDEPTS 162

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 8928549  638 SLDSITEETILGAMKDVVKHRTSIFIAHRLSTV-VDADEIIVLDQGKV 684
Cdd:cd03263 163 GLDPASRRAIWDLILEVRKGRSIILTTHSMDEAeALCDRIAIMSDGKL 210
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
 465-688 1.22e-25

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: 105.53  E-value: 1.22e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  465 ITPQTATVAFDNVHFEYiegqKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESL 544
Cdd:cd03266   2 ITADALTKRFRDVKKTV----QAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEAR 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  545 RRaVGVVPQDAVLF------HNTIYYNLLYGnisASPEEVYA-VAKLAGLhdaiLRMPHGYDTQVGErglkLSGGEKQRV 617
Cdd:cd03266  78 RR-LGFVSDSTGLYdrltarENLEYFAGLYG---LKGDELTArLEELADR----LGMEELLDRRVGG----FSTGMRQKV 145

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 8928549  618 AIARAILKDPPVILYDEATSSLDSITEETILgamkDVVKH-----RTSIFIAHRLSTVVD-ADEIIVLDQGKVAERG 688
Cdd:cd03266 146 AIARALVHDPPVLLLDEPTTGLDVMATRALR----EFIRQlralgKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
cbiO PRK13641
energy-coupling factor transporter ATPase;
471-697 1.85e-25

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 106.84  E-value: 1.85e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   471 TVAFDNVHFEYIEG----QKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQ----DVSLE 542
Cdd:PRK13641   2 SIKFENVDYIYSPGtpmeKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   543 SLRRAVGVVPQ--DAVLFHNTIYYNLLYG--NISASPEEvyavAKLAGLhDAILRMphGYDTQVGERG-LKLSGGEKQRV 617
Cdd:PRK13641  82 KLRKKVSLVFQfpEAQLFENTVLKDVEFGpkNFGFSEDE----AKEKAL-KWLKKV--GLSEDLISKSpFELSGGQMRRV 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   618 AIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKH-RTSIFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGLLA 695
Cdd:PRK13641 155 AIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAgHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKEIFS 234


                 ..
gi 8928549   696 NP 697
Cdd:PRK13641 235 DK 236
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
 476-689 2.10e-25

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 106.43  E-value: 2.10e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   476 NVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQ-- 553
Cdd:PRK13652   8 DLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQnp 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   554 DAVLFHNTIYYNLLYGNISASPEE------VYAVAKLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARAILKDP 627
Cdd:PRK13652  88 DDQIFSPTVEQDIAFGPINLGLDEetvahrVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGVIAMEP 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 8928549   628 PVILYDEATSSLDSITEETILGAMKDVVKH--RTSIFIAHRLSTVVD-ADEIIVLDQGKVAERGT 689
Cdd:PRK13652 157 QVLVLDEPTAGLDPQGVKELIDFLNDLPETygMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGT 221
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
 471-699 2.76e-25

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 105.10  E-value: 2.76e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   471 TVAFDNVHFEYIEGQkVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAG------QNIQDVSLESL 544
Cdd:PRK11124   2 SIQLNGINCFYGAHQ-ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAIREL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   545 RRAVGVVPQDAVLF-HNTIYYNLlygnISAsPEEVYAVAKLAGLHDAI-----LRMphgydTQVGER-GLKLSGGEKQRV 617
Cdd:PRK11124  81 RRNVGMVFQQYNLWpHLTVQQNL----IEA-PCRVLGLSKDQALARAEkllerLRL-----KPYADRfPLHLSGGQQQRV 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   618 AIARAILKDPPVILYDEATSSLD--------SITEE-TILGAMKDVVKHRTSifIAHRLSTVVdadeiIVLDQGKVAERG 688
Cdd:PRK11124 151 AIARALMMEPQVLLFDEPTAALDpeitaqivSIIRElAETGITQVIVTHEVE--VARKTASRV-----VYMENGHIVEQG 223

                        250
                 ....*....|.
gi 8928549   689 THHGlLANPHS 699
Cdd:PRK11124 224 DASC-FTQPQT 233
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
 377-687 5.31e-25

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 110.28  E-value: 5.31e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  377 LNFGQSAIFSVGLTAIMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRE--TRQALIDmnTLFTLLKVDTQI 454
Cdd:COG4178 268 LTFFTTGYGQLAVIFPILVAAPRYFAGEITLGGLMQAASAFGQVQGALSWFVDNYQSlaEWRATVD--RLAGFEEALEAA 345

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  455 KDKVMASPLQITPQTATVAFDNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVR------------------ 516
Cdd:COG4178 346 DALPEAASRIETSEDGALALEDLTLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRaiaglwpygsgriarpag 425

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  517 --LLFRfyePQKgsIYLAgqniqdvsLESLRRAvgvvpqdavlfhntiyynLLYGNI--SASPEEVYAVAKLAGLHDAIL 592
Cdd:COG4178 426 arVLFL---PQR--PYLP--------LGTLREA------------------LLYPATaeAFSDAELREALEAVGLGHLAE 474

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  593 RMphgydTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVD 672
Cdd:COG4178 475 RL-----DEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAF 549

                       330
                ....*....|....*
gi 8928549  673 ADEIIVLDQGKVAER 687
Cdd:COG4178 550 HDRVLELTGDGSWQL 564
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
 468-679 7.27e-25

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 103.64  E-value: 7.27e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   468 QTATVAFDNVHFEyIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRA 547
Cdd:PRK10247   4 NSPLLQLQNVGYL-AGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   548 VGVVPQDAVLFHNTIYYNLL--YGNISASPEEVYAVAKLA--GLHDAILRMPhgydtqVGErglkLSGGEKQRVAIARAI 623
Cdd:PRK10247  83 VSYCAQTPTLFGDTVYDNLIfpWQIRNQQPDPAIFLDDLErfALPDTILTKN------IAE----LSGGEKQRISLIRNL 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   624 LKDPPVILYDEATSSLDS----ITEETILGAMKDvvKHRTSIFIAHRLSTVVDADEIIVL 679
Cdd:PRK10247 153 QFMPKVLLLDEITSALDEsnkhNVNEIIHRYVRE--QNIAVLWVTHDKDEINHADKVITL 210
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
 474-697 7.58e-25

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 105.10  E-value: 7.58e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   474 FDNVHFEYIEG----QKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQ----DVSLESLR 545
Cdd:PRK13634   5 FQKVEHRYQYKtpfeRRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkkNKKLKPLR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   546 RAVGVVPQ--DAVLFHNTIYYNLLYG--NISASPEEVYAVAK----LAGLHDAIL-RMPhgydtqvgergLKLSGGEKQR 616
Cdd:PRK13634  85 KKVGIVFQfpEHQLFEETVEKDICFGpmNFGVSEEDAKQKARemieLVGLPEELLaRSP-----------FELSGGQMRR 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   617 VAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGL 693
Cdd:PRK13634 154 VAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKglTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREI 233


                 ....
gi 8928549   694 LANP 697
Cdd:PRK13634 234 FADP 237
cbiO PRK13650
energy-coupling factor transporter ATPase;
476-695 8.53e-25

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 104.81  E-value: 8.53e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   476 NVHFEYIEGQK--VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQ 553
Cdd:PRK13650   9 NLTFKYKEDQEkyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMVFQ 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   554 --DAVLFHNTIYYNLLYG--NISASPEE----VYAVAKLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARAILK 625
Cdd:PRK13650  89 npDNQFVGATVEDDVAFGleNKGIPHEEmkerVNEALELVGMQDFKEREPA-----------RLSGGQKQRVAIAGAVAM 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 8928549   626 DPPVILYDEATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLLA 695
Cdd:PRK13650 158 RPKIIILDEATSMLDPEGRLELIKTIKGIRDDYqmTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFS 229
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
 472-682 1.02e-24

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


Pssm-ID: 213257 [Multi-domain]  Cd Length: 218  Bit Score: 102.79  E-value: 1.02e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  472 VAFDNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESL----RRA 547
Cdd:cd03290   1 VQVTNGYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATrsrnRYS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  548 VGVVPQDAVLFHNTIYYNLLYGnisaSP---EEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAIL 624
Cdd:cd03290  81 VAYAAQKPWLLNATVEENITFG----SPfnkQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALY 156

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 8928549  625 KDPPVILYDEATSSL-----DSITEETILGAMKDvvKHRTSIFIAHRLSTVVDADEIIVLDQG 682
Cdd:cd03290 157 QNTNIVFLDDPFSALdihlsDHLMQEGILKFLQD--DKRTLVLVTHKLQYLPHADWIIAMKDG 217
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
 472-688 1.19e-24

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


Pssm-ID: 440736 [Multi-domain]  Cd Length: 250  Bit Score: 103.63  E-value: 1.19e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  472 VAFDNVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKG-SIYLAGQNIQDVSLESLRRAVGV 550
Cdd:COG1119   4 LELRNVTVRR-GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKRIGL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  551 VPQDavlFHNTIYYNL---------LYGNI----SASPEEVYAVAKLAglhdAILRMPHGYDTQVGErglkLSGGEKQRV 617
Cdd:COG1119  83 VSPA---LQLRFPRDEtvldvvlsgFFDSIglyrEPTDEQRERARELL----ELLGLAHLADRPFGT----LSQGEQRRV 151

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 8928549  618 AIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKH--RTSIFIAHRLSTVVDA-DEIIVLDQGKVAERG 688
Cdd:COG1119 152 LIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEgaPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAAG 225
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
 476-700 1.20e-24

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 104.39  E-value: 1.20e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   476 NVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQ--DVSLESLRRAVGVVPQ 553
Cdd:PRK13639   6 DLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydKKSLLEVRKTVGIVFQ 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   554 --DAVLFHNTIYYNLLYG--NISASPEEVYAVAKLA----GLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARAILK 625
Cdd:PRK13639  86 npDDQLFAPTVEEDVAFGplNLGLSKEEVEKRVKEAlkavGMEGFENKPPH-----------HLSGGQKKRVAIAGILAM 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 8928549   626 DPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIA-HRLSTV-VDADEIIVLDQGKVAERGTHHGLLANPHSI 700
Cdd:PRK13639 155 KPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIIStHDVDLVpVYADKVYVMSDGKIIKEGTPKEVFSDIETI 231
COG4559 COG4559
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
475-689 1.94e-24

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


Pssm-ID: 443620 [Multi-domain]  Cd Length: 258  Bit Score: 103.27  E-value: 1.94e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  475 DNVHFEYieGQK-VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESL--RRAVgvV 551
Cdd:COG4559   5 ENLSVRL--GGRtLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELarRRAV--L 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  552 PQDAVLfhntiyynllygnisASPEEVYAVAKLAglhdailRMPHGYDT------------QVGERGLK------LSGGE 613
Cdd:COG4559  81 PQHSSL---------------AFPFTVEEVVALG-------RAPHGSSAaqdrqivrealaLVGLAHLAgrsyqtLSGGE 138

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  614 KQRVAIARAIL-------KDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIF-IAHRLS-TVVDADEIIVLDQGKV 684
Cdd:COG4559 139 QQRVQLARVLAqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVaVLHDLNlAAQYADRILLLHQGRL 218


                ....*
gi 8928549  685 AERGT 689
Cdd:COG4559 219 VAQGT 223
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
471-699 2.00e-24

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


Pssm-ID: 443326 [Multi-domain]  Cd Length: 242  Bit Score: 102.78  E-value: 2.00e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  471 TVAFDNVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAG------QNIQDVSLESL 544
Cdd:COG4161   2 SIQLKNINCFY-GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIRLL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  545 RRAVGVVPQDAVLF-HNTIYYNLLygnisASPEEVYAVAKLAGLHDAI-----LRMphgydTQVGER-GLKLSGGEKQRV 617
Cdd:COG4161  81 RQKVGMVFQQYNLWpHLTVMENLI-----EAPCKVLGLSKEQAREKAMkllarLRL-----TDKADRfPLHLSGGQQQRV 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  618 AIARAILKDPPVILYDEATSSLDS---------ITEETILGAMKDVVKHRTSifIAHRLstvvdADEIIVLDQGKVAERG 688
Cdd:COG4161 151 AIARALMMEPQVLLFDEPTAALDPeitaqvveiIRELSQTGITQVIVTHEVE--FARKV-----ASQVVYMEKGRIIEQG 223

                       250
                ....*....|.
gi 8928549  689 THHgLLANPHS 699
Cdd:COG4161 224 DAS-HFTQPQT 233
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
492-695 2.50e-24

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 102.35  E-value: 2.50e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   492 SFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLEslRRAVGVVPQDAVLF-HNTIYYNLLYG- 569
Cdd:PRK10771  19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQENNLFsHLTVAQNIGLGl 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   570 ------NiSASPEEVYAVAKLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSIT 643
Cdd:PRK10771  97 npglklN-AAQREKLHAIARQMGIEDLLARLPG-----------QLSGGQRQRVALARCLVREQPILLLDEPFSALDPAL 164

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 8928549   644 EETILGAMKDVVKHR--TSIFIAHRLStvvDADEI----IVLDQGKVAERGTHHGLLA 695
Cdd:PRK10771 165 RQEMLTLVSQVCQERqlTLLMVSHSLE---DAARIaprsLVVADGRIAWDGPTDELLS 219
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
 482-689 2.58e-24

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 102.93  E-value: 2.58e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   482 IEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLfhnt 561
Cdd:PRK13548  12 LGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSL---- 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   562 iyynllygNISASPEEVYAVAklaglhdailRMPHGYD------------TQVGERGLK------LSGGEKQRVAIARAI 623
Cdd:PRK13548  88 --------SFPFTVEEVVAMG----------RAPHGLSraeddalvaaalAQVDLAHLAgrdypqLSGGEQQRVQLARVL 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 8928549   624 L------KDPPVILYDEATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLS-TVVDADEIIVLDQGKVAERGT 689
Cdd:PRK13548 150 AqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERglAVIVVLHDLNlAARYADRIVLLHQGRLVADGT 224
PTZ00243 PTZ00243
ABC transporter; Provisional
 466-741 2.71e-24

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 109.48  E-value: 2.71e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    466 TPQTATVAFdnvhFEyIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAgqniqdvsleslr 545
Cdd:PTZ00243  659 TPKMKTDDF----FE-LEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE------------- 720

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    546 RAVGVVPQDAVLFHNTIYYNLLYGNisaspEEvyavaKLAGLHDAI---------LRMPHGYDTQVGERGLKLSGGEKQR 616
Cdd:PTZ00243  721 RSIAYVPQQAWIMNATVRGNILFFD-----EE-----DAARLADAVrvsqleadlAQLGGGLETEIGEKGVNLSGGQKAR 790

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    617 VAIARAILKDPPVILYDEATSSLDS-----ITEETILGAMKDvvkhRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHH 691
Cdd:PTZ00243  791 VSLARAVYANRDVYLLDDPLSALDAhvgerVVEECFLGALAG----KTRVLATHQVHVVPRADYVVALGDGRVEFSGSSA 866

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 8928549    692 GLLANPhsIYSEMwhtqssRVQNHDNPkwEAKKENISKEEERKKLQEEIV 741
Cdd:PTZ00243  867 DFMRTS--LYATL------AAELKENK--DSKEGDADAEVAEVDAAPGGA 906
cbiO PRK13640
energy-coupling factor transporter ATPase;
472-689 2.86e-24

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 103.34  E-value: 2.86e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   472 VAFDNVHFEYIEGQK-VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQ---KGSIYLAGQNIQDVSLESLRRA 547
Cdd:PRK13640   6 VEFKHVSFTYPDSKKpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDdnpNSKITVDGITLTAKTVWDIREK 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   548 VGVVPQ--DAVLFHNTIYYNLLYG--NISASPEE----VYAVAKLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVAI 619
Cdd:PRK13640  86 VGIVFQnpDNQFVGATVGDDVAFGleNRAVPRPEmikiVRDVLADVGMLDYIDSEPA-----------NLSGGQKQRVAI 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 8928549   620 ARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLSTVVDADEIIVLDQGKVAERGT 689
Cdd:PRK13640 155 AGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLLAQGS 226
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
484-684 5.70e-24

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 106.26  E-value: 5.70e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  484 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS-LESLRRAVGVVPQDAVLFHN-T 561
Cdd:COG1129  16 GVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSpRDAQAAGIAIIHQELNLVPNlS 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  562 IYYNLLYGNISASP-----EEVYAVAK--LAGLH---DAilrmphgyDTQVGErglkLSGGEKQRVAIARAILKDPPVIL 631
Cdd:COG1129  96 VAENIFLGREPRRGglidwRAMRRRARelLARLGldiDP--------DTPVGD----LSVAQQQLVEIARALSRDARVLI 163

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 8928549  632 YDEATSSLDSiTE-ETILGAMKDVVKH-RTSIFIAHRLSTVVD-ADEIIVLDQGKV 684
Cdd:COG1129 164 LDEPTASLTE-REvERLFRIIRRLKAQgVAIIYISHRLDEVFEiADRVTVLRDGRL 218
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
494-684 1.21e-23

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 103.03  E-value: 1.21e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   494 EVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNI----QDVSLESLRRAVGVVPQDAVLF-HNTIYYNLLY 568
Cdd:PRK11144  20 TLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLfdaeKGICLPPEKRRIGYVFQDARLFpHYKVRGNLRY 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   569 GNISASPEEVYAVAKLAGLHDAILRMPHGydtqvgerglkLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETIL 648
Cdd:PRK11144 100 GMAKSMVAQFDKIVALLGIEPLLDRYPGS-----------LSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELL 168

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 8928549   649 GAMKDVVKH-RTSI-FIAHRLSTVVD-ADEIIVLDQGKV 684
Cdd:PRK11144 169 PYLERLAREiNIPIlYVSHSLDEILRlADRVVVLEQGKV 207
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
 486-698 1.44e-23

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 102.24  E-value: 1.44e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   486 KVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYL----AGQNIQDVS------------LESLRRAVG 549
Cdd:PRK13631  40 VALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyIGDKKNNHElitnpyskkiknFKELRRRVS 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   550 VVPQ--DAVLFHNTIYYNLLYGNISASPEEVYAvAKLAGLHdaILRMphGYDTQVGERG-LKLSGGEKQRVAIARAILKD 626
Cdd:PRK13631 120 MVFQfpEYQLFKDTIEKDIMFGPVALGVKKSEA-KKLAKFY--LNKM--GLDDSYLERSpFGLSGGQKRRVAIAGILAIQ 194

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 8928549   627 PPVILYDEATSSLDSITEETILGAMKDVVKH-RTSIFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGLLANPH 698
Cdd:PRK13631 195 PEILIFDEPTAGLDPKGEHEMMQLILDAKANnKTVFVITHTMEHVLEvADEVIVMDKGKILKTGTPYEIFTDQH 268
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
 487-702 1.48e-23

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 105.17  E-value: 1.48e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   487 VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQkGSIYLAGQNIQDVS---LESLRRAVGVVPQDAVLFHN--- 560
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQ-GEIWFDGQPLHNLNrrqLLPVRHRIQVVFQDPNSSLNprl 379

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   561 ----------TIYYNLLygNISASPEEVYAVAKLAGLhDAILRmpHGYDTQvgerglkLSGGEKQRVAIARAILKDPPVI 630
Cdd:PRK15134 380 nvlqiieeglRVHQPTL--SAAQREQQVIAVMEEVGL-DPETR--HRYPAE-------FSGGQRQRIAIARALILKPSLI 447

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 8928549   631 LYDEATSSLDSITEETILGAMKDV-VKHRTS-IFIAHRLStVVDA--DEIIVLDQGKVAERGTHHGLLANPHSIYS 702
Cdd:PRK15134 448 ILDEPTSSLDKTVQAQILALLKSLqQKHQLAyLFISHDLH-VVRAlcHQVIVLRQGEVVEQGDCERVFAAPQQEYT 522
SapF COG4167
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
491-697 1.66e-23

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


Pssm-ID: 443328 [Multi-domain]  Cd Length: 265  Bit Score: 100.68  E-value: 1.66e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  491 ISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAG------------QNI----QDVSlESL--RRAVGvvp 552
Cdd:COG4167  32 VSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGhkleygdykyrcKHIrmifQDPN-TSLnpRLNIG--- 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  553 Q--DAVLFHNTiyyNLlygNISASPEEVYAVAKLAGLH-DAILRMPHgydtqvgerglKLSGGEKQRVAIARAILKDPPV 629
Cdd:COG4167 108 QilEEPLRLNT---DL---TAEEREERIFATLRLVGLLpEHANFYPH-----------MLSSGQKQRVALARALILQPKI 170

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 8928549  630 ILYDEATSSLDSITEETILGAMKDV-VKHRTS-IFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGLLANP 697
Cdd:COG4167 171 IIADEALAALDMSVRSQIINLMLELqEKLGISyIYVSQHLGIVKHiSDKVLVMHQGEVVEYGKTAEVFANP 241
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
485-686 3.54e-23

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 99.76  E-value: 3.54e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   485 QKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLE---SLRRAVGVVPQD---AVLF 558
Cdd:PRK10419  25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAqrkAFRRDIQMVFQDsisAVNP 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   559 HNTIyynllyGNISASP-------------EEVYAVAKLAGLHDAIL-RMPHgydtqvgerglKLSGGEKQRVAIARAIL 624
Cdd:PRK10419 105 RKTV------REIIREPlrhllsldkaerlARASEMLRAVDLDDSVLdKRPP-----------QLSGGQLQRVCLARALA 167

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 8928549   625 KDPPVILYDEATSSLDSITEETILGAMKDvVKHRTSI---FIAHRLSTVVD-ADEIIVLDQGKVAE 686
Cdd:PRK10419 168 VEPKLLILDEAVSNLDLVLQAGVIRLLKK-LQQQFGTaclFITHDLRLVERfCQRVMVMDNGQIVE 232
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
472-692 4.34e-23

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 98.41  E-value: 4.34e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   472 VAFDNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNI---QDVSLESLRRAV 548
Cdd:PRK10908   2 IRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlKNREVPFLRRQI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   549 GVVPQDA-VLFHNTIYYNLLYGNI--SASPEE----VYAVAKLAGLHDAILRMPhgydtqvgergLKLSGGEKQRVAIAR 621
Cdd:PRK10908  82 GMIFQDHhLLMDRTVYDNVAIPLIiaGASGDDirrrVSAALDKVGLLDKAKNFP-----------IQLSGGEQQRVGIAR 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 8928549   622 AILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIA-HRLSTVVDAD-EIIVLDQGKVAerGTHHG 692
Cdd:PRK10908 151 AVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMAtHDIGLISRRSyRMLTLSDGHLH--GGVGG 221
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
487-701 7.76e-23

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 100.56  E-value: 7.76e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   487 VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLEslRRAVGVVPQDAVLF-HNTIYYN 565
Cdd:PRK11432  21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ--QRDICMVFQSYALFpHMSLGEN 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   566 LLYG---------NISASPEEVYAVAKLAGLHDAilrmphgYDTQVgerglklSGGEKQRVAIARAILKDPPVILYDEAT 636
Cdd:PRK11432  99 VGYGlkmlgvpkeERKQRVKEALELVDLAGFEDR-------YVDQI-------SGGQQQRVALARALILKPKVLLFDEPL 164

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 8928549   637 SSLDSiteeTILGAMKDVVKHR------TSIFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGLLANPHSIY 701
Cdd:PRK11432 165 SNLDA----NLRRSMREKIRELqqqfniTSLYVTHDQSEAFAvSDTVIVMNKGKIMQIGSPQELYRQPASRF 232
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
 488-694 9.80e-23

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 98.32  E-value: 9.80e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   488 LSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYE-----PQKGSIYLAGQNI--QDVSLESLRRAVGVVPQDAVLFHN 560
Cdd:PRK14243  26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNLyaPDVDPVEVRRRIGMVFQKPNPFPK 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   561 TIYYNLLYG-NISASP----EEVYAVAKLAGLHDAIlrmphgyDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEA 635
Cdd:PRK14243 106 SIYDNIAYGaRINGYKgdmdELVERSLRQAALWDEV-------KDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEP 178

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 8928549   636 TSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLL 694
Cdd:PRK14243 179 CSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFNVELTEGGGRYGYL 237
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
 472-698 1.49e-22

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 97.80  E-value: 1.49e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   472 VAFDNVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQ-----KGSIYLAGQNIQD--VSLESL 544
Cdd:PRK14258   8 IKVNNLSFYY-DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVEFFNQNIYErrVNLNRL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   545 RRAVGVVPQDAVLFHNTIYYNLLYGN--ISASPEE-----VYAVAKLAGLHDAILRMPHgydtqvgERGLKLSGGEKQRV 617
Cdd:PRK14258  87 RRQVSMVHPKPNLFPMSVYDNVAYGVkiVGWRPKLeiddiVESALKDADLWDEIKHKIH-------KSALDLSGGQQQRL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   618 AIARAILKDPPVILYDEATSSLDSITEETILGAMKDVV--KHRTSIFIAHRLSTVVDADEIIVLDQG------KVAERGT 689
Cdd:PRK14258 160 CIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlrSELTMVIVSHNLHQVSRLSDFTAFFKGnenrigQLVEFGL 239


                 ....*....
gi 8928549   690 HHGLLANPH 698
Cdd:PRK14258 240 TKKIFNSPH 248
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
486-711 1.63e-22

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 99.77  E-value: 1.63e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   486 KVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQniqDVSLESLR-RAVGVVPQDAVLF-HNTIY 563
Cdd:PRK10851  16 QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGT---DVSRLHARdRKVGFVFQHYALFrHMTVF 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   564 YNLLYGnISASPE----EVYAV-AKLAGLHDaILRMPH---GYDTQvgerglkLSGGEKQRVAIARAILKDPPVILYDEA 635
Cdd:PRK10851  93 DNIAFG-LTVLPRrerpNAAAIkAKVTQLLE-MVQLAHladRYPAQ-------LSGGQKQRVALARALAVEPQILLLDEP 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   636 TSSLDSITEETI---LGAMKDVVKHrTSIFIAHRLSTVVD-ADEIIVLDQGKVAERGThhgllanPhsiySEMWHTQSSR 711
Cdd:PRK10851 164 FGALDAQVRKELrrwLRQLHEELKF-TSVFVTHDQEEAMEvADRVVVMSQGNIEQAGT-------P----DQVWREPATR 231
cbiO PRK13646
energy-coupling factor transporter ATPase;
471-706 3.29e-22

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 97.54  E-value: 3.29e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   471 TVAFDNVHFEYIEG----QKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNI----QDVSLE 542
Cdd:PRK13646   2 TIRFDNVSYTYQKGtpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktKDKYIR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   543 SLRRAVGVVPQ--DAVLFHNTIYYNLLYG--NISASPEEVYAVAklaglHDaiLRMPHGYDTQVGERG-LKLSGGEKQRV 617
Cdd:PRK13646  82 PVRKRIGMVFQfpESQLFEDTVEREIIFGpkNFKMNLDEVKNYA-----HR--LLMDLGFSRDVMSQSpFQMSGGQMRKI 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   618 AIARAILKDPPVILYDEATSSLDSITEETILGAMKD--VVKHRTSIFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGLL 694
Cdd:PRK13646 155 AIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSlqTDENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKELF 234

                        250
                 ....*....|..
gi 8928549   695 ANPHsiYSEMWH 706
Cdd:PRK13646 235 KDKK--KLADWH 244
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
 482-640 4.54e-22

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


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 94.86  E-value: 4.54e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  482 IEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQ---KGSIYLAGQNIQDVSLEslRRAVGVVPQDAVLF 558
Cdd:COG4136  11 LGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAE--QRRIGILFQDDLLF 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  559 -HNTIYYNLLYG-----NISASPEEVYAVAKLAGLHDAILRMPhgyDTqvgerglkLSGGEKQRVAIARAILKDPPVILY 632
Cdd:COG4136  89 pHLSVGENLAFAlpptiGRAQRRARVEQALEEAGLAGFADRDP---AT--------LSGGQRARVALLRALLAEPRALLL 157


                ....*...
gi 8928549  633 DEATSSLD 640
Cdd:COG4136 158 DEPFSKLD 165
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
 464-707 5.26e-22

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 96.14  E-value: 5.26e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   464 QITPQTATVAFDNVhfeyiegqKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYE--PQ---KGSIYLAGQNIQD 538
Cdd:PRK14247   3 KIEIRDLKVSFGQV--------EVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEarvSGEVYLDGQDIFK 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   539 VSLESLRRAVGVVPQDAVLFHN-TIYYNLLYG----NISASPEEVYAVAKLAgLHDAIL--RMPHGYDTQVGerglKLSG 611
Cdd:PRK14247  75 MDVIELRRRVQMVFQIPNPIPNlSIFENVALGlklnRLVKSKKELQERVRWA-LEKAQLwdEVKDRLDAPAG----KLSG 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   612 GEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAH------RLStvvdaDEIIVLDQGKVA 685
Cdd:PRK14247 150 GQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRIS-----DYVAFLYKGQIV 224

                        250       260
                 ....*....|....*....|..
gi 8928549   686 ERGTHHGLLANPHSIYSEMWHT 707
Cdd:PRK14247 225 EWGPTREVFTNPRHELTEKYVT 246
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
 487-640 5.39e-22

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


Pssm-ID: 443809 [Multi-domain]  Cd Length: 229  Bit Score: 95.19  E-value: 5.39e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  487 VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYL--AGQNIqDVS-------LESLRRAVGVVPQdavl 557
Cdd:COG4778  26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWV-DLAqaspreiLALRRRTIGYVSQ---- 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  558 FHNTIyynllyGNISAspEEVyaVAklaglhDAILRMphGYDTQVG-ERGLKL------------------SGGEKQRVA 618
Cdd:COG4778 101 FLRVI------PRVSA--LDV--VA------EPLLER--GVDREEArARARELlarlnlperlwdlppatfSGGEQQRVN 162

                       170       180
                ....*....|....*....|..
gi 8928549  619 IARAILKDPPVILYDEATSSLD 640
Cdd:COG4778 163 IARGFIADPPLLLLDEPTASLD 184
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
 484-688 7.76e-22

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: 94.21  E-value: 7.76e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  484 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDvsLESLRRAVGVVpqdavlfhntIY 563
Cdd:cd03268  12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK--NIEALRRIGAL----------IE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  564 YNLLYGNISASpEEVYAVAKLAGL----HDAILRMPhGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSL 639
Cdd:cd03268  80 APGFYPNLTAR-ENLRLLARLLGIrkkrIDEVLDVV-GLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGL 157

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 8928549  640 D--SITE--ETILgamkDVVKHRTSIFIA-HRLSTVVD-ADEIIVLDQGKVAERG 688
Cdd:cd03268 158 DpdGIKElrELIL----SLRDQGITVLISsHLLSEIQKvADRIGIINKGKLIEEG 208
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
492-701 1.05e-21

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


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 98.18  E-value: 1.05e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   492 SFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESL----RRAVGVVPQD-AVLFHNTIYYNL 566
Cdd:PRK10070  48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELrevrRKKIAMVFQSfALMPHMTVLDNT 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   567 LYG-NISASPEEVYAVAKLAGLHDAILR-MPHGYDTQvgerglkLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITE 644
Cdd:PRK10070 128 AFGmELAGINAEERREKALDALRQVGLEnYAHSYPDE-------LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIR 200

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   645 ETILGAM-KDVVKH-RTSIFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGLLANPHSIY 701
Cdd:PRK10070 201 TEMQDELvKLQAKHqRTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEILNNPANDY 260
cbiO PRK13645
energy-coupling factor transporter ATPase;
469-696 1.73e-21

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 95.46  E-value: 1.73e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   469 TATVAFDNVHFEYIEGQ----KVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSI----YLAGQNIQDV- 539
Cdd:PRK13645   4 SKDIILDNVSYTYAKKTpfefKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTivgdYAIPANLKKIk 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   540 SLESLRRAVGVVPQ--DAVLFHNTIYYNLLYG--NISASPEEVYAvaKLAGLHDaILRMPHGYdtqVGERGLKLSGGEKQ 615
Cdd:PRK13645  84 EVKRLRKEIGLVFQfpEYQLFQETIEKDIAFGpvNLGENKQEAYK--KVPELLK-LVQLPEDY---VKRSPFELSGGQKR 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   616 RVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKH--RTSIFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHG 692
Cdd:PRK13645 158 RVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEykKRIIMVTHNMDQVLRiADEVIVMHEGKVISIGSPFE 237


                 ....
gi 8928549   693 LLAN 696
Cdd:PRK13645 238 IFSN 241
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
469-695 2.53e-21

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 95.26  E-value: 2.53e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   469 TATVAFDNVHFEYIEgQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESlRRAV 548
Cdd:PRK13537   5 VAPIDFRNVEKRYGD-KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA-RQRV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   549 GVVPQdavlFHN-----TIYYNLL----YGNISASPeevyAVAKLAGLHDaILRMPHGYDTQVGErglkLSGGEKQRVAI 619
Cdd:PRK13537  83 GVVPQ----FDNldpdfTVRENLLvfgrYFGLSAAA----ARALVPPLLE-FAKLENKADAKVGE----LSGGMKRRLTL 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   620 ARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFI-------AHRLstvvdADEIIVLDQG-KVAErGTHH 691
Cdd:PRK13537 150 ARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLtthfmeeAERL-----CDRLCVIEEGrKIAE-GAPH 223


                 ....
gi 8928549   692 GLLA 695
Cdd:PRK13537 224 ALIE 227
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
469-684 3.02e-21

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 98.64  E-value: 3.02e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   469 TATVAFDNVHFEYIEGQ---KVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDV---SLE 542
Cdd:PRK10535   2 TALLELKDIRRSYPSGEeqvEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLdadALA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   543 SLRRA-VGVVPQDavlfhntiyYNLLYGNISASPEEVYAV-------AKLAGLHDAILRMphGYDTQVGERGLKLSGGEK 614
Cdd:PRK10535  82 QLRREhFGFIFQR---------YHLLSHLTAAQNVEVPAVyaglerkQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQ 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 8928549   615 QRVAIARAILKDPPVILYDEATSSLDSITEE---TILGAMKDvvKHRTSIFIAHRLSTVVDADEIIVLDQGKV 684
Cdd:PRK10535 151 QRVSIARALMNGGQVILADEPTGALDSHSGEevmAILHQLRD--RGHTVIIVTHDPQVAAQAERVIEIRDGEI 221
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
 486-643 3.34e-21

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: 93.10  E-value: 3.34e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  486 KVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQK---GSIYLAGQniqDVSLESLRRAVGVVPQ-DAVLFHNT 561
Cdd:cd03234  21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQ---PRKPDQFQKCVAYVRQdDILLPGLT 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  562 IYYNLLYGNISASPEEVYAVAKLAglHDAILRMPHGYDTQVGERGLK-LSGGEKQRVAIARAILKDPPVILYDEATSSLD 640
Cdd:cd03234  98 VRETLTYTAILRLPRKSSDAIRKK--RVEDVLLRDLALTRIGGNLVKgISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175


                ...
gi 8928549  641 SIT 643
Cdd:cd03234 176 SFT 178
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
 484-689 5.76e-21

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


Pssm-ID: 213258 [Multi-domain]  Cd Length: 282  Bit Score: 93.77  E-value: 5.76e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  484 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQniqdvsleslrraVGVVPQDAVLFHNTIY 563
Cdd:cd03291  49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQFSWIMPGTIK 115

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  564 YNLLYGnISASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSIT 643
Cdd:cd03291 116 ENIIFG-VSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFT 194

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 8928549  644 EETIL-GAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGT 689
Cdd:cd03291 195 EKEIFeSCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGT 241
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
 476-689 6.13e-21

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 93.76  E-value: 6.13e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   476 NVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIqDVS---LESLRRAVGVVP 552
Cdd:PRK13636  10 ELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSrkgLMKLRESVGMVF 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   553 Q--DAVLFHNTIYYNLLYG--NISASPEEVYAVAKLAGLHDAILRMPHgydtqvgERGLKLSGGEKQRVAIARAILKDPP 628
Cdd:PRK13636  89 QdpDNQLFSASVYQDVSFGavNLKLPEDEVRKRVDNALKRTGIEHLKD-------KPTHCLSFGQKKRVAIAGVLVMEPK 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 8928549   629 VILYDEATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLSTV-VDADEIIVLDQGKVAERGT 689
Cdd:PRK13636 162 VLVLDEPTAGLDPMGVSEIMKLLVEMQKELglTIIIATHDIDIVpLYCDNVFVMKEGRVILQGN 225
cbiO PRK13642
energy-coupling factor transporter ATPase;
475-695 7.08e-21

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 93.23  E-value: 7.08e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   475 DNVHFEYIEGQKV--LSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVP 552
Cdd:PRK13642   8 ENLVFKYEKESDVnqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVF 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   553 Q--DAVLFHNTIYYNLLYG--NISASPEEVyavakLAGLHDAILRMpHGYDTQVGERGlKLSGGEKQRVAIARAILKDPP 628
Cdd:PRK13642  88 QnpDNQFVGATVEDDVAFGmeNQGIPREEM-----IKRVDEALLAV-NMLDFKTREPA-RLSGGQKQRVAVAGIIALRPE 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 8928549   629 VILYDEATSSLDSITEETILGAMKDVVK--HRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLLA 695
Cdd:PRK13642 161 IIILDESTSMLDPTGRQEIMRVIHEIKEkyQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
475-668 1.53e-20

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 91.42  E-value: 1.53e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   475 DNVHFEYIEGQ---KVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLES---LR-RA 547
Cdd:PRK11629   9 DNLCKRYQEGSvqtDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeLRnQK 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   548 VGVVPQdavlFHN---------TIYYNLLYGNISASPEEVYAVAKLAGLhdailrmphGYDTQVGERGLKLSGGEKQRVA 618
Cdd:PRK11629  89 LGFIYQ----FHHllpdftaleNVAMPLLIGKKKPAEINSRALEMLAAV---------GLEHRANHRPSELSGGERQRVA 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   619 IARAILKDPPVILYDEATSSLDSITEETI---LGAMKD-------VVKHrtSIFIAHRLS 668
Cdd:PRK11629 156 IARALVNNPRLVLADEPTGNLDARNADSIfqlLGELNRlqgtaflVVTH--DLQLAKRMS 213
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
470-689 2.11e-20

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


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 93.37  E-value: 2.11e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   470 ATVAFDNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDvsLESLRRAVG 549
Cdd:PRK11650   2 AGLKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNE--LEPADRDIA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   550 VVPQDAVLF-HNTIYYNLLYG-NISASPEE-----VYAVAKLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARA 622
Cdd:PRK11650  80 MVFQNYALYpHMSVRENMAYGlKIRGMPKAeieerVAEAARILELEPLLDRKPR-----------ELSGGQRQRVAMGRA 148

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 8928549   623 ILKDPPVILYDEATSSLDSiteeTILGAMKDVVK--HR----TSIFIAH-RLSTVVDADEIIVLDQGKVAERGT 689
Cdd:PRK11650 149 IVREPAVFLFDEPLSNLDA----KLRVQMRLEIQrlHRrlktTSLYVTHdQVEAMTLADRVVVMNGGVAEQIGT 218
cbiO PRK13649
energy-coupling factor transporter ATPase;
472-689 2.16e-20

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 92.11  E-value: 2.16e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   472 VAFDNVHFEYIEGQ----KVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS----LES 543
Cdd:PRK13649   3 INLQNVSYTYQAGTpfegRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdIKQ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   544 LRRAVGVVPQ--DAVLFHNTIYYNLLYG--NISASPEEVYAVA--KLAGLhdailrmphGYDTQVGERG-LKLSGGEKQR 616
Cdd:PRK13649  83 IRKKVGLVFQfpESQLFEETVLKDVAFGpqNFGVSQEEAEALAreKLALV---------GISESLFEKNpFELSGGQMRR 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 8928549   617 VAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVvkHR---TSIFIAHRLSTVVD-ADEIIVLDQGKVAERGT 689
Cdd:PRK13649 154 VAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKL--HQsgmTIVLVTHLMDDVANyADFVYVLEKGKLVLSGK 228
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
453-702 2.68e-20

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 93.75  E-value: 2.68e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   453 QIKDKVMASPLqITPQTATVAFDnvhfeyieGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLA 532
Cdd:PRK11607   9 QAKTRKALTPL-LEIRNLTKSFD--------GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   533 GQNIQDVSleSLRRAVGVVPQDAVLF-HNTIYYNLLYG---------NISASPEEVYAvakLAGLHDAILRMPHgydtqv 602
Cdd:PRK11607  80 GVDLSHVP--PYQRPINMMFQSYALFpHMTVEQNIAFGlkqdklpkaEIASRVNEMLG---LVHMQEFAKRKPH------ 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   603 gerglKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKH--RTSIFIAH-RLSTVVDADEIIVL 679
Cdd:PRK11607 149 -----QLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERvgVTCVMVTHdQEEAMTMAGRIAIM 223

                        250       260
                 ....*....|....*....|...
gi 8928549   680 DQGKVAERGTHHGLLANPHSIYS 702
Cdd:PRK11607 224 NRGKFVQIGEPEEIYEHPTTRYS 246
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
 433-702 3.41e-20

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 92.46  E-value: 3.41e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   433 ETRQALIDMNTLftllKVDTQIKDKvMASPLQiTPQTAtvafdnvhfeyiegqKVLSGISFEVPAGKKVAIVGGSGSGKS 512
Cdd:PRK15079   3 EGKKVLLEVADL----KVHFDIKDG-KQWFWQ-PPKTL---------------KAVDGVTLRLYEGETLGVVGESGCGKS 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   513 TIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRA---VGVVPQDAVLFHN---TIyynllyGNISASPEEVY------- 579
Cdd:PRK15079  62 TFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVrsdIQMIFQDPLASLNprmTI------GEIIAEPLRTYhpklsrq 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   580 --------AVAKLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAM 651
Cdd:PRK15079 136 evkdrvkaMMLKVGLLPNLINRYPH-----------EFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLL 204

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 8928549   652 KDVVKHR--TSIFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGLLANPHSIYS 702
Cdd:PRK15079 205 QQLQREMglSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEVYHNPLHPYT 258
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
485-691 5.65e-20

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 90.07  E-value: 5.65e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   485 QKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQ-----DAVLFH 559
Cdd:PRK11231  15 KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQhhltpEGITVR 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   560 NTIYY-----NLLYGNISASPEEVYAVAklaglhdailrMPHGYDTQVGERGL-KLSGGEKQRVAIARAILKDPPVILYD 633
Cdd:PRK11231  95 ELVAYgrspwLSLWGRLSAEDNARVNQA-----------MEQTRINHLADRRLtDLSGGQRQRAFLAMVLAQDTPVVLLD 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   634 EATSSLDSITEETILGAMKDV-VKHRTSIFIAHRLSTVVD-ADEIIVLDQGKVAERGTHH 691
Cdd:PRK11231 164 EPTTYLDINHQVELMRLMRELnTQGKTVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPE 223
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
 481-705 6.48e-20

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 90.11  E-value: 6.48e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   481 YIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYE------PQKGSIYLAGQNIQDVSLESLRRAVGVVPQD 554
Cdd:PRK14246  19 YINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQ 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   555 AVLF-HNTIYYNLLYGNISASPEEVYAVAKLagLHDAILRMphGYDTQVGER----GLKLSGGEKQRVAIARAILKDPPV 629
Cdd:PRK14246  99 PNPFpHLSIYDNIAYPLKSHGIKEKREIKKI--VEECLRKV--GLWKEVYDRlnspASQLSGGQQQRLTIARALALKPKV 174

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 8928549   630 ILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGLLANPHSIYSEMW 705
Cdd:PRK14246 175 LLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIFTSPKNELTEKY 251
TauB COG4525
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
475-687 6.92e-20

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


Pssm-ID: 443596 [Multi-domain]  Cd Length: 262  Bit Score: 89.92  E-value: 6.92e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  475 DNVHFEY---IEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLEslrRAVgVV 551
Cdd:COG4525   7 RHVSVRYpggGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGAD---RGV-VF 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  552 PQDAVLFHNTIYYNLLYG----NISASPEEVYAVAKLA--GLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARAILK 625
Cdd:COG4525  83 QKDALLPWLNVLDNVAFGlrlrGVPKAERRARAEELLAlvGLADFARRRIW-----------QLSGGMRQRVGIARALAA 151

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 8928549  626 DPPVILYDEATSSLDSITEETILGAMKDVVK--HRTSIFIAHRL-STVVDADEIIVLD--QGKVAER 687
Cdd:COG4525 152 DPRFLLMDEPFGALDALTREQMQELLLDVWQrtGKGVFLITHSVeEALFLATRLVVMSpgPGRIVER 218
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
 459-684 1.17e-19

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 89.35  E-value: 1.17e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   459 MASPLQITPQTAtVAFDNVHFEYIEgQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIyLAGQniqd 538
Cdd:PRK11247   1 MMNTARLNQGTP-LLLNAVSKRYGE-RTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGT---- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   539 VSLESLRRAVGVVPQDAVLFH-NTIYYNL---LYGNISASPEEVYAVAKLAglhdailrmphgydTQVGERGLKLSGGEK 614
Cdd:PRK11247  74 APLAEAREDTRLMFQDARLLPwKKVIDNVglgLKGQWRDAALQALAAVGLA--------------DRANEWPAALSGGQK 139

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 8928549   615 QRVAIARAILKDPPVILYDEATSSLDSITE-EtilgaMKDVVK------HRTSIFIAHRLSTVVD-ADEIIVLDQGKV 684
Cdd:PRK11247 140 QRVALARALIHRPGLLLLDEPLGALDALTRiE-----MQDLIEslwqqhGFTVLLVTHDVSEAVAmADRVLLIEEGKI 212
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
 474-684 1.27e-19

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 92.82  E-value: 1.27e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  474 FDNVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQniqdvslesLRraVGVVPQ 553
Cdd:COG0488   1 LENLSKSF-GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG---------LR--IGYLPQ 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  554 DAVLF-HNTIYYNLLYGN------------ISASPEEVYAV-AKLAGLHDAILRMpHGY--------------------D 599
Cdd:COG0488  69 EPPLDdDLTVLDTVLDGDaelraleaeleeLEAKLAEPDEDlERLAELQEEFEAL-GGWeaearaeeilsglgfpeedlD 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  600 TQVGErglkLSGGEKQRVAIARAILKDPPVILYDEATSSLD--SIT--EETIL---GAMkdvvkhrtsIFIAH-R--LST 669
Cdd:COG0488 148 RPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDleSIEwlEEFLKnypGTV---------LVVSHdRyfLDR 214

                       250
                ....*....|....*
gi 8928549  670 VVdaDEIIVLDQGKV 684
Cdd:COG0488 215 VA--TRILELDRGKL 227
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
 486-696 1.28e-19

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 90.15  E-value: 1.28e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   486 KVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSI------------------YLAGQNIQDV------SL 541
Cdd:PRK13651  21 KALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekekVLEKLVIQKTrfkkikKI 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   542 ESLRRAVGVVPQDA--VLFHNTIYYNLLYGNIS--ASPEEVYAVAK----LAGLHDAIL-RMPHGydtqvgerglkLSGG 612
Cdd:PRK13651 101 KEIRRRVGVVFQFAeyQLFEQTIEKDIIFGPVSmgVSKEEAKKRAAkyieLVGLDESYLqRSPFE-----------LSGG 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   613 EKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKH-RTSIFIAHRLSTVVD-ADEIIVLDQGKVAERGTH 690
Cdd:PRK13651 170 QKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQgKTIILVTHDLDNVLEwTKRTIFFKDGKIIKDGDT 249


                 ....*.
gi 8928549   691 HGLLAN 696
Cdd:PRK13651 250 YDILSD 255
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
 491-702 1.34e-19

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 93.38  E-value: 1.34e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   491 ISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS---LESLRRAVGVVPQD--AVLF-HNTIYY 564
Cdd:PRK10261 343 VSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDpyASLDpRQTVGD 422

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   565 ---------NLLYGNisASPEEVYAVAKLAGLH-DAILRMPHGYdtqvgerglklSGGEKQRVAIARAILKDPPVILYDE 634
Cdd:PRK10261 423 simeplrvhGLLPGK--AAAARVAWLLERVGLLpEHAWRYPHEF-----------SGGQRQRICIARALALNPKVIIADE 489

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 8928549   635 ATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGLLANPHSIYS 702
Cdd:PRK10261 490 AVSALDVSIRGQIINLLLDLQRDFgiAYLFISHDMAVVERiSHRVAVMYLGQIVEIGPRRAVFENPQHPYT 560
ABC_6TM_exporter_like cd18564
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
 141-436 1.61e-19

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


Pssm-ID: 350008 [Multi-domain]  Cd Length: 307  Bit Score: 89.88  E-value: 1.61e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  141 AISLGFLGGAKAMNIVVPFMFKYAVDS------LNQMSGNMLNLSDAPNTVATMATAVLIGYGVSRAGAAFFNEVrnaVF 214
Cdd:cd18564   2 ALALLALLLETALRLLEPWPLKVVIDDvlgdkpLPGLLGLAPLLGPDPLALLLLAAAALVGIALLRGLASYAGTY---LT 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  215 GKVAQNSIRRIAKNVFLHLHNLDLGFHLSRQTGALskaIDRGTRGISFVLSALVFNLLPI---------MFEVMLVsgvl 285
Cdd:cd18564  79 ALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDL---LSRLTGDVGAIQDLLVSGVLPLltnlltlvgMLGVMFW---- 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  286 yykCGAQFALVTLGTLgtyTAFTVAVTRWRTRFRIEMNKADNDAGN-AAI--DSLLNYETVKYFNNERYEAQRYDGFLKT 362
Cdd:cd18564 152 ---LDWQLALIALAVA---PLLLLAARRFSRRIKEASREQRRREGAlASVaqESLSAIRVVQAFGREEHEERRFARENRK 225

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 8928549  363 YETASLKSTSTLAMLNFGQSAIFSVGLTAIMVLASQGIVAGTLTVGDLvmvngLLFqlslpLNFLGTVYRETRQ 436
Cdd:cd18564 226 SLRAGLRAARLQALLSPVVDVLVAVGTALVLWFGAWLVLAGRLTPGDL-----LVF-----LAYLKNLYKPVRD 289
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
470-688 1.93e-19

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 90.86  E-value: 1.93e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   470 ATVAFDNVHFEYieGQKVLS-GISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVslESLRRAV 548
Cdd:PRK11000   2 ASVTLRNVTKAY--GDVVISkDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDV--PPAERGV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   549 GVVPQDAVLF-HNTIYYNLLYGnisaspeevyavAKLAGLHDA-----------ILRMPHGYDTQVGErglkLSGGEKQR 616
Cdd:PRK11000  78 GMVFQSYALYpHLSVAENMSFG------------LKLAGAKKEeinqrvnqvaeVLQLAHLLDRKPKA----LSGGQRQR 141

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 8928549   617 VAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKH--RTSIFIAH-RLSTVVDADEIIVLDQGKVAERG 688
Cdd:PRK11000 142 VAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRlgRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVG 216
PvdE COG4615
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...
 185-696 2.00e-19

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


Pssm-ID: 443659 [Multi-domain]  Cd Length: 547  Bit Score: 92.55  E-value: 2.00e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  185 VATMATAVLIGYGVSRAGAAFFNEVRNAVFGKVAQNSIRRIAKnvflhlhnldLGFHlsRQTGALSKAIDrgtrgisfVL 264
Cdd:COG4615  59 VLLLLSRLASQLLLTRLGQHAVARLRLRLSRRILAAPLERLER----------IGAA--RLLAALTEDVR--------TI 118

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  265 SALVFNLLPIMFEVMLVSGVLYYKC--GAQFALVTLGTLGtytaFTVAVTRWRT-RFRIEMNKA--DNDAGNAAIDSL-- 337
Cdd:COG4615 119 SQAFVRLPELLQSVALVLGCLAYLAwlSPPLFLLTLVLLG----LGVAGYRLLVrRARRHLRRAreAEDRLFKHFRALle 194

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  338 ------LNYETVKYFNNERYEAQrydgfLKTYETASLKSTSTLAML-NFGQSAIFsvGLTAIMVLASQGIVAGTL-TVGD 409
Cdd:COG4615 195 gfkelkLNRRRRRAFFDEDLQPT-----AERYRDLRIRADTIFALAnNWGNLLFF--ALIGLILFLLPALGWADPaVLSG 267

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  410 LVMVngLLFqLSLPL-NFLGTV--YRETRQALIDMNTLFtlLKVDTQIKDKVMASPLQITPQTATVAFDNVHFEYIEGQK 486
Cdd:COG4615 268 FVLV--LLF-LRGPLsQLVGALptLSRANVALRKIEELE--LALAAAEPAAADAAAPPAPADFQTLELRGVTYRYPGEDG 342

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  487 ----VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNti 562
Cdd:COG4615 343 degfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFDR-- 420

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  563 yynlLYG-NISASPEEVYAVAKLaglhdaiLRMphgyDTQVGERG-----LKLSGGEKQRVAIARAILKDPPVILYDEAT 636
Cdd:COG4615 421 ----LLGlDGEADPARARELLER-------LEL----DHKVSVEDgrfstTDLSQGQRKRLALLVALLEDRPILVFDEWA 485

                       490       500       510       520       530       540       550
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  637 SSLD----SITEETILGAMKDvvKHRTSIFIAHrlstvvD------ADEIIVLDQGKVAERGTHHGLLAN 696
Cdd:COG4615 486 ADQDpefrRVFYTELLPELKA--RGKTVIAISH------DdryfdlADRVLKMDYGKLVELTGPAALAAS 547
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
 481-668 2.09e-19

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 88.29  E-value: 2.09e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   481 YIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYE--PQ---KGSIYLAGQNIQDVSLES--LRRAVGVVPQ 553
Cdd:PRK14239  14 YYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnPEvtiTGSIVYNGHNIYSPRTDTvdLRKEIGMVFQ 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   554 DAVLFHNTIYYNLLYGnisaspeevyavAKLAGLHD-AILrmphgyDTQVgERGLK------------------LSGGEK 614
Cdd:PRK14239  94 QPNPFPMSIYENVVYG------------LRLKGIKDkQVL------DEAV-EKSLKgasiwdevkdrlhdsalgLSGGQQ 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 8928549   615 QRVAIARAILKDPPVILYDEATSSLDSIT----EETILGAMKD----VVKHrtSIFIAHRLS 668
Cdd:PRK14239 155 QRVCIARVLATSPKIILLDEPTSALDPISagkiEETLLGLKDDytmlLVTR--SMQQASRIS 214
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
 459-703 2.43e-19

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 92.08  E-value: 2.43e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   459 MASPLqITPQTATVAFDNVHfeyiEGQKVLSGISFEVPAGKKVAIVGGSGSGKS----TIVRLLFR---FYePQkGSIYL 531
Cdd:PRK15134   1 MTQPL-LAIENLSVAFRQQQ----TVRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSppvVY-PS-GDIRF 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   532 AGQNIQDVSLESLRRAVGvvPQDAVLFHNTI-----YYNL---LYGNIS--------ASPEEVYAVAKLAGLHDAILRM- 594
Cdd:PRK15134  74 HGESLLHASEQTLRGVRG--NKIAMIFQEPMvslnpLHTLekqLYEVLSlhrgmrreAARGEILNCLDRVGIRQAAKRLt 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   595 --PHgydtqvgerglKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVK--HRTSIFIAHRLSTV 670
Cdd:PRK15134 152 dyPH-----------QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIV 220

                        250       260       270
                 ....*....|....*....|....*....|....
gi 8928549   671 VD-ADEIIVLDQGKVAERGTHHGLLANPHSIYSE 703
Cdd:PRK15134 221 RKlADRVAVMQNGRCVEQNRAATLFSAPTHPYTQ 254
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
 484-688 3.39e-19

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 90.67  E-value: 3.39e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   484 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAvlfhnTIY 563
Cdd:PRK09536  15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDT-----SLS 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   564 YNLlygnisaspeEVYAVAKLAglhdailRMPH--------GYDTQVGERGLK--------------LSGGEKQRVAIAR 621
Cdd:PRK09536  90 FEF----------DVRQVVEMG-------RTPHrsrfdtwtETDRAAVERAMErtgvaqfadrpvtsLSGGERQRVLLAR 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 8928549   622 AILKDPPVILYDEATSSLDSITEETILGAMKDVVKH-RTSIFIAHRLSTVVD-ADEIIVLDQGKVAERG 688
Cdd:PRK09536 153 ALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDgKTAVAAIHDLDLAARyCDELVLLADGRVRAAG 221
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
 488-688 3.50e-19

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: 87.14  E-value: 3.50e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    488 LSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSleslrravgvvPQDAVLFHNtiyYNLL 567
Cdd:TIGR01184   1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPG-----------PDRMVVFQN---YSLL 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    568 -----YGNISASPEEVYAVA------KLAGLHDAILRMPHGYDTQVGErglkLSGGEKQRVAIARAILKDPPVILYDEAT 636
Cdd:TIGR01184  67 pwltvRENIALAVDRVLPDLskserrAIVEEHIALVGLTEAADKRPGQ----LSGGMKQRVAIARALSIRPKVLLLDEPF 142

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 8928549    637 SSLDSITEETILGAMKDVVK--HRTSIFIAHRL-STVVDADEIIVLDQGKVAERG 688
Cdd:TIGR01184 143 GALDALTRGNLQEELMQIWEehRVTVLMVTHDVdEALLLSDRVVMLTNGPAANIG 197
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
 490-689 4.43e-19

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


Pssm-ID: 213232 [Multi-domain]  Cd Length: 220  Bit Score: 86.65  E-value: 4.43e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  490 GISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGqniQDVSLES--LRRAVGVVPQDAVL------FHNT 561
Cdd:cd03265  18 GVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAG---HDVVREPreVRRRIGIVFQDLSVddeltgWENL 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  562 IYYNLLYGNISAS-PEEVYAVAKLAGLHDAilrmphgYDTQVGerglKLSGGEKQRVAIARAILKDPPVILYDEATSSLD 640
Cdd:cd03265  95 YIHARLYGVPGAErRERIDELLDFVGLLEA-------ADRLVK----TYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLD 163

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 8928549  641 SITEETILGAMKDVVK-HRTSIFI-------AHRLstvvdADEIIVLDQGKVAERGT 689
Cdd:cd03265 164 PQTRAHVWEYIEKLKEeFGMTILLtthymeeAEQL-----CDRVAIIDHGRIIAEGT 215
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
 488-684 8.59e-19

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 90.09  E-value: 8.59e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  488 LSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGqniQDVSLESLRRA----VGVVPQDAVLFHN-TI 562
Cdd:COG3845  21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDG---KPVRIRSPRDAialgIGMVHQHFMLVPNlTV 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  563 YYNLLYG---------NISASPEEVYAVAKLAGLH---DAIlrmphgydtqVGErglkLSGGEKQRVAIARAILKDPPVI 630
Cdd:COG3845  98 AENIVLGleptkggrlDRKAARARIRELSERYGLDvdpDAK----------VED----LSVGEQQRVEILKALYRGARIL 163

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 8928549  631 LYDEATSSLdsiT-EET-----ILGAMKDvvKHRTSIFIAHRLSTVVD-ADEIIVLDQGKV 684
Cdd:COG3845 164 ILDEPTAVL---TpQEAdelfeILRRLAA--EGKSIIFITHKLREVMAiADRVTVLRRGKV 219
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
453-690 1.17e-18

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 87.96  E-value: 1.17e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   453 QIKDKVMASPLQITPQTAtVAFDNVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLA 532
Cdd:PRK13536  24 QGISEAKASIPGSMSTVA-IDLAGVSKSY-GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVL 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   533 GQNIQDVSlESLRRAVGVVPQ-DAVLFHNTIYYNLL-YGN-ISASPEEVYAVakLAGLHDaILRMPHGYDTQVGErglkL 609
Cdd:PRK13536 102 GVPVPARA-RLARARIGVVPQfDNLDLEFTVRENLLvFGRyFGMSTREIEAV--IPSLLE-FARLESKADARVSD----L 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   610 SGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFI-------AHRLstvvdADEIIVLDQG 682
Cdd:PRK13536 174 SGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLtthfmeeAERL-----CDRLCVLEAG 248


                 ....*....
gi 8928549   683 -KVAERGTH 690
Cdd:PRK13536 249 rKIAEGRPH 257
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
 488-689 1.29e-18

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


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 90.11  E-value: 1.29e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    488 LSGISFEVPAGKKVAIVGGSGSGKSTIVRLLfRFYEPQ----KGSIYLAGQNIQdvsLESLRRAVGVVPQDAVLF-HNTI 562
Cdd:TIGR00955  41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNAL-AFRSPKgvkgSGSVLLNGMPID---AKEMRAISAYVQQDDLFIpTLTV 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    563 YYNLLYGNISASPEEVYAVAKLAGLHDAILRMPHG--YDTQVGERGLK--LSGGEKQRVAIARAILKDPPVILYDEATSS 638
Cdd:TIGR00955 117 REHLMFQAHLRMPRRVTKKEKRERVDEVLQALGLRkcANTRIGVPGRVkgLSGGERKRLAFASELLTDPPLLFCDEPTSG 196

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 8928549    639 LDSITEETILGAMKDVV-KHRTSIFIAHRLSTVVDA--DEIIVLDQGKVAERGT 689
Cdd:TIGR00955 197 LDSFMAYSVVQVLKGLAqKGKTIICTIHQPSSELFElfDKIILMAEGRVAYLGS 250
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
 486-684 1.39e-18

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: 85.02  E-value: 1.39e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  486 KVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDvsleSLRRAVGVVPQDAVLFHN-TIYY 564
Cdd:cd03269  14 TALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDI----AARNRIGYLPEERGLYPKmKVID 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  565 NLLYgnisaspeevyaVAKLAGL-HDAILRMPHGYDTQVGERGLK------LSGGEKQRVAIARAILKDPPVILYDEATS 637
Cdd:cd03269  90 QLVY------------LAQLKGLkKEEARRRIDEWLERLELSEYAnkrveeLSKGNQQKVQFIAAVIHDPELLILDEPFS 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 8928549  638 SLDSITEETILGAMKDVV-KHRTSIFIAHRLSTVVD-ADEIIVLDQGKV 684
Cdd:cd03269 158 GLDPVNVELLKDVIRELArAGKTVILSTHQMELVEElCDRVLLLNKGRA 206
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
 484-682 1.40e-18

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: 91.13  E-value: 1.40e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549     484 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQniqdvsleslrraVGVVPQDAVLFHNTIY 563
Cdd:TIGR01271  438 VTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQTSWIMPGTIK 504

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549     564 YNLLYGnISASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSIT 643
Cdd:TIGR01271  505 DNIIFG-LSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVT 583

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 8928549     644 EETIL-GAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQG 682
Cdd:TIGR01271  584 EKEIFeSCLCKLMSNKTRILVTSKLEHLKKADKILLLHEG 623
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
 487-689 1.81e-18

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


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 85.52  E-value: 1.81e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  487 VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQniqdVS--LEslrraVGVVpqdavlFH----- 559
Cdd:COG1134  41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR----VSalLE-----LGAG------FHpeltg 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  560 --NtIYYN-LLYGNISASPEEVYA-VAKLAGLHDAIlrmphgyDTQVGerglKLSGGEKQRVAIARAILKDPPVILYDEA 635
Cdd:COG1134 106 reN-IYLNgRLLGLSRKEIDEKFDeIVEFAELGDFI-------DQPVK----TYSSGMRARLAFAVATAVDPDILLVDEV 173

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 8928549  636 TSSLDSITEETILGAMKDVVKH-RTSIFIAHRLSTVVD-ADEIIVLDQGKVAERGT 689
Cdd:COG1134 174 LAVGDAAFQKKCLARIRELRESgRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGD 229
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
475-687 2.18e-18

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 85.52  E-value: 2.18e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   475 DNVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLEslrRAVgVVPQD 554
Cdd:PRK11248   5 SHLYADY-GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAE---RGV-VFQNE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   555 AVLFHNTIYYNLLYG----NISASPEEVYAVAKLA--GLHDAILRMPhgydtqvgergLKLSGGEKQRVAIARAILKDPP 628
Cdd:PRK11248  80 GLLPWRNVQDNVAFGlqlaGVEKMQRLEIAHQMLKkvGLEGAEKRYI-----------WQLSGGQRQRVGIARALAANPQ 148

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 8928549   629 VILYDEATSSLDSITEETilgaMKDV---VKHRTS---IFIAHRL-STVVDADEIIVL--DQGKVAER 687
Cdd:PRK11248 149 LLLLDEPFGALDAFTREQ----MQTLllkLWQETGkqvLLITHDIeEAVFMATELVLLspGPGRVVER 212
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
485-697 2.44e-18

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 85.59  E-value: 2.44e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   485 QKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS---LESLRRAVGVVPQDAVLFHN- 560
Cdd:PRK11831  20 RCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSrsrLYTVRKRMSMLFQSGALFTDm 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   561 TIYYNLLYG--NISASPEEVY---AVAKL--AGLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARAILKDPPVILYD 633
Cdd:PRK11831 100 NVFDNVAYPlrEHTQLPAPLLhstVMMKLeaVGLRGAAKLMPS-----------ELSGGMARRAALARAIALEPDLIMFD 168

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 8928549   634 EATSSLDSITeETILGAMKDVVKHR---TSIFIAHRLSTVVD-AD-EIIVLDQGKVAErGTHHGLLANP 697
Cdd:PRK11831 169 EPFVGQDPIT-MGVLVKLISELNSAlgvTCVVVSHDVPEVLSiADhAYIVADKKIVAH-GSAQALQANP 235
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
 481-707 3.98e-18

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 84.89  E-value: 3.98e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   481 YIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQ-----KGSIYLAGQNI--QDVSLESLRRAVGVVPQ 553
Cdd:PRK14267  13 YYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIysPDVDPIEVRREVGMVFQ 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   554 DAVLF-HNTIYYNLLYG----NISAS----PEEVYAVAKLAGLHDAILRMPHGYDTQvgerglkLSGGEKQRVAIARAIL 624
Cdd:PRK14267  93 YPNPFpHLTIYDNVAIGvklnGLVKSkkelDERVEWALKKAALWDEVKDRLNDYPSN-------LSGGQRQRLVIARALA 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   625 KDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGLLANPHSIYSE 703
Cdd:PRK14267 166 MKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARvSDYVAFLYLGKLIEVGPTRKVFENPEHELTE 245


                 ....
gi 8928549   704 MWHT 707
Cdd:PRK14267 246 KYVT 249
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
 487-651 6.87e-18

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 82.61  E-value: 6.87e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   487 VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGvvPQDAVLFHNTIYYNL 566
Cdd:PRK13539  17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLG--HRNAMKPALTVAENL 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   567 -----LYGNisaSPEEVYAVAKLAGLHDaILRMPHGYdtqvgerglkLSGGEKQRVAIARAILKDPPVILYDEATSSLDS 641
Cdd:PRK13539  95 efwaaFLGG---EELDIAAALEAVGLAP-LAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160

                        170
                 ....*....|
gi 8928549   642 ITEETILGAM 651
Cdd:PRK13539 161 AAVALFAELI 170
cbiO PRK13643
energy-coupling factor transporter ATPase;
472-704 9.95e-18

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 84.40  E-value: 9.95e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   472 VAFDNVHFEYIE----GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS----LES 543
Cdd:PRK13643   2 IKFEKVNYTYQPnspfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeIKP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   544 LRRAVGVVPQ--DAVLFHNTIYYNLLYG--NISASPEEVYAVAKlaglhdAILRMPhGYDTQVGERG-LKLSGGEKQRVA 618
Cdd:PRK13643  82 VRKKVGVVFQfpESQLFEETVLKDVAFGpqNFGIPKEKAEKIAA------EKLEMV-GLADEFWEKSpFELSGGQMRRVA 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   619 IARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKH-RTSIFIAHRLSTVVD-ADEIIVLDQGKVAERGThhgllan 696
Cdd:PRK13643 155 IAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSgQTVVLVTHLMDDVADyADYVYLLEKGHIISCGT------- 227


                 ....*...
gi 8928549   697 PHSIYSEM 704
Cdd:PRK13643 228 PSDVFQEV 235
ABC_6TM_YknU_like cd18542
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ...
 140-428 1.16e-17

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: 84.02  E-value: 1.16e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  140 VAISLGFLGGAKAMNIVVPFMFKYAVDSLnQMSGNMLNLsdapntvaTMATAVLIGYGVSRAGAAFfneVRNAVFGKVAQ 219
Cdd:cd18542   1 YLLAILALLLATALNLLIPLLIRRIIDSV-IGGGLRELL--------WLLALLILGVALLRGVFRY---LQGYLAEKASQ 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  220 NSIRRIAKNVFLHLHNLDLGFHLSRQTGALskaIDRGT-------RGISFVLSALVFNLLpiMFevmLVSGVLYYKCGAQ 292
Cdd:cd18542  69 KVAYDLRNDLYDHLQRLSFSFHDKARTGDL---MSRCTsdvdtirRFLAFGLVELVRAVL--LF---IGALIIMFSINWK 140

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  293 FALVTLGTlgtyTAFTVAVTRW-----RTRFRI------EMNKA--DNDAGNaaidsllnyETVKYFNNERYEAQRYDGF 359
Cdd:cd18542 141 LTLISLAI----IPFIALFSYVffkkvRPAFEEireqegELNTVlqENLTGV---------RVVKAFAREDYEIEKFDKE 207

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 8928549  360 LKTYETASLKSTSTLA----MLNFgqsaIFSVGLTAIMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLG 428
Cdd:cd18542 208 NEEYRDLNIKLAKLLAkywpLMDF----LSGLQIVLVLWVGGYLVINGEITLGELVAFISYLWMLIWPVRQLG 276
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
 465-689 2.09e-17

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


Pssm-ID: 132313 [Multi-domain]  Cd Length: 520  Bit Score: 86.01  E-value: 2.09e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    465 ITPQTATVAFDnvhfeyieGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLL--FRFYEPQKGSI-----------YL 531
Cdd:TIGR03269   1 IEVKNLTKKFD--------GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIiyhvalcekcgYV 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    532 -----AGQNI---------QDVSL----ESLRRAVgvVPQDAVLFHNTIyynLLYGN-------ISASPEEVYAVAKLAG 586
Cdd:TIGR03269  73 erpskVGEPCpvcggtlepEEVDFwnlsDKLRRRI--RKRIAIMLQRTF---ALYGDdtvldnvLEALEEIGYEGKEAVG 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    587 LHDAILRMphgydTQVGER----GLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHR--TS 660
Cdd:TIGR03269 148 RAVDLIEM-----VQLSHRithiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgiSM 222

                         250       260       270
                  ....*....|....*....|....*....|
gi 8928549    661 IFIAHRLSTVVD-ADEIIVLDQGKVAERGT 689
Cdd:TIGR03269 223 VLTSHWPEVIEDlSDKAIWLENGEIKEEGT 252
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
 476-688 2.49e-17

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: 81.03  E-value: 2.49e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  476 NVHFEyIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRF--YEPQKGSIYLAGQNIQDVSL-ESLRRAVGVVP 552
Cdd:cd03217   5 DLHVS-VGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPeERARLGIFLAF 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  553 QdavlfhntiyynllygnisaSPEEVYAVaKLAGLhdaiLRmphgydtQVGErglKLSGGEKQRVAIARAILKDPPVILY 632
Cdd:cd03217  84 Q--------------------YPPEIPGV-KNADF----LR-------YVNE---GFSGGEKKRNEILQLLLLEPDLAIL 128

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 8928549  633 DEATSSLD----SITEETIlGAMKDvvKHRTSIFIAH--RLSTVVDADEIIVLDQGKVAERG 688
Cdd:cd03217 129 DEPDSGLDidalRLVAEVI-NKLRE--EGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSG 187
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
 470-698 2.60e-17

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 81.86  E-value: 2.60e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   470 ATVAFDNVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSL-ESLRRAV 548
Cdd:PRK10895   2 ATLTAKNLAKAY-KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhARARRGI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   549 GVVPQDAVLFHN-TIYYNLL-----YGNISASPEEVYAVAKLAGLHDAILRmphgydtqvGERGLKLSGGEKQRVAIARA 622
Cdd:PRK10895  81 GYLPQEASIFRRlSVYDNLMavlqiRDDLSAEQREDRANELMEEFHIEHLR---------DSMGQSLSGGERRRVEIARA 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   623 ILKDPPVILYDEATSSLDSITEETIlgamKDVVKH-RTS----IFIAHRLSTVVDADE-IIVLDQGKVAERGTHHGLLAN 696
Cdd:PRK10895 152 LAANPKFILLDEPFAGVDPISVIDI----KRIIEHlRDSglgvLITDHNVRETLAVCErAYIVSQGHLIAHGTPTEILQD 227


                 ..
gi 8928549   697 PH 698
Cdd:PRK10895 228 EH 229
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
 487-688 2.85e-17

ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.


Pssm-ID: 213187 [Multi-domain]  Cd Length: 224  Bit Score: 81.42  E-value: 2.85e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  487 VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGqniQDVSLesLRRAVGVVPqDAVLFHNTIYYNL 566
Cdd:cd03220  37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG---RVSSL--LGLGGGFNP-ELTGRENIYLNGR 110

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  567 LYGnisASPEEVYA----VAKLAGLHDAIlrmphgyDTQVGErglkLSGGEKQRVAIARAILKDPPVILYDEATSSLDSI 642
Cdd:cd03220 111 LLG---LSRKEIDEkideIIEFSELGDFI-------DLPVKT----YSSGMKARLAFAIATALEPDILLIDEVLAVGDAA 176

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 8928549  643 TEETILGAMKDVVKH-RTSIFIAHRLSTVVD-ADEIIVLDQGKVAERG 688
Cdd:cd03220 177 FQEKCQRRLRELLKQgKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
468-688 3.73e-17

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 82.24  E-value: 3.73e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   468 QTATVAFDNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLrra 547
Cdd:PRK15056   3 QQAGIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL--- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   548 VGVVPQD-------AVLFHNTIYYNlLYGnisaspeevyavaklaglHDAILRMPHGYDTQVGERGL------------- 607
Cdd:PRK15056  80 VAYVPQSeevdwsfPVLVEDVVMMG-RYG------------------HMGWLRRAKKRDRQIVTAALarvdmvefrhrqi 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   608 -KLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKH-RTSIFIAHRLSTVVDADEIIVLDQGKVA 685
Cdd:PRK15056 141 gELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEgKTMLVSTHNLGSVTEFCDYTVMVKGTVL 220


                 ...
gi 8928549   686 ERG 688
Cdd:PRK15056 221 ASG 223
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
 474-683 4.62e-17

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


Pssm-ID: 213188 [Multi-domain]  Cd Length: 144  Bit Score: 78.64  E-value: 4.62e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  474 FDNVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIyLAGQNIQdvsleslrraVGVVPQ 553
Cdd:cd03221   3 LENLSKTY-GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV-TWGSTVK----------IGYFEQ 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  554 davlfhntiyynllygnisaspeevyavaklaglhdailrmphgydtqvgerglkLSGGEKQRVAIARAILKDPPVILYD 633
Cdd:cd03221  71 -------------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLD 95

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 8928549  634 EATSSLDSITEETILGAMKDvvKHRTSIFIAH-R--LSTVvdADEIIVLDQGK 683
Cdd:cd03221  96 EPTNHLDLESIEALEEALKE--YPGTVILVSHdRyfLDQV--ATKIIELEDGK 144
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
 486-697 4.81e-17

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: 81.05  E-value: 4.81e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  486 KVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSL-ESLRRAVGVVPQDAVLFHN-TIY 563
Cdd:cd03218  14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMhKRARLGIGYLPQEASIFRKlTVE 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  564 YNLLygnisaspeevyAVAKLAGLHDAILRmpHGYDTQVGE---------RGLKLSGGEKQRVAIARAILKDPPVILYDE 634
Cdd:cd03218  94 ENIL------------AVLEIRGLSKKERE--EKLEELLEEfhithlrksKASSLSGGERRRVEIARALATNPKFLLLDE 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 8928549  635 ATSSLDSITEETILGAMKDVVKHRTSIFIA-HRLSTVVD-ADEIIVLDQGKVAERGTHHGLLANP 697
Cdd:cd03218 160 PFAGVDPIAVQDIQKIIKILKDRGIGVLITdHNVRETLSiTDRAYIIYEGKVLAEGTPEEIAANE 224
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
491-697 5.79e-17

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 81.76  E-value: 5.79e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   491 ISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQ--DVSLESLRraVGVVPQDAVLFHN------TI 562
Cdd:PRK15112  32 LSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDYSYRSQR--IRMIFQDPSTSLNprqrisQI 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   563 YYNLLYGNISASPEE----VYAVAKLAGL-HDAILRMPHgydtqvgerglKLSGGEKQRVAIARAILKDPPVILYDEATS 637
Cdd:PRK15112 110 LDFPLRLNTDLEPEQrekqIIETLRQVGLlPDHASYYPH-----------MLAPGQKQRLGLARALILRPKVIIADEALA 178

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 8928549   638 SLDSITEETILGAMKDVV-KHRTS-IFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGLLANP 697
Cdd:PRK15112 179 SLDMSMRSQLINLMLELQeKQGISyIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVLASP 241
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
 472-686 7.44e-17

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 84.35  E-value: 7.44e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  472 VAFDNVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLaGQNIQdvsleslrraVGVV 551
Cdd:COG0488 316 LELEGLSKSY-GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK----------IGYF 383

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  552 PQDAVLFH--NTIYYNLLYGNISASPEEVYAVakLAGL----HDAilrmphgyDTQVGerglKLSGGEKQRVAIARAILK 625
Cdd:COG0488 384 DQHQEELDpdKTVLDELRDGAPGGTEQEVRGY--LGRFlfsgDDA--------FKPVG----VLSGGEKARLALAKLLLS 449

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 8928549  626 DPPVILYDEATSSLD--SIT--EETIL---GAMkdvvkhrtsIFIAH-R--LSTVvdADEIIVLDQGKVAE 686
Cdd:COG0488 450 PPNVLLLDEPTNHLDieTLEalEEALDdfpGTV---------LLVSHdRyfLDRV--ATRILEFEDGGVRE 509
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
 482-684 8.68e-17

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: 79.01  E-value: 8.68e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  482 IEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS-LESLRRAVGVVPQD---AVL 557
Cdd:cd03215  10 LSVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSpRDAIRAGIAYVPEDrkrEGL 89

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  558 FHN-TIYYNLLYGNIsaspeevyavaklaglhdailrmphgydtqvgerglkLSGGEKQRVAIARAILKDPPVILYDEAT 636
Cdd:cd03215  90 VLDlSVAENIALSSL-------------------------------------LSGGNQQKVVLARWLARDPRVLILDEPT 132

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 8928549  637 SSLDSITEETILGAMKDVVKHRTSIFIahrLSTVVD-----ADEIIVLDQGKV 684
Cdd:cd03215 133 RGVDVGAKAEIYRLIRELADAGKAVLL---ISSELDellglCDRILVMYEGRI 182
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
 484-697 9.80e-17

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 81.30  E-value: 9.80e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   484 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEP-----QKGSIYLAGQNI---QDVsLEsLRRAVGVVPQDA 555
Cdd:PRK14271  33 GKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIfnyRDV-LE-FRRRVGMLFQRP 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   556 VLFHNTIYYNLLYGNISAS--PEEVY---AVAKLA--GLHDAIlrmphgyDTQVGERGLKLSGGEKQRVAIARAILKDPP 628
Cdd:PRK14271 111 NPFPMSIMDNVLAGVRAHKlvPRKEFrgvAQARLTevGLWDAV-------KDRLSDSPFRLSGGQQQLLCLARTLAVNPE 183

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   629 VILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGLLANP 697
Cdd:PRK14271 184 VLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLFSSP 253
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 484-689 1.32e-16

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


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 80.92  E-value: 1.32e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  484 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDvsleSLRRAVGvvpqdavlfhntiY 563
Cdd:COG4152  13 DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDP----EDRRRIG-------------Y 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  564 ynL-----LYGNISASpEEVYAVAKLAGL--HDAILRMPHGYDT-QVGERGLK----LSGGEKQRVAIARAILKDPPVIL 631
Cdd:COG4152  76 --LpeergLYPKMKVG-EQLVYLARLKGLskAEAKRRADEWLERlGLGDRANKkveeLSKGNQQKVQLIAALLHDPELLI 152

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 8928549  632 YDEATSSLDSITEETilgaMKDVVKH-----RTSIFIAHRLSTVVD-ADEIIVLDQGKVAERGT 689
Cdd:COG4152 153 LDEPFSGLDPVNVEL----LKDVIRElaakgTTVIFSSHQMELVEElCDRIVIINKGRKVLSGS 212
ABC_6TM_bac_exporter_ABCB8_10_like cd18576
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ...
 143-438 1.45e-16

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: 80.99  E-value: 1.45e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  143 SLGFLGGAKAMNIVVPFMFKYAVDSLNQmSGNMLNLsdapNTVATMATAVLigygVSRAGAAFFnevRNAVFGKVAQNSI 222
Cdd:cd18576   1 GLILLLLSSAIGLVFPLLAGQLIDAALG-GGDTASL----NQIALLLLGLF----LLQAVFSFF---RIYLFARVGERVV 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  223 RRIAKNVFLHLHNLDLGFHLSRQTGALSKaidRGTRGISFVLSALVFNLLPIMFEVMLVSG--VLYYKCGAQFALVTLGT 300
Cdd:cd18576  69 ADLRKDLYRHLQRLPLSFFHERRVGELTS---RLSNDVTQIQDTLTTTLAEFLRQILTLIGgvVLLFFISWKLTLLMLAT 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  301 LGTYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNERYEAQRYDGFLKTYETASLKSTSTLAMLNFG 380
Cdd:cd18576 146 VPVVVLVAVLFGRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSF 225

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 8928549  381 QSAIFSVGLTAIMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQAL 438
Cdd:cd18576 226 IIFLLFGAIVAVLWYGGRLVLAGELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKAL 283
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
468-704 1.60e-16

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 83.04  E-value: 1.60e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   468 QTATVAFDNVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSL-ESLRR 546
Cdd:PRK11288   1 SSPYLSFDGIGKTF-PGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTtAALAA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   547 AVGVVPQDAVLFHN-TIYYNLLYGNISASPEEV-------YAVAKLAGLHDAIlrMPhgyDTQVGErglkLSGGEKQRVA 618
Cdd:PRK11288  80 GVAIIYQELHLVPEmTVAENLYLGQLPHKGGIVnrrllnyEAREQLEHLGVDI--DP---DTPLKY----LSIGQRQMVE 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   619 IARAILKDPPVILYDEATSSLdSITEETIL----GAMKDvvKHRTSIFIAHRLSTVVD-ADEIIVLDQGKVAErgTHHGL 693
Cdd:PRK11288 151 IAKALARNARVIAFDEPTSSL-SAREIEQLfrviRELRA--EGRVILYVSHRMEEIFAlCDAITVFKDGRYVA--TFDDM 225

                        250
                 ....*....|..
gi 8928549   694 LANPH-SIYSEM 704
Cdd:PRK11288 226 AQVDRdQLVQAM 237
BtuD COG4138
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ...
 488-689 1.66e-16

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


Pssm-ID: 443313 [Multi-domain]  Cd Length: 248  Bit Score: 79.88  E-value: 1.66e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  488 LSGISFEVPAGKKVAIVGGSGSGKSTivrLLFRF--YEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVL------FH 559
Cdd:COG4138  12 LGPISAQVNAGELIHLIGPNGAGKST---LLARMagLLPGQGEILLNGRPLSDWSAAELARHRAYLSQQQSPpfampvFQ 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  560 ntiyYNLLYGNISASPEEV-YAVAKLA---GLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARAILKDPPVI----- 630
Cdd:COG4138  89 ----YLALHQPAGASSEAVeQLLAQLAealGLEDKLSRPLT-----------QLSGGEWQRVRLAAVLLQVWPTInpegq 153

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 8928549  631 --LYDEATSSLDsITEETilgAMKDVVKH-----RTSIFIAHRLS-TVVDADEIIVLDQGKVAERGT 689
Cdd:COG4138 154 llLLDEPMNSLD-VAQQA---ALDRLLRElcqqgITVVMSSHDLNhTLRHADRVWLLKQGKLVASGE 216
ABC_6TM_exporter_like cd18563
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
 140-438 1.86e-16

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: 80.63  E-value: 1.86e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  140 VAISLGFLGGAKAMNIVVPFMFKYAVDSLNQMSGNMLNLSDAPNTVATMAtavligygVSRAGAAFFNEVRNAVFGKVAQ 219
Cdd:cd18563   1 LILGFLLMLLGTALGLVPPYLTKILIDDVLIQLGPGGNTSLLLLLVLGLA--------GAYVLSALLGILRGRLLARLGE 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  220 NSIRRIAKNVFLHLHNLDLGFHLSRQTGALskaIDRGTRG-------ISFVLSALVFNLLPIMFevmlVSGVLYYkCGAQ 292
Cdd:cd18563  73 RITADLRRDLYEHLQRLSLSFFDKRQTGSL---MSRVTSDtdrlqdfLSDGLPDFLTNILMIIG----IGVVLFS-LNWK 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  293 FALVTLGTLgtytAFTVAVTRW---RTRFRIEMNKADNDAGNAAI-DSLLNYETVKYFNNERYEAQRYDGFLKTYETASL 368
Cdd:cd18563 145 LALLVLIPV----PLVVWGSYFfwkKIRRLFHRQWRRWSRLNSVLnDTLPGIRVVKAFGQEKREIKRFDEANQELLDANI 220

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  369 KSTSTLAMLNFGQSAIFSVGLTAIMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQAL 438
Cdd:cd18563 221 RAEKLWATFFPLLTFLTSLGTLIVWYFGGRQVLSGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRAL 290
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
464-689 6.57e-16

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 78.29  E-value: 6.57e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   464 QITPQTATVAFDNVHFEyIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLES 543
Cdd:PRK10575   4 YTNHSDTTFALRNVSFR-VPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   544 LRRAVGVVPQDavlfhntiyynlLYGNISASPEEVYAVAKLAgLHDAILRMPHGYDTQVGER----GLK---------LS 610
Cdd:PRK10575  83 FARKVAYLPQQ------------LPAAEGMTVRELVAIGRYP-WHGALGRFGAADREKVEEAislvGLKplahrlvdsLS 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   611 GGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLSTVVD-ADEIIVLDQGKVAER 687
Cdd:PRK10575 150 GGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERglTVIAVLHDINMAARyCDYLVALRGGEMIAQ 229


                 ..
gi 8928549   688 GT 689
Cdd:PRK10575 230 GT 231
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
 482-699 9.48e-16

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 77.82  E-value: 9.48e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   482 IEGQKVL-SGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPqkGSIYLAGQNIQD---VSLESLR-RAVGVV---PQ 553
Cdd:PRK10418  12 LQAAQPLvHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPA--GVRQTAGRVLLDgkpVAPCALRgRKIATImqnPR 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   554 DAvlfhntiyYNLLYGNISASPEEVYAVAKLAglHDAilRMPHGYDtQVG----ERGLKL-----SGGEKQRVAIARAIL 624
Cdd:PRK10418  90 SA--------FNPLHTMHTHARETCLALGKPA--DDA--TLTAALE-AVGlenaARVLKLypfemSGGMLQRMMIALALL 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 8928549   625 KDPPVILYDEATSSLDSITEETILGAMKDVVKHRTS--IFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGLLANPHS 699
Cdd:PRK10418 157 CEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALgmLLVTHDMGVVARlADDVAVMSHGRIVEQGDVETLFNAPKH 234
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
 487-684 1.03e-15

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: 77.37  E-value: 1.03e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  487 VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRaVGVV------------PQD 554
Cdd:cd03267  36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRR-IGVVfgqktqlwwdlpVID 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  555 AVLFHNTIYynllygNIsaspEEVYAVAKLAGLHDaILRMPHGYDTQVgeRglKLSGGEKQRVAIARAILKDPPVILYDE 634
Cdd:cd03267 115 SFYLLAAIY------DL----PPARFKKRLDELSE-LLDLEELLDTPV--R--QLSLGQRMRAEIAAALLHEPEILFLDE 179

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 8928549  635 ATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLSTVVD-ADEIIVLDQGKV 684
Cdd:cd03267 180 PTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEAlARRVLVIDKGRL 232
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
 486-704 1.16e-15

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


Pssm-ID: 132313 [Multi-domain]  Cd Length: 520  Bit Score: 80.62  E-value: 1.16e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    486 KVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIY-LAGQNIQDVS----LESLR--RAVGVVPQDAVLF 558
Cdd:TIGR03269 298 KAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvRVGDEWVDMTkpgpDGRGRakRYIGILHQEYDLY 377

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    559 -HNTIYYNLLYGNISASPEE------VYaVAKLAGLHD----AIL-RMPHgydtqvgerglKLSGGEKQRVAIARAILKD 626
Cdd:TIGR03269 378 pHRTVLDNLTEAIGLELPDElarmkaVI-TLKMVGFDEekaeEILdKYPD-----------ELSEGERHRVALAQVLIKE 445

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    627 PPVILYDEATSSLDSITE----ETILGAMKDVvkHRTSIFIAHRLSTVVD-ADEIIVLDQGKVAERGthhgllaNPHSIY 701
Cdd:TIGR03269 446 PRIVILDEPTGTMDPITKvdvtHSILKAREEM--EQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIG-------DPEEIV 516


                  ...
gi 8928549    702 SEM 704
Cdd:TIGR03269 517 EEL 519
PRK10522 PRK10522
multidrug transporter membrane component/ATP-binding component; Provisional
 471-686 2.45e-15

multidrug transporter membrane component/ATP-binding component; Provisional


Pssm-ID: 236707 [Multi-domain]  Cd Length: 547  Bit Score: 79.63  E-value: 2.45e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   471 TVAFDNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGV 550
Cdd:PRK10522 322 TLELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSA 401

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   551 VPQDAVLFHNTIyynllygnisaSPEEVYAVAKLAGLHDAILRMPHGYDTQVGE-RGLKLSGGEKQRVAIARAILKDPPV 629
Cdd:PRK10522 402 VFTDFHLFDQLL-----------GPEGKPANPALVEKWLERLKMAHKLELEDGRiSNLKLSKGQKKRLALLLALAEERDI 470

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 8928549   630 ILYDEATSSLD----SITEETILGAMKDVVKhrTSIFIAHRLSTVVDADEIIVLDQGKVAE 686
Cdd:PRK10522 471 LLLDEWAADQDphfrREFYQVLLPLLQEMGK--TIFAISHDDHYFIHADRLLEMRNGQLSE 529
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
468-696 3.60e-15

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


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 75.69  E-value: 3.60e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   468 QTATVAFDNVHFEYIEGQkVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQD-VSLESLRR 546
Cdd:PRK11614   2 EKVMLSFDKVSAHYGKIQ-ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDwQTAKIMRE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   547 AVGVVPQDAVLFHN-TIYYNLLYGNISASPEEVYA-VAKLAGLhdailrMPHGYDTQVgERGLKLSGGEKQRVAIARAIL 624
Cdd:PRK11614  81 AVAIVPEGRRVFSRmTVEENLAMGGFFAERDQFQErIKWVYEL------FPRLHERRI-QRAGTMSGGEQQMLAIGRALM 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 8928549   625 KDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLS--TVVDADEIIVLDQGKVAERGTHHGLLAN 696
Cdd:PRK11614 154 SQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNAnqALKLADRGYVLENGHVVLEDTGDALLAN 227
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
 502-689 4.22e-15

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: 80.06  E-value: 4.22e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549     502 AIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQdVSLESLRRAVGVVPQDAVLFHNTIY--YNLLYGNISASPEEVY 579
Cdd:TIGR01257  960 AFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIE-TNLDAVRQSLGMCPQHNILFHHLTVaeHILFYAQLKGRSWEEA 1038

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549     580 AVAKLAGLHDAilrmphGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRT 659
Cdd:TIGR01257 1039 QLEMEAMLEDT------GLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRT 1112

                          170       180       190
                   ....*....|....*....|....*....|.
gi 8928549     660 SIFIAHRLSTV-VDADEIIVLDQGKVAERGT 689
Cdd:TIGR01257 1113 IIMSTHHMDEAdLLGDRIAIISQGRLYCSGT 1143
ABC_6TM_MsbA_like cd18552
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ...
 140-438 6.06e-15

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


Pssm-ID: 349996 [Multi-domain]  Cd Length: 292  Bit Score: 75.92  E-value: 6.06e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  140 VAISLGFLGGAKAMNIVVPFMFKYAVDSLNQmsgnmlnlSDAPNTVATMATAVLIGYGVsRAGAAFFNEVrnaVFGKVAQ 219
Cdd:cd18552   1 LALAILGMILVAATTAALAWLLKPLLDDIFV--------EKDLEALLLVPLAIIGLFLL-RGLASYLQTY---LMAYVGQ 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  220 NSIRRIAKNVFLHLHNLDLGFHLSRQTGAL-SKA---IDRGTRGISFVLSALVFNLLPIMFevmLVSGVLYYkcGAQFAL 295
Cdd:cd18552  69 RVVRDLRNDLFDKLLRLPLSFFDRNSSGDLiSRItndVNQVQNALTSALTVLVRDPLTVIG---LLGVLFYL--DWKLTL 143

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  296 VTLGTLGtytAFTVAVTRWRTRFRIEMNKADNDAGN---AAIDSLLNYETVKYFNNERYEAQRYDGFLKTYETASLKSTS 372
Cdd:cd18552 144 IALVVLP---LAALPIRRIGKRLRKISRRSQESMGDltsVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIAR 220

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 8928549  373 TLAMLNFGQSAIFSVGLTAIMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQAL 438
Cdd:cd18552 221 ARALSSPLMELLGAIAIALVLWYGGYQVISGELTPGEFISFITALLLLYQPIKRLSNVNANLQRGL 286
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
 472-666 1.11e-14

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: 72.19  E-value: 1.11e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  472 VAFDNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGqniqdvsleslRRAVGVV 551
Cdd:cd03223   1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPE-----------GEDLLFL 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  552 PQDAvlfhntiYYNLlyGNisaspeevyavaklagLHDAILRmPHGydtqvgergLKLSGGEKQRVAIARAILKDPPVIL 631
Cdd:cd03223  70 PQRP-------YLPL--GT----------------LREQLIY-PWD---------DVLSGGEQQRLAFARLLLHKPKFVF 114

                       170       180       190
                ....*....|....*....|....*....|....*
gi 8928549  632 YDEATSSLDSITEETILGAMKDvvKHRTSIFIAHR 666
Cdd:cd03223 115 LDEATSALDEESEDRLYQLLKE--LGITVISVGHR 147
ABC_6TM_TAP_ABCB8_10_like cd18557
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ...
 144-438 2.31e-14

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: 74.13  E-value: 2.31e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  144 LGFLGGAKAMNIVVPFMFKYAVDSLNQMSGnmlnlSDAPNTVATMATAVLIGYGVsragaafFNEVRNAVFGKVAQNSIR 223
Cdd:cd18557   2 LLFLLISSAAQLLLPYLIGRLIDTIIKGGD-----LDVLNELALILLAIYLLQSV-------FTFVRYYLFNIAGERIVA 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  224 RIAKNVFLHLHNLDLGFHLSRQTGALskaIDRGTRGISFVLSALVFNLLPIMFEVMLVSGVLY--YKCGAQFALVTLGTL 301
Cdd:cd18557  70 RLRRDLFSSLLRQEIAFFDKHKTGEL---TSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIilFILSWKLTLVLLLVI 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  302 GTYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNERYEAQRYDGFLKTYETASLKSTSTLAMLNFGQ 381
Cdd:cd18557 147 PLLLIASKIYGRYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGIT 226

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 8928549  382 SAIFSVGLTAIMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQAL 438
Cdd:cd18557 227 SLLIYLSLLLVLWYGGYLVLSGQLTVGELTSFILYTIMVASSVGGLSSLLADIMKAL 283
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
 442-686 2.37e-14

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


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 73.07  E-value: 2.37e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  442 NTLFTLLKVDtqikdKVMASPLQITPQTATV--AFdNVHFEYIEgQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLF 519
Cdd:COG2401   5 NPFFVLMRVT-----KVYSSVLDLSERVAIVleAF-GVELRVVE-RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLA 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  520 RFYE--PQKGSIYLAGQNI-QDVSLeslrravgvvpQDAVLfhntiyynllygnISASPEEVYAVAKLAGLHDAILrmph 596
Cdd:COG2401  78 GALKgtPVAGCVDVPDNQFgREASL-----------IDAIG-------------RKGDFKDAVELLNAVGLSDAVL---- 129

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  597 gYDTQVGErglkLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHR--TSIFIAHRlSTVVDA- 673
Cdd:COG2401 130 -WLRRFKE----LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAgiTLVVATHH-YDVIDDl 203

                       250
                ....*....|....*
gi 8928549  674 --DEIIVLDQGKVAE 686
Cdd:COG2401 204 qpDLLIFVGYGGVPE 218
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
 487-647 2.70e-14

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 72.89  E-value: 2.70e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   487 VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLE---SLR-RAVGVVPQDAVL----- 557
Cdd:PRK10584  25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEaraKLRaKHVGFVFQSFMLiptln 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   558 -FHNTIYYNLLYG-NISASPEEVYAVAKLAGLHDAILRMPhgydtqvgergLKLSGGEKQRVAIARAILKDPPVILYDEA 635
Cdd:PRK10584 105 aLENVELPALLRGeSSRQSRNGAKALLEQLGLGKRLDHLP-----------AQLSGGEQQRVALARAFNGRPDVLFADEP 173

                        170
                 ....*....|..
gi 8928549   636 TSSLDSITEETI 647
Cdd:PRK10584 174 TGNLDRQTGDKI 185
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
487-688 5.72e-14

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 72.71  E-value: 5.72e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   487 VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNL 566
Cdd:PRK10253  22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDITVQEL 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   567 L-YGNISASP-------EEVYAVAK---LAGLHDAILRmphGYDTqvgerglkLSGGEKQRVAIARAILKDPPVILYDEA 635
Cdd:PRK10253 102 VaRGRYPHQPlftrwrkEDEEAVTKamqATGITHLADQ---SVDT--------LSGGQRQRAWIAMVLAQETAIMLLDEP 170

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 8928549   636 TSSLDSITEETILGAMKDVVKHR--TSIFIAHRLSTVVD-ADEIIVLDQGKVAERG 688
Cdd:PRK10253 171 TTWLDISHQIDLLELLSELNREKgyTLAAVLHDLNQACRyASHLIALREGKIVAQG 226
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
 484-683 5.78e-14

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


Pssm-ID: 131681 [Multi-domain]  Cd Length: 500  Bit Score: 75.25  E-value: 5.78e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    484 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYePQ---KGSIYLAGQNIQDVSL-ESLRRAVGVVPQDAVLFH 559
Cdd:TIGR02633  13 GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHgtwDGEIYWSGSPLKASNIrDTERAGIVIIHQELTLVP 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    560 N-TIYYNLLYGNISASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSS 638
Cdd:TIGR02633  92 ElSVAENIFLGNEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSS 171

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 8928549    639 LDSITEETILGAMKDVVKHRTS-IFIAHRLSTV-VDADEIIVLDQGK 683
Cdd:TIGR02633 172 LTEKETEILLDIIRDLKAHGVAcVYISHKLNEVkAVCDTICVIRDGQ 218
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
483-679 6.34e-14

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 70.73  E-value: 6.34e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   483 EGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGqniqdvsleslRRAVGVVPQdavlfhnti 562
Cdd:NF040873   3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQ--------- 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   563 yynllygnISASPEEVYA-VAKLAGL----HDAILRMPHGYDTQVGERGLK--------------LSGGEKQRVAIARAI 623
Cdd:NF040873  63 --------RSEVPDSLPLtVRDLVAMgrwaRRGLWRRLTRDDRAAVDDALErvgladlagrqlgeLSGGQRQRALLAQGL 134

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 8928549   624 LKDPPVILYDEATSSLDSITEETILGAMKDVV-KHRTSIFIAHRLSTVVDADEIIVL 679
Cdd:NF040873 135 AQEADLLLLDEPTTGLDAESRERIIALLAEEHaRGATVVVVTHDLELVRRADPCVLL 191
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
 484-651 6.55e-14

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: 70.98  E-value: 6.55e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  484 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIY 563
Cdd:cd03231  12 GRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVL 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  564 YNLLY---GNISASPEEVYAVAKLAGLHDAilrmPHGYdtqvgerglkLSGGEKQRVAIARAILKDPPVILYDEATSSLD 640
Cdd:cd03231  92 ENLRFwhaDHSDEQVEEALARVGLNGFEDR----PVAQ----------LSAGQQRRVALARLLLSGRPLWILDEPTTALD 157

                       170
                ....*....|.
gi 8928549  641 SITEETILGAM 651
Cdd:cd03231 158 KAGVARFAEAM 168
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
 484-685 6.60e-14

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 75.09  E-value: 6.60e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   484 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSlESLRRAVGV--VPQDAVLFHN- 560
Cdd:PRK15439  23 GVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLT-PAKAHQLGIylVPQEPLLFPNl 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   561 TIYYNLLYGnisaSPEEVYAVAKLAGLHdAILRMPHGYDTQVGerglKLSGGEKQRVAIARAILKDPPVILYDEATSSLD 640
Cdd:PRK15439 102 SVKENILFG----LPKRQASMQKMKQLL-AALGCQLDLDSSAG----SLEVADRQIVEILRGLMRDSRILILDEPTASLT 172

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 8928549   641 SITEETILGAMKDVVKHRTSI-FIAHRLSTVVD-ADEIIVLDQGKVA 685
Cdd:PRK15439 173 PAETERLFSRIRELLAQGVGIvFISHKLPEIRQlADRISVMRDGTIA 219
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
 484-683 7.22e-14

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 74.97  E-value: 7.22e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   484 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYePQ---KGSIYLAGQNIQDVSL-ESLRRAVGVVPQDAVLFH 559
Cdd:PRK13549  17 GVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQASNIrDTERAGIAIIHQELALVK 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   560 N-TIYYNLLYGN-ISASP----EEVYAVAK--LAGLHDAIlrmphGYDTQVGErglkLSGGEKQRVAIARAILKDPPVIL 631
Cdd:PRK13549  96 ElSVLENIFLGNeITPGGimdyDAMYLRAQklLAQLKLDI-----NPATPVGN----LGLGQQQLVEIAKALNKQARLLI 166

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 8928549   632 YDEATSSLDSITEETILGAMKDVVKHR-TSIFIAHRLSTVVD-ADEIIVLDQGK 683
Cdd:PRK13549 167 LDEPTASLTESETAVLLDIIRDLKAHGiACIYISHKLNEVKAiSDTICVIRDGR 220
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
 476-703 7.51e-14

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 75.28  E-value: 7.51e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   476 NVHFEYiEGQKV--LSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEP-----QKGSIYLAGQNIQDVSLESLRRA- 547
Cdd:PRK10261  19 NIAFMQ-EQQKIaaVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQagglvQCDKMLLRRRSRQVIELSEQSAAq 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   548 --------VGVVPQDAVLFHNTIY---------YNLLYGnisASPEEVYAVAK-------LAGLHDAILRMPHgydtqvg 603
Cdd:PRK10261  98 mrhvrgadMAMIFQEPMTSLNPVFtvgeqiaesIRLHQG---ASREEAMVEAKrmldqvrIPEAQTILSRYPH------- 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   604 erglKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKdVVKHRTS---IFIAHRLSTVVD-ADEIIVL 679
Cdd:PRK10261 168 ----QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIK-VLQKEMSmgvIFITHDMGVVAEiADRVLVM 242

                        250       260
                 ....*....|....*....|....
gi 8928549   680 DQGKVAERGTHHGLLANPHSIYSE 703
Cdd:PRK10261 243 YQGEAVETGSVEQIFHAPQHPYTR 266
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
 488-720 1.02e-13

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 71.50  E-value: 1.02e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   488 LSGISFEVPAGKKVAIVGGSGSGKSTivrLLFRF--YEPQKGSIYLAGQNIQDVSLESL--RRAVgVVPQDAVLFHNTIY 563
Cdd:PRK03695  12 LGPLSAEVRAGEILHLVGPNGAGKST---LLARMagLLPGSGSIQFAGQPLEAWSAAELarHRAY-LSQQQTPPFAMPVF 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   564 YNL-LYG----NISASPEEVYAVAKLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARAILKDPPVI-------L 631
Cdd:PRK03695  88 QYLtLHQpdktRTEAVASALNEVAEALGLDDKLGRSVN-----------QLSGGEWQRVRLAAVVLQVWPDInpagqllL 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   632 YDEATSSLDsITEEtilGAMKDVVKH-----RTSIFIAHRLS-TVVDADEIIVLDQGKVAERGTHHGLLANPhsIYSEMW 705
Cdd:PRK03695 157 LDEPMNSLD-VAQQ---AALDRLLSElcqqgIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVLTPE--NLAQVF 230

                        250
                 ....*....|....*
gi 8928549   706 HTQSSRVQNHDNPKW 720
Cdd:PRK03695 231 GVNFRRLDVEGHPML 245
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
 484-687 1.23e-13

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 73.88  E-value: 1.23e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   484 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQ-DVSLESLRRAVGVVPQDAVLFHN-T 561
Cdd:PRK10762  16 GVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfNGPKSSQEAGIGIIHQELNLIPQlT 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   562 IYYNLLYGNISASP------EEVYAVAklaglhDAILR---MPHGYDTQVGErglkLSGGEKQRVAIARAILKDPPVILY 632
Cdd:PRK10762  96 IAENIFLGREFVNRfgridwKKMYAEA------DKLLArlnLRFSSDKLVGE----LSIGEQQMVEIAKVLSFESKVIIM 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   633 DEATSSL-DSITEE--TILGAMKDvvKHRTSIFIAHRLSTVVD-ADEIIVLDQGK-VAER 687
Cdd:PRK10762 166 DEPTDALtDTETESlfRVIRELKS--QGRGIVYISHRLKEIFEiCDDVTVFRDGQfIAER 223
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
486-691 1.25e-13

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 71.58  E-value: 1.25e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   486 KVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGS---IYLAGQNIQDV-----SLESLRRAVGVVPQDAVL 557
Cdd:PRK09984  18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAgshIELLGRTVQREgrlarDIRKSRANTGYIFQQFNL 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   558 FHN-TIYYNLLYGNISASP-----EEVYAVAKLAGLHDAILRMphGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVIL 631
Cdd:PRK09984  98 VNRlSVLENVLIGALGSTPfwrtcFSWFTREQKQRALQALTRV--GMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVIL 175

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 8928549   632 YDEATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLSTVVD-ADEIIVLDQGKVAERGTHH 691
Cdd:PRK09984 176 ADEPIASLDPESARIVMDTLRDINQNDgiTVVVTLHQVDYALRyCERIVALRQGHVFYDGSSQ 238
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
472-688 1.41e-13

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 71.58  E-value: 1.41e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   472 VAFDNVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQ--NIQDVSLESLRRAVG 549
Cdd:PRK13638   2 LATSDLWFRY-QDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQVA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   550 VVPQDAvlfHNTIYYNLLYGNISaspeevYAVAKLAGLHDAILRMPHGYDTQVGERGLK------LSGGEKQRVAIARAI 623
Cdd:PRK13638  81 TVFQDP---EQQIFYTDIDSDIA------FSLRNLGVPEAEITRRVDEALTLVDAQHFRhqpiqcLSHGQKKRVAIAGAL 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 8928549   624 LKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFI-AHRLSTVVD-ADEIIVLDQGKVAERG 688
Cdd:PRK13638 152 VLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIIsSHDIDLIYEiSDAVYVLRQGQILTHG 218
ABC_6TM_exporter_like cd18565
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
 140-430 1.43e-13

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: 72.21  E-value: 1.43e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  140 VAISLGFLGGAKAMNIVVPFMFKYAVDS-LNQMSGNMLNLSDAPNTVATMATAVLIGY--GVSRAGAAFFNEVRNAVFGK 216
Cdd:cd18565   1 LVLGLLASILNRLFDLAPPLLIGVAIDAvFNGEASFLPLVPASLGPADPRGQLWLLGGltVAAFLLESLFQYLSGVLWRR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  217 VAQNSIRRIAKNVFLHLHNLDLGFHLSRQTG----ALSKAIDRGTRgisfVLSALVFNLLPIMFEVMLVSGVLYYkCGAQ 292
Cdd:cd18565  81 FAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGdlmsVLNNDVNQLER----FLDDGANSIIRVVVTVLGIGAILFY-LNWQ 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  293 FALVTLGTLgtytAFTVAVTRWRTRfRIEMNKAD--NDAG--NAAI-DSLLNYETVKYFNNERYEAQRYDGFLKTYETAS 367
Cdd:cd18565 156 LALVALLPV----PLIIAGTYWFQR-RIEPRYRAvrEAVGdlNARLeNNLSGIAVIKAFTAEDFERERVADASEEYRDAN 230

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 8928549  368 LKSTSTLAMLNFGQSAIFSVGLTAI------MVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTV 430
Cdd:cd18565 231 WRAIRLRAAFFPVIRLVAGAGFVATfvvggyWVLDGPPLFTGTLTVGTLVTFLFYTQRLLWPLTRLGDL 299
ABC_6TM_Rv0194_D1_like cd18543
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ...
 140-437 2.05e-13

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: 71.36  E-value: 2.05e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  140 VAISLGFLGGAKAMNIVVPFMFKYAVDSLnqmsgnmlnLSDAPNTVATMATAVLIGYGVSRAGAAFfneVRNAVFGKVA- 218
Cdd:cd18543   1 LILALLAALLATLAGLAIPLLTRRAIDGP---------IAHGDRSALWPLVLLLLALGVAEAVLSF---LRRYLAGRLSl 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  219 --QNSIRRiakNVFLHLHNLDLGFHLSRQTGAL-SKAI-DRGT--RGISFVLSALVFNL-LPIMFEVMLVSGVLyykcga 291
Cdd:cd18543  69 gvEHDLRT---DLFAHLQRLDGAFHDRWQSGQLlSRATsDLSLvqRFLAFGPFLLGNLLtLVVGLVVMLVLSPP------ 139

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  292 qFALVTLGTLGtytAFTVAVTRWRTRFRIEMNKADNDAGNAA--ID-SLLNYETVKYFNNERYEAQRYDGFLKTYETASL 368
Cdd:cd18543 140 -LALVALASLP---PLVLVARRFRRRYFPASRRAQDQAGDLAtvVEeSVTGIRVVKAFGRERRELDRFEAAARRLRATRL 215

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 8928549  369 KSTSTLAMLNFGQSAIFSVGLTAIMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQA 437
Cdd:cd18543 216 RAARLRARFWPLLEALPELGLAAVLALGGWLVANGSLTLGTLVAFSAYLTMLVWPVRMLGWLLAMAQRA 284
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
 484-697 2.67e-13

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


Pssm-ID: 440752 [Multi-domain]  Cd Length: 240  Bit Score: 70.06  E-value: 2.67e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  484 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIvrllfrFY------EPQKGSIYLAGQNIQDVSLEslRRA---VGVVPQD 554
Cdd:COG1137  15 KRTVVKDVSLEVNQGEIVGLLGPNGAGKTTT------FYmivglvKPDSGRIFLDGEDITHLPMH--KRArlgIGYLPQE 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  555 AVLFHN-TIYYNLLygnisaspeevyAVAKLAGLH--------DAIL---RMPHGYDTqvgeRGLKLSGGEKQRVAIARA 622
Cdd:COG1137  87 ASIFRKlTVEDNIL------------AVLELRKLSkkereerlEELLeefGITHLRKS----KAYSLSGGERRRVEIARA 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  623 ILKDPPVILYDEATSSLDSITEETIlgamKDVVKHRTS----IFIA-HR----LSTVvdaDEIIVLDQGKVAERGTHHGL 693
Cdd:COG1137 151 LATNPKFILLDEPFAGVDPIAVADI----QKIIRHLKErgigVLITdHNvretLGIC---DRAYIISEGKVLAEGTPEEI 223


                ....
gi 8928549  694 LANP 697
Cdd:COG1137 224 LNNP 227
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 477-696 5.01e-13

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


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 70.89  E-value: 5.01e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  477 VHFEYIEgQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRaVGVV----- 551
Cdd:COG4586  28 FRREYRE-VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFARR-IGVVfgqrs 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  552 -------PQDAVLFHNTIYynllygNIsasPEEVYA--VAKLAGLhdaiLRMPHGYDTQVgeRglKLSGGEKQRVAIARA 622
Cdd:COG4586 106 qlwwdlpAIDSFRLLKAIY------RI---PDAEYKkrLDELVEL----LDLGELLDTPV--R--QLSLGQRMRCELAAA 168

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 8928549  623 ILKDPPVILYDEATSSLDSITEETILGAMKDVVK-HRTSIFIA-HRLSTVVD-ADEIIVLDQGKVAERGTHHGLLAN 696
Cdd:COG4586 169 LLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNReRGTTILLTsHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKER 245
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
 491-703 5.29e-13

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 70.93  E-value: 5.29e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   491 ISFEVPAGKKVAIVGGSGSGKS----TIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVG----VVPQDAVLFHN-- 560
Cdd:PRK11022  26 ISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISEKERRNLVGaevaMIFQDPMTSLNpc 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   561 -TIYYNLLY-------GNISASPEEVYAVAKLAGLHDAILRM---PHgydtqvgerglKLSGGEKQRVAIARAILKDPPV 629
Cdd:PRK11022 106 yTVGFQIMEaikvhqgGNKKTRRQRAIDLLNQVGIPDPASRLdvyPH-----------QLSGGMSQRVMIAMAIACRPKL 174

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 8928549   630 ILYDEATSSLDSITEETILGAMKDVVKHRTS--IFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGLLANPHSIYSE 703
Cdd:PRK11022 175 LIADEPTTALDVTIQAQIIELLLELQQKENMalVLITHDLALVAEaAHKIIVMYAGQVVETGKAHDIFRAPRHPYTQ 251
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
 476-658 5.53e-13

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127 [Multi-domain]  Cd Length: 200  Bit Score: 68.44  E-value: 5.53e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   476 NVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIqDVSLESLRRAV------- 548
Cdd:PRK13540   6 ELDFDY-HDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI-KKDLCTYQKQLcfvghrs 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   549 GVVPQdaVLFHNTIYYNLLYGNISASPEEVYAVAKLAGLHDailrMPHGYdtqvgerglkLSGGEKQRVAIARAILKDPP 628
Cdd:PRK13540  84 GINPY--LTLRENCLYDIHFSPGAVGITELCRLFSLEHLID----YPCGL----------LSSGQKRQVALLRLWMSKAK 147

                        170       180       190
                 ....*....|....*....|....*....|
gi 8928549   629 VILYDEATSSLDSITEETIlgaMKDVVKHR 658
Cdd:PRK13540 148 LWLLDEPLVALDELSLLTI---ITKIQEHR 174
ABC_6TM_PCAT1_LagD_like cd18570
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ...
 154-475 2.10e-12

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: 68.63  E-value: 2.10e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  154 NIVVPFMFKYAVDS-LNQMSGNMLNLsdapntvatMATAVLIGYGVSragaAFFNEVRNAVFGKVAQNSIRRIAKNVFLH 232
Cdd:cd18570  18 GIAGSFFFQILIDDiIPSGDINLLNI---------ISIGLILLYLFQ----SLLSYIRSYLLLKLSQKLDIRLILGYFKH 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  233 LHNLDLGFHLSRQTGA-LSKAIDrgTRGISFVLSALVFNLlPIMFEVMLVSGVLYYKCGAQFALVTLGTLGTYTAFTVA- 310
Cdd:cd18570  85 LLKLPLSFFETRKTGEiISRFND--ANKIREAISSTTISL-FLDLLMVIISGIILFFYNWKLFLITLLIIPLYILIILLf 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  311 VTRWRTRFRIEMNK-ADNDAgnAAIDSLLNYETVKYFNNERYEAQRYDGFLKTYetasLKSTSTLAMLNFGQSAIF---- 385
Cdd:cd18570 162 NKPFKKKNREVMESnAELNS--YLIESLKGIETIKSLNAEEQFLKKIEKKFSKL----LKKSFKLGKLSNLQSSIKglis 235

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  386 SVGLTAIMVLASQGIVAGTLTVGDLVMVNGLLfqlslpLNFLGTVyretrQALIDmntlftllkvdtqikdkvmaspLQI 465
Cdd:cd18570 236 LIGSLLILWIGSYLVIKGQLSLGQLIAFNALL------GYFLGPI-----ENLIN----------------------LQP 282

                       330
                ....*....|
gi 8928549  466 TPQTATVAFD 475
Cdd:cd18570 283 KIQEAKVAAD 292
3a01203 TIGR00954
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...
 389-674 2.83e-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: 2.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    389 LTAIMVLASQGIVAGTLTVGDLV---MVNG-LLFQLSLPLNFLGTVYRETRQALIDMNTLFTLLKV-------------- 450
Cdd:TIGR00954 344 AVSIPIFDKTHPAFLEMSEEELMqefYNNGrLLLKAADALGRLMLAGRDMTRLAGFTARVDTLLQVlddvksgnfkrprv 423

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    451 --DTQIKDKVMASPL-----QITPQTATVAFDNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLF---- 519
Cdd:TIGR00954 424 eeIESGREGGRNSNLvpgrgIVEYQDNGIKFENIPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGelwp 503

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    520 ----RFYEPQKGSIYLAGQNIQdVSLESLRravgvvpqDAVLFHNTIYYNLLYGNISASPEEVYAVAKLaglhDAILRMP 595
Cdd:TIGR00954 504 vyggRLTKPAKGKLFYVPQRPY-MTLGTLR--------DQIIYPDSSEDMKRRGLSDKDLEQILDNVQL----THILERE 570

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    596 HGYDTqVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDV------VKHRTSIFIAHRLST 669
Cdd:TIGR00954 571 GGWSA-VQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREFgitlfsVSHRKSLWKYHEYLL 649


                  ....*
gi 8928549    670 VVDAD 674
Cdd:TIGR00954 650 YMDGR 654
ABC_6TM_Pgp_ABCB1_D1_like cd18577
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ...
 142-413 3.07e-12

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: 67.88  E-value: 3.07e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  142 ISLGFLG--GAKAMNIVVPFMFKYAVDSLNQMSGNMLNLSDAPNTVATMATA-VLIGygvsrAGAAFFNEVRNAVFGKVA 218
Cdd:cd18577   1 LIIGLLAaiAAGAALPLMTIVFGDLFDAFTDFGSGESSPDEFLDDVNKYALYfVYLG-----IGSFVLSYIQTACWTITG 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  219 QNSIRRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTR----GISFVLSALVFNLlpimfeVMLVSGV---LYYkcGA 291
Cdd:cd18577  76 ERQARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNliqdGIGEKLGLLIQSL------STFIAGFiiaFIY--SW 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  292 QFALVTLGTLGTYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNERYEAQRYDGFLKTYETASLKST 371
Cdd:cd18577 148 KLTLVLLATLPLIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKG 227

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 8928549  372 STLAMlnfgQSAIFSVGLTAIMVLA----SQGIVAGTLTVGDLVMV 413
Cdd:cd18577 228 LVSGL----GLGLLFFIIFAMYALAfwygSRLVRDGEISPGDVLTV 269
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
 481-704 4.41e-12

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: 66.66  E-value: 4.41e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  481 YIEGQKVLSGISFEVPAG-----KKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIylagqniqdvslESLRRAVGVVPQDA 555
Cdd:cd03237   3 YPTMKKTLGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI------------EIELDTVSYKPQYI 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  556 VLFHNTIYYNLLYGNISASPEEVYAVAKLAGlhdaILRMPHGYDTQVGErglkLSGGEKQRVAIARAILKDPPVILYDEA 635
Cdd:cd03237  71 KADYEGTVRDLLSSITKDFYTHPYFKTEIAK----PLQIEQILDREVPE----LSGGELQRVAIAACLSKDADIYLLDEP 142

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  636 TSSLDSitEETILGAmkDVVKHrtsiFIAHRLST--VVD---------ADEIIVLDqGKVAERGTHHGllanPHSIYSEM 704
Cdd:cd03237 143 SAYLDV--EQRLMAS--KVIRR----FAENNEKTafVVEhdiimidylADRLIVFE-GEPSVNGVANP----PQSLRSGM 209
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
 484-640 4.92e-12

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 68.90  E-value: 4.92e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  484 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRA-VGVVPQD-----AVL 557
Cdd:COG3845 270 GVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgVAYIPEDrlgrgLVP 349

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  558 fHNTIYYNLLYGNISASP---------EEVYAVAKlaglhDAILRM---PHGYDTQVGerglKLSGGEKQRVAIARAILK 625
Cdd:COG3845 350 -DMSVAENLILGRYRRPPfsrggfldrKAIRAFAE-----ELIEEFdvrTPGPDTPAR----SLSGGNQQKVILARELSR 419

                       170
                ....*....|....*
gi 8928549  626 DPPVILYDEATSSLD 640
Cdd:COG3845 420 DPKLLIAAQPTRGLD 434
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
 469-640 7.09e-12

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 66.29  E-value: 7.09e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   469 TATVAFDNVHFEYieGQ-KVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQniqdvslesLRra 547
Cdd:PRK09544   2 TSLVSLENVSVSF--GQrRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK---------LR-- 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   548 VGVVPQ----DAVLFHNTIYYNLLYGNI-SASPEEVYAVAKLAGLHDAILRmphgydtqvgerglKLSGGEKQRVAIARA 622
Cdd:PRK09544  69 IGYVPQklylDTTLPLTVNRFLRLRPGTkKEDILPALKRVQAGHLIDAPMQ--------------KLSGGETQRVLLARA 134

                        170
                 ....*....|....*...
gi 8928549   623 ILKDPPVILYDEATSSLD 640
Cdd:PRK09544 135 LLNRPQLLVLDEPTQGVD 152
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
 490-700 7.10e-12

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


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 66.17  E-value: 7.10e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   490 GISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRaVGVVP--QDAVLFHN-TIYYNL 566
Cdd:PRK11300  23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIAR-MGVVRtfQHVRLFREmTVIENL 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   567 LygnisaspeevyaVAK--------LAGL----------HDAILRMPHGYDtQVGERGL------KLSGGEKQRVAIARA 622
Cdd:PRK11300 102 L-------------VAQhqqlktglFSGLlktpafrraeSEALDRAATWLE-RVGLLEHanrqagNLAYGQQRRLEIARC 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   623 ILKDPPVILYDEATSSLDSitEETI-LGAMKDVVK--HRTSI-FIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGLLANP 697
Cdd:PRK11300 168 MVTQPEILMLDEPAAGLNP--KETKeLDELIAELRneHNVTVlLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEIRNNP 245


                 ...
gi 8928549   698 HSI 700
Cdd:PRK11300 246 DVI 248
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
 484-704 8.41e-12

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 66.10  E-value: 8.41e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   484 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSL----ESLRRAV-----GVVPQD 554
Cdd:PRK11701  18 PRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLyalsEAERRRLlrtewGFVHQH 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   555 A-------VLFHNTIYYNLL------YGNISASpeevyAVAKLAGLHDAILRM---PHGYdtqvgerglklSGGEKQRVA 618
Cdd:PRK11701  98 PrdglrmqVSAGGNIGERLMavgarhYGDIRAT-----AGDWLERVEIDAARIddlPTTF-----------SGGMQQRLQ 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   619 IARAILKDPPVILYDEATSSLDSITEETILGAMKDVVK--HRTSIFIAHRLSTV-VDADEIIVLDQGKVAERGTHHGLLA 695
Cdd:PRK11701 162 IARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRelGLAVVIVTHDLAVArLLAHRLLVMKQGRVVESGLTDQVLD 241


                 ....*....
gi 8928549   696 NPHSIYSEM 704
Cdd:PRK11701 242 DPQHPYTQL 250
ABC_6TM_TmrA_like cd18544
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ...
 140-412 9.53e-12

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: 66.64  E-value: 9.53e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  140 VAISLGFLGGAKAMNIVVPFMFKYAVDS-LNQMSGNMLNLsdapntvatmaTAVLIGYGVSRAGAAFFNEVRNAVFGKVA 218
Cdd:cd18544   1 FILALLLLLLATALELLGPLLIKRAIDDyIVPGQGDLQGL-----------LLLALLYLGLLLLSFLLQYLQTYLLQKLG 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  219 QNSIRRIAKNVFLHLHNLDLGFHLSRQTGALSkaidrgTRGIS--------F--VLSALVFNLLPI--MFEVMLVSGVly 286
Cdd:cd18544  70 QRIIYDLRRDLFSHIQRLPLSFFDRTPVGRLV------TRVTNdtealnelFtsGLVTLIGDLLLLigILIAMFLLNW-- 141

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  287 ykcgaQFALVTLGTLgtytAFTVAVTRWrtrFRIEMNKADND--AGNAAIDSLLNyE------TVKYFNNERYEAQRYDG 358
Cdd:cd18544 142 -----RLALISLLVL----PLLLLATYL---FRKKSRKAYREvrEKLSRLNAFLQ-EsisgmsVIQLFNREKREFEEFDE 208

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 8928549  359 FLKTYETASLKSTSTLAMLNFGQSAIFSVGLTAIMVLASQGIVAGTLTVGDLVM 412
Cdd:cd18544 209 INQEYRKANLKSIKLFALFRPLVELLSSLALALVLWYGGGQVLSGAVTLGVLYA 262
ABC_6TM_TAP cd18572
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ...
 143-438 3.30e-11

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


Pssm-ID: 350016 [Multi-domain]  Cd Length: 289  Bit Score: 64.87  E-value: 3.30e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  143 SLGFLGGAKAMNIVVPFMFKYAVDSLNQMSGnmlnlsdapntVATMATAVLIgYGVSRAGAAFFNEVRNAVFGKVAQNSI 222
Cdd:cd18572   1 AFVFLVVAALSELAIPHYTGAVIDAVVADGS-----------REAFYRAVLL-LLLLSVLSGLFSGLRGGCFSYAGTRLV 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  223 RRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGISFVLSaLVFNllpIMFE--VMLVSGVLY-YKCGAQFALVTLG 299
Cdd:cd18572  69 RRLRRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLS-TNLN---VFLRnlVQLVGGLAFmFSLSWRLTLLAFI 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  300 TLGtytaFTVAVTRWRTRFRIEMNKADND----AGNAAIDSLLNYETVKYFNNERYEAQRYDGFLKTYETASLKStstlA 375
Cdd:cd18572 145 TVP----VIALITKVYGRYYRKLSKEIQDalaeANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQ----A 216

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 8928549  376 MLNFGQSAIFSVGLTAIMVLA----SQGIVAGTLTVGDLVMVngLLFQLSL--PLNFLGTVYRETRQAL 438
Cdd:cd18572 217 LAYAGYVAVNTLLQNGTQVLVlfygGHLVLSGRMSAGQLVTF--MLYQQQLgeAFQSLGDVFSSLMQAV 283
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
484-636 3.34e-11

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 66.20  E-value: 3.34e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  484 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQ--NIQDVSlESLRRAVGVVPQD----AVL 557
Cdd:COG1129 264 VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpvRIRSPR-DAIRAGIAYVPEDrkgeGLV 342

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  558 FHNTIYYNLLYGNISA-------SPEEVYAVAKlaglhDAILRM---PHGYDTQVGErglkLSGGEKQRVAIARAILKDP 627
Cdd:COG1129 343 LDLSIRENITLASLDRlsrggllDRRRERALAE-----EYIKRLrikTPSPEQPVGN----LSGGNQQKVVLAKWLATDP 413


                ....*....
gi 8928549  628 PVILYDEAT 636
Cdd:COG1129 414 KVLILDEPT 422
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 498-680 8.44e-11

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 60.85  E-value: 8.44e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549     498 GKKVAIVGGSGSGKSTIVRLLFRFYEPQKGS-IYLAGQNIQDVSLESLRravgvvpqdavlfhntiyynllygnisaspe 576
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPGGGvIYIDGEDILEEVLDQLL------------------------------- 50

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549     577 evyavaklaglhdailrmphgyDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVK 656
Cdd:smart00382  51 ----------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLL 108

                          170       180       190
                   ....*....|....*....|....*....|.
gi 8928549     657 HRTS-------IFIAHRLSTVVDADEIIVLD 680
Cdd:smart00382 109 LLLKseknltvILTTNDEKDLGPALLRRRFD 139
PLN03211 PLN03211
ABC transporter G-25; Provisional
 480-683 1.37e-10

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 64.52  E-value: 1.37e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   480 EYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLF-RFYEPQKGSIYLAgqNIQDVSLESLRRaVGVVPQDAVLF 558
Cdd:PLN03211  76 RQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgRIQGNNFTGTILA--NNRKPTKQILKR-TGFVTQDDILY 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   559 -HNTIYYNLLYGNISASPEEVYAVAKLAGLHDAI--LRMPHGYDTQVGERGLK-LSGGEKQRVAIARAILKDPPVILYDE 634
Cdd:PLN03211 153 pHLTVRETLVFCSLLRLPKSLTKQEKILVAESVIseLGLTKCENTIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDE 232

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 8928549   635 ATSSLDSITEETILGAMKDVV-KHRTSIFIAHRLSTVVDA--DEIIVLDQGK 683
Cdd:PLN03211 233 PTSGLDATAAYRLVLTLGSLAqKGKTIVTSMHQPSSRVYQmfDSVLVLSEGR 284
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
459-682 2.17e-10

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 63.65  E-value: 2.17e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   459 MASPLqITPQTATVAFDNVHfeyiegqkVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQD 538
Cdd:PRK09700   1 MATPY-ISMAGIGKSFGPVH--------ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNK 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   539 VSLE-SLRRAVGVVPQD-AVLFHNTIYYNLLYGNISASP---------EEVYAVAKLAGLHDAILRMPhgyDTQVGErgl 607
Cdd:PRK09700  72 LDHKlAAQLGIGIIYQElSVIDELTVLENLYIGRHLTKKvcgvniidwREMRVRAAMMLLRVGLKVDL---DEKVAN--- 145

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 8928549   608 kLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSI-FIAHRLSTVVD-ADEIIVLDQG 682
Cdd:PRK09700 146 -LSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIvYISHKLAEIRRiCDRYTVMKDG 221
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
 488-677 7.98e-10

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: 58.49  E-value: 7.98e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  488 LSGISFEVPAGKKVAIVGGSGSGKSTIVrllfrfyepqKGSIYLAGQNIQDVSLESlrravgvvpqdavlfhntiyynll 567
Cdd:cd03238  11 LQNLDVSIPLNVLVVVTGVSGSGKSTLV----------NEGLYASGKARLISFLPK------------------------ 56

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  568 ygnisASPEEVYAVAKLAGLHDAILrmphGYDTqVGERGLKLSGGEKQRVAIARAILKDPPVILY--DEATSSLDSITEE 645
Cdd:cd03238  57 -----FSRNKLIFIDQLQFLIDVGL----GYLT-LGQKLSTLSGGELQRVKLASELFSEPPGTLFilDEPSTGLHQQDIN 126

                       170       180       190
                ....*....|....*....|....*....|...
gi 8928549  646 TILGAMKDVV-KHRTSIFIAHRLSTVVDADEII 677
Cdd:cd03238 127 QLLEVIKGLIdLGNTVILIEHNLDVLSSADWII 159
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
 484-640 7.98e-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: 61.87  E-value: 7.98e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    484 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLfrfyepqkgsiylAG--QNIQDVSLESLRRAVGVVPQDAVLFHN- 560
Cdd:TIGR03719  17 KKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIM-------------AGvdKDFNGEARPQPGIKVGYLPQEPQLDPTk 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    561 TIYYNLLYG-----NISASPEEVYA------------VAKLAGLHDAI------------------LRMPHGyDTQVGer 605
Cdd:TIGR03719  84 TVRENVEEGvaeikDALDRFNEISAkyaepdadfdklAAEQAELQEIIdaadawdldsqleiamdaLRCPPW-DADVT-- 160

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 8928549    606 glKLSGGEKQRVAIARAILKDPPVILYDEATSSLD 640
Cdd:TIGR03719 161 --KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD 193
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 479-692 1.38e-09

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


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 61.34  E-value: 1.38e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  479 FEYIEGQKVLSGISFEVPAGK-----KVAIVGGSGSGKSTIVRLLFRFYEPQKGSI-----------YLagQNIQDVSLE 542
Cdd:COG1245 342 VEYPDLTKSYGGFSLEVEGGEiregeVLGIVGPNGIGKTTFAKILAGVLKPDEGEVdedlkisykpqYI--SPDYDGTVE 419

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  543 S-LRRAVGVVpqdavlFHNTIYYNLlygnisaspeevyaVAKLAGLHdailRMphgYDTQVGErglkLSGGEKQRVAIAR 621
Cdd:COG1245 420 EfLRSANTDD------FGSSYYKTE--------------IIKPLGLE----KL---LDKNVKD----LSGGELQRVAIAA 468

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 8928549  622 AILKDPPVILYDEATSSLDSitEETILGA--MKDVV--KHRTSIFIAHRLsTVVD--ADEIIVLDqGKVAERGTHHG 692
Cdd:COG1245 469 CLSRDADLYLLDEPSAHLDV--EQRLAVAkaIRRFAenRGKTAMVVDHDI-YLIDyiSDRLMVFE-GEPGVHGHASG 541
ABC_6TM_exporter_like cd18778
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
 140-411 1.90e-09

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


Pssm-ID: 350051 [Multi-domain]  Cd Length: 293  Bit Score: 59.47  E-value: 1.90e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  140 VAISLGFLGGAKAMNIVVPFMFKYAVDSLnqmsgnmlnlsdapnTVATMATAVLIGYGVSRAGA----AFFNEVRNAVFG 215
Cdd:cd18778   1 LILTLLCALLSTLLGLVPPWLIRELVDLV---------------TIGSKSLGLLLGLALLLLGAyllrALLNFLRIYLNH 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  216 KVAQNSIRRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGISFVLSALVFNLLPIMFEVMLVSGVLYYKcGAQFAL 295
Cdd:cd18778  66 VAEQKVVADLRSDLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSI-NPKLAL 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  296 VTLGTLGTYTAFTVAVTRW-RTRFRI------EMNKA--DNDAGNAAIdsllnyetvKYFNNERYEAQRYDGFLKTYETA 366
Cdd:cd18778 145 LTLIPIPFLALGAWLYSKKvRPRYRKvrealgELNALlqDNLSGIREI---------QAFGREEEEAKRFEALSRRYRKA 215

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 8928549  367 SLKSTSTLAMlnFGQSAIFSVGLTAIMVLASQG--IVAGTLTVGDLV 411
Cdd:cd18778 216 QLRAMKLWAI--FHPLMEFLTSLGTVLVLGFGGrlVLAGELTIGDLV 260
ABC_6TM_HetC_like cd18568
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ...
 230-444 3.26e-09

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: 58.73  E-value: 3.26e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  230 FLHLHNLDLGFHLSRQTGALskaIDR-----------GTRGISFVLSAL-VFNLLPIMFevmlvsgvlYYKcgAQFALVT 297
Cdd:cd18568  82 YKHLLSLPLSFFASRKVGDI---ITRfqenqkirrflTRSALTTILDLLmVFIYLGLMF---------YYN--LQLTLIV 147

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  298 LGTLGTYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNERYEAQRYDGFLKTYETASLKSTSTLAML 377
Cdd:cd18568 148 LAFIPLYVLLTLLSSPKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAERPIRWRWENKFAKALNTRFRGQKLSIVL 227

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 8928549  378 NFGQSAIFSVGLTAIMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDMNTL 444
Cdd:cd18568 228 QLISSLINHLGTIAVLWYGAYLVISGQLTIGQLVAFNMLFGSVINPLLALVGLWDELQETRISVERL 294
ABC_6TM_YknV_like cd18545
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ...
 139-431 3.51e-09

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: 58.63  E-value: 3.51e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  139 RVAISLGFLGGAKAMNIVVPFMFKYAVDSlNQMSGNMLNLsdapntvatmaTAVLIGYGVSRAGAAFFNEVRNAVFGKVA 218
Cdd:cd18545   1 KLLLALLLMLLSTAASLAGPYLIKIAIDE-YIPNGDLSGL-----------LIIALLFLALNLVNWVASRLRIYLMAKVG 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  219 QNSIRRIAKNVFLHLHNLDLGFHLSRQTGA-LSKAI-DRGTrgISFVLSALVFNLLPIMFEVMLVSGVLYYKcGAQFALV 296
Cdd:cd18545  69 QRILYDLRQDLFSHLQKLSFSFFDSRPVGKiLSRVInDVNS--LSDLLSNGLINLIPDLLTLVGIVIIMFSL-NVRLALV 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  297 TLGTLgtyTAFTVAVTRW----RTRFRIEMNKADNdaGNAAI-DSLLNYETVKYFNNERYEAQRYDGFLKTYETASLKST 371
Cdd:cd18545 146 TLAVL---PLLVLVVFLLrrraRKAWQRVRKKISN--LNAYLhESISGIRVIQSFAREDENEEIFDELNRENRKANMRAV 220

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 8928549  372 STLAMLNFGQSAIFSVGLTAIMVLASQGIVAGTLTVGDLV-MVN--GLLFQlslPLNFLGTVY 431
Cdd:cd18545 221 RLNALFWPLVELISALGTALVYWYGGKLVLGGAITVGVLVaFIGyvGRFWQ---PIRNLSNFY 280
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
480-692 3.71e-09

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 59.82  E-value: 3.71e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   480 EYIEGQKVLSGISFEVPAGKK-----VAIVGGSGSGKSTIVRLLFRFYEPQKGSI-----------YLAGQniQDVSLES 543
Cdd:PRK13409 342 EYPDLTKKLGDFSLEVEGGEIyegevIGIVGPNGIGKTTFAKLLAGVLKPDEGEVdpelkisykpqYIKPD--YDGTVED 419

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   544 LRRAVGVVpqdavlFHNTIYYNLLygnisASPeevyavaklaglhdaiLRMPHGYDTQVGErglkLSGGEKQRVAIARAI 623
Cdd:PRK13409 420 LLRSITDD------LGSSYYKSEI-----IKP----------------LQLERLLDKNVKD----LSGGELQRVAIAACL 468

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 8928549   624 LKDPPVILYDEATSSLDSitEETILGA--MKDVVKHR--TSIFIAHRLsTVVD--ADEIIVLDqGKVAERGTHHG 692
Cdd:PRK13409 469 SRDADLYLLDEPSAHLDV--EQRLAVAkaIRRIAEEReaTALVVDHDI-YMIDyiSDRLMVFE-GEPGKHGHASG 539
GguA NF040905
sugar ABC transporter ATP-binding protein;
484-686 4.46e-09

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 59.42  E-value: 4.46e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   484 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLL-----FRFYEpqkGSIYLAGQ-----NIQDvsleSLRRAVGVVPQ 553
Cdd:NF040905  13 GVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLsgvypHGSYE---GEILFDGEvcrfkDIRD----SEALGIVIIHQ 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   554 D-AVLFHNTIYYNLLYGNISASP-----EEVYAVAK--LA--GLHDAilrmPhgyDTQVGERGLklsgGEKQRVAIARAI 623
Cdd:NF040905  86 ElALIPYLSIAENIFLGNERAKRgvidwNETNRRARelLAkvGLDES----P---DTLVTDIGV----GKQQLVEIAKAL 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 8928549   624 LKDPPVILYDEATSSL---DSiteETILGAMKDVVKHR-TSIFIAHRLSTVVD-ADEIIVLDQGKVAE 686
Cdd:NF040905 155 SKDVKLLILDEPTAALneeDS---AALLDLLLELKAQGiTSIIISHKLNEIRRvADSITVLRDGRTIE 219
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
 484-683 4.70e-09

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 59.36  E-value: 4.70e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   484 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQ-DVSLESLRRAVGVVPQDAVLF-HNT 561
Cdd:PRK10982  10 GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQELNLVlQRS 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   562 IYYNLLYGNisaspeevYAVAKLAGLHDAILRMPH------GYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEA 635
Cdd:PRK10982  90 VMDNMWLGR--------YPTKGMFVDQDKMYRDTKaifdelDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEP 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 8928549   636 TSSLdsiTEE------TILGAMKDvvKHRTSIFIAHRLSTVVD-ADEIIVLDQGK 683
Cdd:PRK10982 162 TSSL---TEKevnhlfTIIRKLKE--RGCGIVYISHKMEEIFQlCDEITILRDGQ 211
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
 576-683 4.86e-09

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


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 60.12  E-value: 4.86e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549     576 EEVYAvAKLAGLHDAILRMPHGYDTQVGE---RGLklSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMK 652
Cdd:TIGR00956  177 REEYA-KHIADVYMATYGLSHTRNTKVGNdfvRGV--SGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALK 253

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 8928549     653 dvvkhrTSIFIAHRLSTVV------DA----DEIIVLDQGK 683
Cdd:TIGR00956  254 ------TSANILDTTPLVAiyqcsqDAyelfDKVIVLYEGY 288
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
 488-685 5.00e-09

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 59.29  E-value: 5.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   488 LSG-----ISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESlRRAVGVV--PQD------ 554
Cdd:PRK15439 274 LTGegfrnISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ-RLARGLVylPEDrqssgl 352

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   555 ---AVLFHNTiyYNLLYGNISASPEEVYAVAKLAGLHDAI-LRMPHGyDTQVGerglKLSGGEKQRVAIARAILKDPPVI 630
Cdd:PRK15439 353 yldAPLAWNV--CALTHNRRGFWIKPARENAVLERYRRALnIKFNHA-EQAAR----TLSGGNQQKVLIAKCLEASPQLL 425

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 8928549   631 LYDEATSSLDSITEETILGAMKDVVKHRTSI-FIAHRLSTVVD-ADEIIVLDQGKVA 685
Cdd:PRK15439 426 IVDEPTRGVDVSARNDIYQLIRSIAAQNVAVlFISSDLEEIEQmADRVLVMHQGEIS 482
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 498-680 9.11e-09

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


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 58.64  E-value: 9.11e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  498 GKKVAIVGGSGSGKSTIVRLLfrfyepqkgsiylAGQ---NIQDVSLEslrravgvVPQDAVL--FHNTI---YYNLLY- 568
Cdd:COG1245  99 GKVTGILGPNGIGKSTALKIL-------------SGElkpNLGDYDEE--------PSWDEVLkrFRGTElqdYFKKLAn 157

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  569 GNISAS--PEEVYAVAKL--------------AGLHDAI---LRMPHGYDTQVGErglkLSGGEKQRVAIARAILKDPPV 629
Cdd:COG1245 158 GEIKVAhkPQYVDLIPKVfkgtvrellekvdeRGKLDELaekLGLENILDRDISE----LSGGELQRVAIAAALLRDADF 233

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 8928549  630 ILYDEATSSLDsITEE-TILGAMKDVVKHRTSIFiahrlstVVDADeIIVLD 680
Cdd:COG1245 234 YFFDEPSSYLD-IYQRlNVARLIRELAEEGKYVL-------VVEHD-LAILD 276
ABC_6TM_ABCB10_like cd18573
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ...
 143-421 9.21e-09

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


Pssm-ID: 350017 [Multi-domain]  Cd Length: 294  Bit Score: 57.52  E-value: 9.21e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  143 SLGFLGGAKAMNIVVPFMFKYAVDSLNQMSGNMLNLSDAPNTVAT-MATAVLIGygvsragaAFFNEVRNAVFGKVAQNS 221
Cdd:cd18573   1 ALALLLVSSAVTMSVPFAIGKLIDVASKESGDIEIFGLSLKTFALaLLGVFVVG--------AAANFGRVYLLRIAGERI 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  222 IRRIAKNVFLHLHNLDLGFHLSRQTG---------------ALSKAIDRGTRGISFVLSALVfnllpIMFevmLVSgvly 286
Cdd:cd18573  73 VARLRKRLFKSILRQDAAFFDKNKTGelvsrlssdtsvvgkSLTQNLSDGLRSLVSGVGGIG-----MML---YIS---- 140

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  287 ykcgAQFALVTLGTLGTYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNERYEAQRYDGflKTYETA 366
Cdd:cd18573 141 ----PKLTLVMLLVVPPIAVGAVFYGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAK--KVDEVF 214

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 8928549  367 SLKSTSTLAMLNFGQSAIFSVGLTAIMVLASQG--IVAGTLTVGDL-------VMVNGLLFQLS 421
Cdd:cd18573 215 DLAKKEALASGLFFGSTGFSGNLSLLSVLYYGGslVASGELTVGDLtsflmyaVYVGSSVSGLS 278
ABC_6TM_Tm287_like cd18548
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ...
 140-430 9.90e-09

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: 57.41  E-value: 9.90e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  140 VAISLGFLGGAKAMNIVVPFMFKYAVDS---------LNQMSGNMLNLsdapnTVATMATAVLIGYGVSRAGAAFFNEVR 210
Cdd:cd18548   1 AILAPLFKLLEVLLELLLPTLMADIIDEgiangdlsyILRTGLLMLLL-----ALLGLIAGILAGYFAAKASQGFGRDLR 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  211 NAVFGKVAQNSirriaknvflhLHNLDlgfHLSrqTGALskaIDRGTRGISFVLSAlVFNLL------PIMFevmLVSGV 284
Cdd:cd18548  76 KDLFEKIQSFS-----------FAEID---KFG--TSSL---ITRLTNDVTQVQNF-VMMLLrmlvraPIML---IGAII 132

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  285 LYYKCGAQFALVTLGTLGTYTAFTVAVTRW-RTRFRIEMNKadNDAGNAAI-DSLLNYETVKYFNNERYEAQRYDGFLKT 362
Cdd:cd18548 133 MAFRINPKLALILLVAIPILALVVFLIMKKaIPLFKKVQKK--LDRLNRVVrENLTGIRVIRAFNREDYEEERFDKANDD 210

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 8928549  363 YETASLKSTSTLAMLNFGQSAIFSVGLTAIMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTV 430
Cdd:cd18548 211 LTDTSLKAGRLMALLNPLMMLIMNLAIVAILWFGGHLINAGSLQVGDLVAFINYLMQILMSLMMLSMV 278
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
 469-684 1.19e-08

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: 55.73  E-value: 1.19e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  469 TATVAFDNVHFEYIEGQ---KVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLL---FRFYEPQKGSIYLAGQNIQDVSlE 542
Cdd:cd03233   1 ASTLSWRNISFTTGKGRskiPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALanrTEGNVSVEGDIHYNGIPYKEFA-E 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  543 SLRRAVGVVPQDAVLFHN-TIYynllygnisaspEEVYAVAKLAGlhDAILRmphgydtqvgerglKLSGGEKQRVAIAR 621
Cdd:cd03233  80 KYPGEIIYVSEEDVHFPTlTVR------------ETLDFALRCKG--NEFVR--------------GISGGERKRVSIAE 131

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 8928549  622 AILKDPPVILYDEATSSLDSITEETILGAMKDVVKhrtsifiAHRLSTVVDA-----------DEIIVLDQGKV 684
Cdd:cd03233 132 ALVSRASVLCWDNSTRGLDSSTALEILKCIRTMAD-------VLKTTTFVSLyqasdeiydlfDKVLVLYEGRQ 198
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
 486-693 1.36e-08

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: 57.91  E-value: 1.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    486 KVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQ-KGSIYLAGQNIQDVS-LESLRRAVGVVPQDAVlfHNTIY 563
Cdd:TIGR02633 274 KRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNpAQAIRAGIAMVPEDRK--RHGIV 351

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    564 YNLLYG-NISASPEEVY-------AVAKLAGLHDAILRM---PHGYDTQVGerglKLSGGEKQRVAIARAILKDPPVILY 632
Cdd:TIGR02633 352 PILGVGkNITLSVLKSFcfkmridAAAELQIIGSAIQRLkvkTASPFLPIG----RLSGGNQQKAVLAKMLLTNPRVLIL 427

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 8928549    633 DEATSSLDSITEETILGAMKDVVKHRTS-IFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGL 693
Cdd:TIGR02633 428 DEPTRGVDVGAKYEIYKLINQLAQEGVAiIVVSSELAEVLGlSDRVLVIGEGKLKGDFVNHAL 490
ABC_6TM_CyaB_HlyB_like cd18588
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ...
 229-444 1.48e-08

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


Pssm-ID: 350032 [Multi-domain]  Cd Length: 294  Bit Score: 56.74  E-value: 1.48e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  229 VFLHLHNLDLGFHLSRQTGALskaIDRgTRGIS----FVLSALVFNLLPIMFEVMLVSGVLYYKcgAQFALVTLGTLGTY 304
Cdd:cd18588  81 LFRHLLRLPLSYFESRQVGDT---VAR-VRELEsirqFLTGSALTLVLDLVFSVVFLAVMFYYS--PTLTLIVLASLPLY 154

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  305 TAFTVAVTRwRTRFRIEmNKADNDAGNAA--IDSLLNYETVKYFNNERYEAQRYDGFLKTYETASLKsTSTLAmlNFGQS 382
Cdd:cd18588 155 ALLSLLVTP-ILRRRLE-EKFQRGAENQSflVETVTGIETVKSLAVEPQFQRRWEELLARYVKASFK-TANLS--NLASQ 229

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 8928549  383 AIFSVGLT---AIMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDMNTL 444
Cdd:cd18588 230 IVQLIQKLttlAILWFGAYLVMDGELTIGQLIAFNMLAGQVSQPVLRLVQLWQDFQQAKVSVERL 294
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
 491-703 1.94e-08

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 56.66  E-value: 1.94e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   491 ISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQ---KGSIYLAGQNIQDVSLESLRR----AVGVVPQDAVLFHNTiy 563
Cdd:PRK09473  35 LNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNLPEKELNKlraeQISMIFQDPMTSLNP-- 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   564 ynllYGNISASPEEVYAVAKLAGLHDAI---LRM----------------PHgydtqvgerglKLSGGEKQRVAIARAIL 624
Cdd:PRK09473 113 ----YMRVGEQLMEVLMLHKGMSKAEAFeesVRMldavkmpearkrmkmyPH-----------EFSGGMRQRVMIAMALL 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   625 KDPPVILYDEATSSLDSITEETILGAMKDVVKH-RTS-IFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGLLANPHSIY 701
Cdd:PRK09473 178 CRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAiIMITHDLGVVAGiCDKVLVMYAGRTMEYGNARDVFYQPSHPY 257


                 ..
gi 8928549   702 SE 703
Cdd:PRK09473 258 SI 259
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
482-640 2.11e-08

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 55.20  E-value: 2.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   482 IEGQKVL-SGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQdvsleSLRRAvgvvpqdavlFHn 560
Cdd:PRK13538  10 ERDERILfSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIR-----RQRDE----------YH- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   561 tiyYNLLY-GNISA-----SPEE-VYAVAKLAGLHD-----AILRmphgydtQVGERGLK------LSGGEKQRVAIARA 622
Cdd:PRK13538  74 ---QDLLYlGHQPGiktelTALEnLRFYQRLHGPGDdealwEALA-------QVGLAGFEdvpvrqLSAGQQRRVALARL 143

                        170
                 ....*....|....*...
gi 8928549   623 ILKDPPVILYDEATSSLD 640
Cdd:PRK13538 144 WLTRAPLWILDEPFTAID 161
ABC_6TM_LmrA_like cd18551
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ...
 140-438 2.17e-08

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: 56.29  E-value: 2.17e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  140 VAISLGFLGGAkaMNIVVPFMFKYAVDSLNQMSGNMlnlsdapNTVATMATAVLIGygvsragaAFFNEVRNAVFGKVAQ 219
Cdd:cd18551   3 LALLLSLLGTA--ASLAQPLLVKNLIDALSAGGSSG-------GLLALLVALFLLQ--------AVLSALSSYLLGRTGE 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  220 NSIRRIAKNVFLHLHNLDLGFHLSRQTG-----------ALSKAIDRGTrgISFVLSALVFNL-LPIMFevmLVSGVLyy 287
Cdd:cd18551  66 RVVLDLRRRLWRRLLRLPVSFFDRRRSGdlvsrvtndttLLRELITSGL--PQLVTGVLTVVGaVVLMF---LLDWVL-- 138

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  288 kcgaqfALVTLGTLGTYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNERYEAQRYDGFLKTYETAS 367
Cdd:cd18551 139 ------TLVTLAVVPLAFLIILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAG 212

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 8928549  368 LKSTSTLAMLNFGQSAIFSVGLTAIMVLASQGIVAGTLTVGDLV---MvngLLFQLSLPLNFLGTVYRETRQAL 438
Cdd:cd18551 213 LKAAKIEALIGPLMGLAVQLALLVVLGVGGARVASGALTVGTLVaflL---YLFQLITPLSQLSSFFTQLQKAL 283
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
482-702 3.65e-08

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 56.46  E-value: 3.65e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   482 IEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNiqdVSLESLRRAV--GVV--PQD--- 554
Cdd:PRK11288 263 LKGPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKP---IDIRSPRDAIraGIMlcPEDrka 339

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   555 -AVLFHNTIYYNLlygNISASPEEVYA--------VAKLAGLHDAILRM--PHGyDTQVGerglKLSGGEKQRVAIARAI 623
Cdd:PRK11288 340 eGIIPVHSVADNI---NISARRHHLRAgclinnrwEAENADRFIRSLNIktPSR-EQLIM----NLSGGNQQKAILGRWL 411

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   624 LKDPPVILYDEATSSLDSITEETILGAMKDVVKH-RTSIFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGllANPHSIY 701
Cdd:PRK11288 412 SEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQgVAVLFVSSDLPEVLGvADRIVVMREGRIAGELAREQ--ATERQAL 489


                 .
gi 8928549   702 S 702
Cdd:PRK11288 490 S 490
PLN03073 PLN03073
ABC transporter F family; Provisional
 467-691 4.87e-08

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 56.41  E-value: 4.87e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   467 PQTATVAFDNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYlagqniqdvslESLRR 546
Cdd:PLN03073 504 PGPPIISFSDASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF-----------RSAKV 572

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   547 AVGVVPQdavlfHNTIYYNLlygniSASPEeVYAVAKLAGLHDAILRMPHGYDTQVGERGLK----LSGGEKQRVAIARA 622
Cdd:PLN03073 573 RMAVFSQ-----HHVDGLDL-----SSNPL-LYMMRCFPGVPEQKLRAHLGSFGVTGNLALQpmytLSGGQKSRVAFAKI 641

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 8928549   623 ILKDPPVILYDEATSSLDSITEETILGAMkdVVKHRTSIFIAHRLSTVVDA-DEIIVLDQGKVAE-RGTHH 691
Cdd:PLN03073 642 TFKKPHILLLDEPSNHLDLDAVEALIQGL--VLFQGGVLMVSHDEHLISGSvDELWVVSEGKVTPfHGTFH 710
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
498-679 6.31e-08

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 55.97  E-value: 6.31e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   498 GKKVAIVGGSGSGKSTIVRLLfrfyepqkgsiylAGQ---NIQDVSLES-----LRRAVGVVPQDavlfhntiYYNLLY- 568
Cdd:PRK13409  99 GKVTGILGPNGIGKTTAVKIL-------------SGElipNLGDYEEEPswdevLKRFRGTELQN--------YFKKLYn 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   569 GNISAS--PEEVYAVAK-LAGLHDAILRmphgydtQVGERGL-------------------KLSGGEKQRVAIARAILKD 626
Cdd:PRK13409 158 GEIKVVhkPQYVDLIPKvFKGKVRELLK-------KVDERGKldevverlglenildrdisELSGGELQRVAIAAALLRD 230

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 8928549   627 PPVILYDEATSSLDsITEE-TILGAMKDVVKHRTSIFIAHRLsTVVD--ADEIIVL 679
Cdd:PRK13409 231 ADFYFFDEPTSYLD-IRQRlNVARLIRELAEGKYVLVVEHDL-AVLDylADNVHIA 284
ABCG_PDR_domain2 cd03232
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...
 486-682 6.97e-08

Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213199 [Multi-domain]  Cd Length: 192  Bit Score: 53.40  E-value: 6.97e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  486 KVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQ--KGSIYLAGQNIQdvslESLRRAVGVVPQDAVLFHN-TI 562
Cdd:cd03232  21 QLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRPLD----KNFQRSTGYVEQQDVHSPNlTV 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  563 YYNLLYGnisaspeevyavAKLaglhdailrmphgydtqvgeRGLKLSggEKQRVAIARAILKDPPVILYDEATSSLDSI 642
Cdd:cd03232  97 REALRFS------------ALL--------------------RGLSVE--QRKRLTIGVELAAKPSILFLDEPTSGLDSQ 142

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 8928549  643 TEETILGAMKDVVKH-RTSIFIAHRLSTVVDA--DEIIVLDQG 682
Cdd:cd03232 143 AAYNIVRFLKKLADSgQAILCTIHQPSASIFEkfDRLLLLKRG 185
sufC PRK09580
cysteine desulfurase ATPase component; Reviewed
 482-690 8.53e-08

cysteine desulfurase ATPase component; Reviewed


Pssm-ID: 181965 [Multi-domain]  Cd Length: 248  Bit Score: 54.03  E-value: 8.53e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   482 IEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLF--RFYEPQKGSIYLAGQNIQDVSLESlRRAVGV--------- 550
Cdd:PRK09580  11 VEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDLLELSPED-RAGEGIfmafqypve 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   551 VPQDAVLFHNTIYYNLLYGNISASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGlkLSGGEKQRVAIARAILKDPPVI 630
Cdd:PRK09580  90 IPGVSNQFFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALLKMPEDLLTRSVNVG--FSGGEKKRNDILQMAVLEPELC 167

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 8928549   631 LYDEATSSLD----SITEETIlGAMKDvvKHRTSIFIAH--RLSTVVDADEIIVLDQGKVAERGTH 690
Cdd:PRK09580 168 ILDESDSGLDidalKIVADGV-NSLRD--GKRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDF 230
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
 484-648 9.46e-08

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


Pssm-ID: 274744 [Multi-domain]  Cd Length: 552  Bit Score: 55.33  E-value: 9.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    484 GQKVL-SGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLaGQNIQdvsleslrraVGVVPQ--DAVLFHN 560
Cdd:TIGR03719 333 GDKLLiDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVK----------LAYVDQsrDALDPNK 401

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    561 TIYynllygnisaspEEVyavaklAGLHDAIL----RMP----------HGYDTQ--VGErglkLSGGEKQRVAIARAIL 624
Cdd:TIGR03719 402 TVW------------EEI------SGGLDIIKlgkrEIPsrayvgrfnfKGSDQQkkVGQ----LSGGERNRVHLAKTLK 459

                         170       180
                  ....*....|....*....|....*...
gi 8928549    625 KDPPVILYDEATSSLDSIT----EETIL 648
Cdd:TIGR03719 460 SGGNVLLLDEPTNDLDVETlralEEALL 487
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
491-686 1.79e-07

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 54.41  E-value: 1.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   491 ISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS-LESLRRAVGVVPQ---DAVLFHN-TIYYN 565
Cdd:PRK09700 282 ISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSpLDAVKKGMAYITEsrrDNGFFPNfSIAQN 361

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   566 L-------------LYGNISASPEevyavAKLAGLHDAILRMP-HGYDTQVGErglkLSGGEKQRVAIARAILKDPPVIL 631
Cdd:PRK09700 362 MaisrslkdggykgAMGLFHEVDE-----QRTAENQRELLALKcHSVNQNITE----LSGGNQQKVLISKWLCCCPEVII 432

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 8928549   632 YDEATSSLDSITEETILGAMKDVVKH-RTSIFIAHRLSTVVDA-DEIIVLDQGKVAE 686
Cdd:PRK09700 433 FDEPTRGIDVGAKAEIYKVMRQLADDgKVILMVSSELPEIITVcDRIAVFCEGRLTQ 489
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
 483-665 1.80e-07

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 54.51  E-value: 1.80e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   483 EGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAgQNIQdvsleslrraVGVVPQD-AVLFHNT 561
Cdd:PRK15064 330 DNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWS-ENAN----------IGYYAQDhAYDFEND 398

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   562 IyyNLLygnisaspeEVYAVAKLAGlHD-----AIL-RMPHGYDtQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEA 635
Cdd:PRK15064 399 L--TLF---------DWMSQWRQEG-DDeqavrGTLgRLLFSQD-DIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEP 465

                        170       180       190
                 ....*....|....*....|....*....|..
gi 8928549   636 TSSLD--SIteETILGAMKDVvkHRTSIFIAH 665
Cdd:PRK15064 466 TNHMDmeSI--ESLNMALEKY--EGTLIFVSH 493
ABC_6TM_AtABCB27_like cd18780
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ...
 154-438 2.48e-07

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: 53.02  E-value: 2.48e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  154 NIVVPFMFKYAVDSLNQMSGNmlNLSDAPNTVATMATAVLIGYGVSragaAFFNEVRNAVFGKVAQNSIRRIAKNVFLHL 233
Cdd:cd18780  12 NLALPYFFGQVIDAVTNHSGS--GGEEALRALNQAVLILLGVVLIG----SIATFLRSWLFTLAGERVVARLRKRLFSAI 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  234 HNLDLGFHLSRQTGALSKAIDRGTRGISFVLSALVFNLLPIMFEVMLVSGVLYYKCgaqfALVTLGTLGTYTAFTVAvTR 313
Cdd:cd18780  86 IAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTS----WKLTLVMLSVVPPLSIG-AV 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  314 WRTRFRIEMNKADND----AGNAAIDSLLNYETVKYFNNERYEAQRYDGflKTYETASL--KSTSTLAMLNFGQSAIFSV 387
Cdd:cd18780 161 IYGKYVRKLSKKFQDalaaASTVAEESISNIRTVRSFAKETKEVSRYSE--KINESYLLgkKLARASGGFNGFMGAAAQL 238

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 8928549  388 GLTAIMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQAL 438
Cdd:cd18780 239 AIVLVLWYGGRLVIDGELTTGLLTSFLLYTLTVAMSFAFLSSLYGDFMQAV 289
ABC_6TM_TAP1 cd18589
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ...
 223-438 2.51e-07

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: 52.86  E-value: 2.51e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  223 RRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGISFVLSAlvfNLLPIMFEVMLVSGVLYY--KCGAQFALVTLGT 300
Cdd:cd18589  69 SRLQGLVFAAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSE---NLSLLMWYLARGLFLFIFmlWLSPKLALLTALG 145

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  301 LGTYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNERYEAQRYDGFL-KTYETASLKSTS-TLAMLN 378
Cdd:cd18589 146 LPLLLLVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEEGEAQRYRQRLqKTYRLNKKEAAAyAVSMWT 225

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 8928549  379 FGQSAIF-SVGltaIMVLASQGIVAGTLTVGDLVMVngLLFQL--SLPLNFLGTVYRETRQAL 438
Cdd:cd18589 226 SSFSGLAlKVG---ILYYGGQLVTAGTVSSGDLVTF--VLYELqfTSAVEVLLSYYPSVMKAV 283
ABC_6TM_Pgp_ABCB1_D2_like cd18578
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ...
 201-418 2.61e-07

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: 53.22  E-value: 2.61e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  201 AGAAFFNEVRNAVFGKVAQNSIRRIAKNVFLHLHNLDLGFH--LSRQTGALSKAIDRGT---RGI-SFVLSALVFNLlpi 274
Cdd:cd18578  63 IVAGIAYFLQGYLFGIAGERLTRRLRKLAFRAILRQDIAWFddPENSTGALTSRLSTDAsdvRGLvGDRLGLILQAI--- 139

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  275 mfeVMLVSGV---LYYkcGAQFALVTLGTLGTYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNERY 351
Cdd:cd18578 140 ---VTLVAGLiiaFVY--GWKLALVGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDY 214

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 8928549  352 EAQRYDGFLKTYETASLKStSTLAMLNFG--QSAIFSVglTAI-----MVLasqgIVAGTLTVGDLVMV-NGLLF 418
Cdd:cd18578 215 FLEKYEEALEEPLKKGLRR-ALISGLGFGlsQSLTFFA--YALafwygGRL----VANGEYTFEQFFIVfMALIF 282
ABC_6TM_exporter_like cd18550
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
 140-438 2.76e-07

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


Pssm-ID: 349994 [Multi-domain]  Cd Length: 294  Bit Score: 52.87  E-value: 2.76e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  140 VAISLGFLGGAKAMNIVVPFMFKYAVDS---------LNQMSGNMLNLsdapnTVATMATAVLIGYGVSRAGAAFFNEVR 210
Cdd:cd18550   1 LALVLLLILLSALLGLLPPLLLREIIDDalpqgdlglLVLLALGMVAV-----AVASALLGVVQTYLSARIGQGVMYDLR 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  211 NAVFGkvaqnsirriaknvflHLHNLDLGFHLSRQTGALSKAIDRGTRGISFVLSALVFNLLPIMFEVMLVSGVLYYKcG 290
Cdd:cd18550  76 VQLYA----------------HLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLAL-D 138

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  291 AQFALVTLGTLgtytAFTVAVTRW--RTRFRIEMNKADNdagNAAIDSLLNyET--------VKYFNNERYEAQRYDGfl 360
Cdd:cd18550 139 WRLALLSLVLL----PLFVLPTRRvgRRRRKLTREQQEK---LAELNSIMQ-ETlsvsgallVKLFGREDDEAARFAR-- 208

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  361 KTYETASLKSTSTLAMLNFGQ--SAIFSVGLTAIMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQAL 438
Cdd:cd18550 209 RSRELRDLGVRQALAGRWFFAalGLFTAIGPALVYWVGGLLVIGGGLTIGTLVAFTALLGRLYGPLTQLLNIQVDLMTSL 288
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
 484-640 3.85e-07

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 53.58  E-value: 3.85e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   484 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLA-GQNI------------QDVsLESLRRAVGV 550
Cdd:PRK11819  19 KKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPApGIKVgylpqepqldpeKTV-RENVEEGVAE 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   551 VpQDAVLFHNTIYynLLYGNISASPEEVyaVAKLAGLHDAI------------------LRMPHGyDTQVGerglKLSGG 612
Cdd:PRK11819  98 V-KAALDRFNEIY--AAYAEPDADFDAL--AAEQGELQEIIdaadawdldsqleiamdaLRCPPW-DAKVT----KLSGG 167

                        170       180
                 ....*....|....*....|....*...
gi 8928549   613 EKQRVAIARAILKDPPVILYDEATSSLD 640
Cdd:PRK11819 168 ERRRVALCRLLLEKPDMLLLDEPTNHLD 195
ABC_6TM_Tm288_like cd18547
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ...
 140-425 3.88e-07

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: 52.41  E-value: 3.88e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  140 VAISLGFLGGAKAMNIVVPFMFKYAVDSLNQMSGNMLNlsDAPNTVATMATAVLIGYGVSragaAFFNEVRNAVFGKVAQ 219
Cdd:cd18547   1 LILVIILAIISTLLSVLGPYLLGKAIDLIIEGLGGGGG--VDFSGLLRILLLLLGLYLLS----ALFSYLQNRLMARVSQ 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  220 NSIRRIAKNVFLHLHNLDLGFHLSRQTGA-LSKA---IDRGTRGISFVLSALVFNLLPI--MFEVMLV-SGVLyykcgaq 292
Cdd:cd18547  75 RTVYDLRKDLFEKLQRLPLSYFDTHSHGDiMSRVtndVDNISQALSQSLTQLISSILTIvgTLIMMLYiSPLL------- 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  293 fALVTLGTLGTYTAFTVAVTRW-RTRFRIEMNKadndAG--NAAID-SLLNYETVKYFNNERYEAQRYDGFLKTYETASL 368
Cdd:cd18547 148 -TLIVLVTVPLSLLVTKFIAKRsQKYFRKQQKA----LGelNGYIEeMISGQKVVKAFNREEEAIEEFDEINEELYKASF 222

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 8928549  369 KSTSTLAML--------NFGQSAIFSVGltAIMVLasqgivAGTLTVGDLV----MVNgllfQLSLPLN 425
Cdd:cd18547 223 KAQFYSGLLmpimnfinNLGYVLVAVVG--GLLVI------NGALTVGVIQaflqYSR----QFSQPIN 279
ycf16 CHL00131
sulfate ABC transporter protein; Validated
 482-689 4.68e-07

sulfate ABC transporter protein; Validated


Pssm-ID: 214372 [Multi-domain]  Cd Length: 252  Bit Score: 51.95  E-value: 4.68e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   482 IEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRF--YEPQKGSIYLAGQNIQDvsLESLRRA------------ 547
Cdd:CHL00131  17 VNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILD--LEPEERAhlgiflafqypi 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   548 --VGVVPQDavlFHNTIYYNLL--YGNISASPEEVYAV----AKLAGLHdailrmPHGYDTQVGErglKLSGGEKQRVAI 619
Cdd:CHL00131  95 eiPGVSNAD---FLRLAYNSKRkfQGLPELDPLEFLEIinekLKLVGMD------PSFLSRNVNE---GFSGGEKKRNEI 162

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 8928549   620 ARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSI-FIAH--RLSTVVDADEIIVLDQGKVAERGT 689
Cdd:CHL00131 163 LQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIiLITHyqRLLDYIKPDYVHVMQNGKIIKTGD 235
ABC_6TM_Rv0194_D2_like cd18546
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ...
 140-437 4.69e-07

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


Pssm-ID: 349990 [Multi-domain]  Cd Length: 292  Bit Score: 52.11  E-value: 4.69e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  140 VAISLGFLGGAKAMNIVVPFMFKYAVDS-LNQMSGNMLNLsdapnTVATMATAVLIGYGVSRAgaaffnevRNAVFGKVA 218
Cdd:cd18546   1 LALALLLVVVDTAASLAGPLLVRYGIDSgVRAGDLGVLLL-----AAAAYLAVVLAGWVAQRA--------QTRLTGRTG 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  219 QNSIRRIAKNVFLHLHNLDLGFH--------LSRQTG---ALSKAIDRGtrgisfvLSALVFNLLPIMF-EVMLVsgVLy 286
Cdd:cd18546  68 ERLLYDLRLRVFAHLQRLSLDFHeretsgriMTRMTSdidALSELLQTG-------LVQLVVSLLTLVGiAVVLL--VL- 137

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  287 ykcGAQFALVTLGTLgtytAFTVAVTRWrtrFRIEMNKADNDAGNAAIDSLLNY-ET------VKYFNNERYEAQRYDGF 359
Cdd:cd18546 138 ---DPRLALVALAAL----PPLALATRW---FRRRSSRAYRRARERIAAVNADLqETlagirvVQAFRRERRNAERFAEL 207

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  360 LKTYETASLKSTSTLAMLNFGQSAIFSVGLTAIMVLASQGIVAGTLTVGDLV---MVNGLLFQlslPLNFLGTVYRETRQ 436
Cdd:cd18546 208 SDDYRDARLRAQRLVAIYFPGVELLGNLATAAVLLVGAWRVAAGTLTVGVLVaflLYLRRFFA---PIQQLSQVFDSYQQ 284


                .
gi 8928549  437 A 437
Cdd:cd18546 285 A 285
tagH PRK13545
teichoic acids export protein ATP-binding subunit; Provisional
 488-742 1.30e-06

teichoic acids export protein ATP-binding subunit; Provisional


Pssm-ID: 184130 [Multi-domain]  Cd Length: 549  Bit Score: 51.81  E-value: 1.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   488 LSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGqniqdvSLESLRRAVGVVPQDAVLfHNTIYYNLL 567
Cdd:PRK13545  40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG------SAALIAISSGLNGQLTGI-ENIELKGLM 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   568 YGNISASPEEVY-AVAKLAGLHDAILRMPHGYdtqvgerglklSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEET 646
Cdd:PRK13545 113 MGLTKEKIKEIIpEIIEFADIGKFIYQPVKTY-----------SSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKK 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   647 ILGAMKDVVKH-RTSIFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGLLANphsiYSEMwhtqssrvqnhdnpkweAKK 724
Cdd:PRK13545 182 CLDKMNEFKEQgKTIFFISHSLSQVKSfCTKALWLHYGQVKEYGDIKEVVDH----YDEF-----------------LKK 240

                        250
                 ....*....|....*...
gi 8928549   725 ENISKEEERKKLQEEIVN 742
Cdd:PRK13545 241 YNQMSVEERKDFREEQIS 258
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
 485-685 1.38e-06

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 51.65  E-value: 1.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   485 QKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS-LESL----------RRAVGVVPQ 553
Cdd:PRK10982 261 QPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNaNEAInhgfalvteeRRSTGIYAY 340

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   554 DAVLFhNTIYYNL--------LYGNISASPEEVYAVaklaglhDAILRMPHGYDTQVGErglkLSGGEKQRVAIARAILK 625
Cdd:PRK10982 341 LDIGF-NSLISNIrnyknkvgLLDNSRMKSDTQWVI-------DSMRVKTPGHRTQIGS----LSGGNQQKVIIGRWLLT 408

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 8928549   626 DPPVILYDEATSSLDSITEETILGAMKDVVKH-RTSIFIAHRLSTVVD-ADEIIVLDQGKVA 685
Cdd:PRK10982 409 QPEILMLDEPTRGIDVGAKFEIYQLIAELAKKdKGIIIISSEMPELLGiTDRILVMSNGLVA 470
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
 475-645 1.63e-06

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 51.49  E-value: 1.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   475 DNVHFEyIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYlAGQNIQDVSLESLRRAVGvvPQd 554
Cdd:PRK11147 323 ENVNYQ-IDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIH-CGTKLEVAYFDQHRAELD--PE- 397

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   555 avlfhNTIYYNLLYGN----ISASPEEVyavakLAGLHDaILRMPHGYDTQVGerglKLSGGEKQRVAIARAILKDPPVI 630
Cdd:PRK11147 398 -----KTVMDNLAEGKqevmVNGRPRHV-----LGYLQD-FLFHPKRAMTPVK----ALSGGERNRLLLARLFLKPSNLL 462

                        170
                 ....*....|....*
gi 8928549   631 LYDEATSSLDSITEE 645
Cdd:PRK11147 463 ILDEPTNDLDVETLE 477
hmuV PRK13547
heme ABC transporter ATP-binding protein;
484-698 2.11e-06

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 49.83  E-value: 2.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   484 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLF-RFYEPQ-------KGSIYLAGQNIQDVSLESLRRAVGVVPQDA 555
Cdd:PRK13547  13 HRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGGaprgarvTGDVTLNGEPLAAIDAPRLARLRAVLPQAA 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   556 V-LFHNTIYYNLLYGNISASPEEVYAVAKLAGLHDAILRMPhGYDTQVGERGLKLSGGEKQRVAIARAILK--------- 625
Cdd:PRK13547  93 QpAFAFSAREIVLLGRYPHARRAGALTHRDGEIAWQALALA-GATALVGRDVTTLSGGELARVQFARVLAQlwpphdaaq 171

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 8928549   626 DPPVILYDEATSSLDSITEETILGAMKDVVK--HRTSIFIAHRLSTVV-DADEIIVLDQGKVAERGTHHGLLANPH 698
Cdd:PRK13547 172 PPRYLLLDEPTAALDLAHQHRLLDTVRRLARdwNLGVLAIVHDPNLAArHADRIAMLADGAIVAHGAPADVLTPAH 247
ABC_6TM_TmrB_like cd18541
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ...
 141-428 5.04e-06

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: 48.95  E-value: 5.04e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  141 AISLGFLGGAKAMNIVVPFMFKYAVDSLNQMSGNMLNLsdapntvaTMATAVLIGYGVSRAGAAFFneVRNAVFGkvaqn 220
Cdd:cd18541   2 LLGILFLILVDLLQLLIPRIIGRAIDALTAGTLTASQL--------LRYALLILLLALLIGIFRFL--WRYLIFG----- 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  221 SIRRIAK----NVFLHLHNLDLGFHLSRQTGALskaIDRGTRGISFVLSALVFNLLPIMFEVMLVSGVLYykcgAQFAL- 295
Cdd:cd18541  67 ASRRIEYdlrnDLFAHLLTLSPSFYQKNRTGDL---MARATNDLNAVRMALGPGILYLVDALFLGVLVLV----MMFTIs 139

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  296 --VTLGTLGTYTAFTVAVTRW----RTRFRI------EMNkadndagNAAIDSLLNYETVKYFNNERYEAQRYDGFLKTY 363
Cdd:cd18541 140 pkLTLIALLPLPLLALLVYRLgkkiHKRFRKvqeafsDLS-------DRVQESFSGIRVIKAFVQEEAEIERFDKLNEEY 212

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 8928549  364 ETASLKststLAMLN--FGQSAIFSVGLTAIMVLA--SQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLG 428
Cdd:cd18541 213 VEKNLR----LARVDalFFPLIGLLIGLSFLIVLWygGRLVIRGTITLGDLVAFNSYLGMLIWPMMALG 277
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
 488-695 6.85e-06

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 49.23  E-value: 6.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   488 LSG-----ISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSleslrravgvvPQDAVlfHNTI 562
Cdd:PRK10762 263 LSGpgvndVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRS-----------PQDGL--ANGI 329

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   563 YY--------NLLYG-----NISASP--------------EEVYAVAKLAGLHDaiLRMPhGYDTQVGerglKLSGGEKQ 615
Cdd:PRK10762 330 VYisedrkrdGLVLGmsvkeNMSLTAlryfsraggslkhaDEQQAVSDFIRLFN--IKTP-SMEQAIG----LLSGGNQQ 402

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   616 RVAIARAILKDPPVILYDEATSSLDsiteetiLGAMKDVVKhRTSIFIAHRLSTVV----------DADEIIVLDQGKV- 684
Cdd:PRK10762 403 KVAIARGLMTRPKVLILDEPTRGVD-------VGAKKEIYQ-LINQFKAEGLSIILvssempevlgMSDRILVMHEGRIs 474

                        250
                 ....*....|....*
gi 8928549   685 ----AERGTHHGLLA 695
Cdd:PRK10762 475 geftREQATQEKLMA 489
ABC_6TM_McjD_like cd18556
Six-transmembrane helical domain of the antibacterial peptide ATP-binding cassette transporter ...
 220-438 6.92e-06

Six-transmembrane helical domain of the antibacterial peptide ATP-binding cassette transporter McjD and similar proteins; This group represents the 6-TM subunit of the ABC transporter McjD that exports the antibacterial peptide microcin J25, which is an antimicrobial peptide produced by Enterobacteriaceae against other microorganisms for survival under nutrient starvation. Thus, the ABC exporter McjD provides self-immunity of the producing bacteria through export of the toxic peptide out of the cell. Bacterial ABC exporters are typically expressed as half-transporters that contain one transmembrane domain (TMD) fused to a nucleotide-binding domain (NBD), which dimerize to form the full transporter.


Pssm-ID: 350000  Cd Length: 298  Bit Score: 48.79  E-value: 6.92e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  220 NSIRRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGISFVLSALVFNLLP----IMFEVMLVSGVLYYKCGAQFAL 295
Cdd:cd18556  74 ELIISISSSYFRYLYEQPKTFFVKENSGDITQRLNQASNDLYTLVRNLSTNILPpllqLIIAIVVILSSGDYFVAALFLL 153

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  296 VTLgtlgTYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNERYEAQRYDGFLKTYETAS---LKSTS 372
Cdd:cd18556 154 YAV----LFVINNTIFTKKIVSLRNDLMDAGRKSYSLLTDSVKNIVAAKQNNAFDFLFKRYEATLTNDRNSQkryWKLTF 229

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 8928549  373 TLAMLNFGQSAIFsVGLTAIMVLAsqGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQAL 438
Cdd:cd18556 230 KMLILNSLLNVIL-FGLSFFYSLY--GVVNGQVSIGHFVLITSYILLLSTPIESLGNMLSELRQSV 292
ABC_6TM_PrtD_LapB_HlyB_like cd18566
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ...
 182-425 7.77e-06

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


Pssm-ID: 350010 [Multi-domain]  Cd Length: 294  Bit Score: 48.35  E-value: 7.77e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  182 PNTVATMATAVLIGYGVSRAGAAFFNEVRNAVFGKVAQNSIRRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGIS 261
Cdd:cd18566  34 PNESIPTLQVLVIGVVIAILLESLLRLLRSYILAWIGARFDHRLSNAAFEHLLSLPLSFFEREPSGAHLERLNSLEQIRE 113

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  262 FVLSALVFNLLPIMFEVMLVSGVLYYkcGAQFALVTLGTLGTYTAFTVAV-TRWRTRFRiEMNKADNDAGNAAIDSLLNY 340
Cdd:cd18566 114 FLTGQALLALLDLPFVLIFLGLIWYL--GGKLVLVPLVLLGLFVLVAILLgPILRRALK-ERSRADERRQNFLIETLTGI 190

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  341 ETVKYFNNERYEAQRYDGFLKTYETASLKSTSTLAMLNfGQSAIFSVgLTAIMVLA--SQGIVAGTLTVGDLVMVNGLLF 418
Cdd:cd18566 191 HTIKAMAMEPQMLRRYERLQANAAYAGFKVAKINAVAQ-TLGQLFSQ-VSMVAVVAfgALLVINGDLTVGALIACTMLSG 268


                ....*..
gi 8928549  419 QLSLPLN 425
Cdd:cd18566 269 RVLQPLQ 275
ABC_6TM_Sav1866_like cd18554
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ...
 142-442 7.82e-06

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: 48.57  E-value: 7.82e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  142 ISLGFLGGAKAMNI--VVPFMFKYAVDSLNQmsGNMLNLSDAPNTVATMATAVLIGYGVSRAGAAFfneVRNAVFGKVAQ 219
Cdd:cd18554   1 IIITIVIGLVRFGIplLLPLILKYIVDDVIQ--GSSLTLDEKVYKLFTIIGIMFFIFLILRPPVEY---YRQYFAQWIAN 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  220 NSIRRIAKNVFLHLHNLDLGFHLSRQTGAL-SKAIDRGTRGISFVLSALVfNLLPIMFEVMLVSGVLyYKCGAQFALVTL 298
Cdd:cd18554  76 KILYDIRKDLFDHLQKLSLRYYANNRSGEIiSRVINDVEQTKDFITTGLM-NIWLDMITIIIAICIM-LVLNPKLTFVSL 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  299 GTLGTYtafTVAVTRWRTRFRI---EMNKADNDAGNAAIDSLLNYETVKYFNNERYEAQRYDGFLKTYETASLKSTS--- 372
Cdd:cd18554 154 VIFPFY---ILAVKYFFGRLRKltkERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRALKHTRwna 230

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 8928549  373 -TLAMLNfgqsAIFSVGLTAIMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDMN 442
Cdd:cd18554 231 kTFSAVN----TITDLAPLLVIGFAAYLVIEGNLTVGTLVAFVGYMERMYSPLRRLVNSFTTLTQSFASMD 297
PRK15093 PRK15093
peptide ABC transporter ATP-binding protein SapD;
608-703 7.86e-06

peptide ABC transporter ATP-binding protein SapD;


Pssm-ID: 185049 [Multi-domain]  Cd Length: 330  Bit Score: 48.65  E-value: 7.86e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   608 KLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLSTVVD-ADEIIVLDQGKV 684
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNntTILLISHDLQMLSQwADKINVLYCGQT 237

                         90
                 ....*....|....*....
gi 8928549   685 AERGTHHGLLANPHSIYSE 703
Cdd:PRK15093 238 VETAPSKELVTTPHHPYTQ 256
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
 484-684 8.55e-06

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 49.16  E-value: 8.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   484 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQK-GSIYLAGQniqDVSLESLRRAV-------------- 548
Cdd:PRK13549 274 HIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWeGEIFIDGK---PVKIRNPQQAIaqgiamvpedrkrd 350

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   549 GVVPQDAVLfHNTIYYNL----LYGNISASPEEVYAVAKLAGLHdaiLRMPHGyDTQVGerglKLSGGEKQRVAIARAIL 624
Cdd:PRK13549 351 GIVPVMGVG-KNITLAALdrftGGSRIDDAAELKTILESIQRLK---VKTASP-ELAIA----RLSGGNQQKAVLAKCLL 421

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 8928549   625 KDPPVILYDEATSSLDSITEETILGAMKDVVKHRTS-IFIAHRLSTVVD-ADEIIVLDQGKV 684
Cdd:PRK13549 422 LNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAiIVISSELPEVLGlSDRVLVMHEGKL 483
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
 609-684 9.37e-06

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 49.18  E-value: 9.37e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 8928549   609 LSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDvvkHRTSI-FIAHRLSTVVD-ADEIIVLDQGKV 684
Cdd:PRK11147 157 LSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKT---FQGSIiFISHDRSFIRNmATRIVDLDRGKL 231
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
 495-640 1.07e-05

The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.


Pssm-ID: 213203 [Multi-domain]  Cd Length: 255  Bit Score: 47.75  E-value: 1.07e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  495 VPA-GKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSI-----------YLAGQNIQDVsLESLRRA---VGVVPQDAVLFH 559
Cdd:cd03236  22 VPReGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppdwdeildEFRGSELQNY-FTKLLEGdvkVIVKPQYVDLIP 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  560 NTIYynllyGNISASPEEVYAVAKLAGLHDAiLRMPHGYDTQVGErglkLSGGEKQRVAIARAILKDPPVILYDEATSSL 639
Cdd:cd03236 101 KAVK-----GKVGELLKKKDERGKLDELVDQ-LELRHVLDRNIDQ----LSGGELQRVAIAAALARDADFYFFDEPSSYL 170


                .
gi 8928549  640 D 640
Cdd:cd03236 171 D 171
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
 607-680 4.26e-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: 44.87  E-value: 4.26e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 8928549  607 LKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKH--RTSIFIAHRLsTVVD--ADEIIVLD 680
Cdd:cd03222  70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEgkKTALVVEHDL-AVLDylSDRIHVFE 146
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
 495-667 4.57e-05

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


Pssm-ID: 130324 [Multi-domain]  Cd Length: 2272  Bit Score: 47.32  E-value: 4.57e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549     495 VPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQdVSLESLRRAVGVVPQ-DAVlfhntiyYNLLYGNisa 573
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIL-TNISDVHQNMGYCPQfDAI-------DDLLTGR--- 2030

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549     574 spEEVYAVAKLAGLHDAILRMPHGYDTQvgERGLKL---------SGGEKQRVAIARAILKDPPVILYDEATSSLDSITE 644
Cdd:TIGR01257 2031 --EHLYLYARLRGVPAEEIEKVANWSIQ--SLGLSLyadrlagtySGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQAR 2106

                          170       180
                   ....*....|....*....|....
gi 8928549     645 ETILGAMKDVVKH-RTSIFIAHRL 667
Cdd:TIGR01257 2107 RMLWNTIVSIIREgRAVVLTSHSM 2130
ABC_6TM_T1SS_like cd18555
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ...
 152-433 6.76e-05

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


Pssm-ID: 349999 [Multi-domain]  Cd Length: 294  Bit Score: 45.58  E-value: 6.76e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  152 AMNIVVPFMFKYAVDSLNqMSGNMLNLsdapNTVATMATAVLIGYGVsragaafFNEVRNAVFGKVaQNSI-RRIAKNVF 230
Cdd:cd18555  16 LLTLLIPILTQYVIDNVI-VPGNLNLL----NVLGIGILILFLLYGL-------FSFLRGYIIIKL-QTKLdKSLMSDFF 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  231 LHLHNLDLGFHLSRQTGAL-----SKAIDRG---TRGISFVLSALvfnLLPIMFEVMLVSGVLYykcgaqfALVTLgTLG 302
Cdd:cd18555  83 EHLLKLPYSFFENRSSGDLlfranSNVYIRQilsNQVISLIIDLL---LLVIYLIYMLYYSPLL-------TLIVL-LLG 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  303 TYTAFTVAVTRWRTRFRIEMNKADN-DAGNAAIDSLLNYETVKYFNNERyeaQRYDGFLKTYET---ASLKSTSTLAMLN 378
Cdd:cd18555 152 LLIVLLLLLTRKKIKKLNQEEIVAQtKVQSYLTETLYGIETIKSLGSEK---NIYKKWENLFKKqlkAFKKKERLSNILN 228

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 8928549  379 FGQSAIFSVGLTAIMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRE 433
Cdd:cd18555 229 SISSSIQFIAPLLILWIGAYLVINGELTLGELIAFSSLAGSFLTPIVSLINSYNQ 283
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
 496-677 1.13e-04

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


Pssm-ID: 213194 [Multi-domain]  Cd Length: 162  Bit Score: 43.12  E-value: 1.13e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  496 PAGKKVAIVGGSGSGKSTIVR-----LLFRFYEPQKGSIYLAGQNIQDVSLEslrrAVGVVPQdavlfhntiyynllygn 570
Cdd:cd03227  19 GEGSLTIITGPNGSGKSTILDaiglaLGGAQSATRRRSGVKAGCIVAAVSAE----LIFTRLQ----------------- 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  571 isaspeevyavaklaglhdailrmphgydtqvgerglkLSGGEKQRVAIARAI----LKDPPVILYDEATSSLDSITEET 646
Cdd:cd03227  78 --------------------------------------LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQA 119

                       170       180       190
                ....*....|....*....|....*....|..
gi 8928549  647 ILGAMKD-VVKHRTSIFIAHRLSTVVDADEII 677
Cdd:cd03227 120 LAEAILEhLVKGAQVIVITHLPELAELADKLI 151
ABC_6TM_TAP2 cd18590
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ...
 194-431 1.15e-04

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: 44.64  E-value: 1.15e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  194 IGY-GVSRAGAAFFNEVRNAVFGKVAQNSIRRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTrgisfvlsALVFNLL 272
Cdd:cd18590  39 IGLmCLFSLGSSLSAGLRGGLFMCTLSRLNLRLRHQLFSSLVQQDIGFFEKTKTGDLTSRLSTDT--------TLMSRSV 110

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  273 PIMFEVMLVS-----GVLYYKCGA--QFALVTL-GTLGTYTAFTVAVTRWRtRFRIEMNKADNDAGNAAIDSLLNYETVK 344
Cdd:cd18590 111 ALNANVLLRSlvktlGMLGFMLSLswQLTLLTLiEMPLTAIAQKVYNTYHQ-KLSQAVQDSIAKAGELAREAVSSIRTVR 189

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  345 YFNNERYEAQRYDGFLK-TYETASLKSTSTLAMLNFGQsaIFSVGLTAIMV-LASQGIVAGTLTVGDLVMVngLLFQLSL 422
Cdd:cd18590 190 SFKAEEEEACRYSEALErTYNLKDRRDTVRAVYLLVRR--VLQLGVQVLMLyCGRQLIQSGHLTTGSLVSF--ILYQKNL 265


                ....*....
gi 8928549  423 PLNFLGTVY 431
Cdd:cd18590 266 GSYVRTLVY 274
ABC_6TM_ABCB9_like cd18784
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ...
 259-431 1.19e-04

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: 44.61  E-value: 1.19e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  259 GISFVLSALVFNLLPIMFEVMLVSGVlYYKcgaqfalvtlgtlgtytaftvavtrwrtRFRIEMNKADNDAGNAAIDSLL 338
Cdd:cd18784 133 KLSWQLSLVTLIGLPLIAIVSKVYGD-YYK----------------------------KLSKAVQDSLAKANEVAEETIS 183

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  339 NYETVKYFNNERYEAQRYDGFLKtyETASLKSTSTLAMLNF-GQSAIFSVGLTAIMvLASQG--IVAGTLTVGDLVMVng 415
Cdd:cd18784 184 SIRTVRSFANEDGEANRYSEKLK--DTYKLKIKEALAYGGYvWSNELTELALTVST-LYYGGhlVITGQISGGNLISF-- 258

                       170
                ....*....|....*...
gi 8928549  416 LLFQLSL--PLNFLGTVY 431
Cdd:cd18784 259 ILYQLELgsCLESVGSVY 276
ABC_6TM_bac_exporter_ABCB8_10_like cd18575
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ...
 328-411 1.25e-04

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: 44.78  E-value: 1.25e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  328 DAGNAAIDSLLNYETVKYFNNERYEAQRYDGFLKTYETASLKSTSTLAMLNFgqSAIFSV--GLTAIMVLASQGIVAGTL 405
Cdd:cd18575 173 DLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRARALLTA--LVIFLVfgAIVFVLWLGAHDVLAGRM 250


                ....*.
gi 8928549  406 TVGDLV 411
Cdd:cd18575 251 SAGELS 256
PRK13541 PRK13541
cytochrome c biogenesis protein CcmA; Provisional
 503-640 1.39e-04

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184128 [Multi-domain]  Cd Length: 195  Bit Score: 43.71  E-value: 1.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   503 IVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSleslrravgvVPQDAVLFHN-------TIYYNL-LYGNISAS 574
Cdd:PRK13541  31 IKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIA----------KPYCTYIGHNlglklemTVFENLkFWSEIYNS 100

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 8928549   575 PEEVYAVAKLAGLHDAIlrmphgydtqvGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLD 640
Cdd:PRK13541 101 AETLYAAIHYFKLHDLL-----------DEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLS 155
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
 472-653 1.76e-04

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 44.72  E-value: 1.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   472 VAFDNVHFEYieGQKVL-SGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLaGQNIQdvsleslrraVGV 550
Cdd:PRK11819 325 IEAENLSKSF--GDRLLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETVK----------LAY 391

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   551 VPQ--DAVLFHNTIYynllygnisaspEEVyavaklAGLHDAIL----RMP----------HGYDTQ--VGErglkLSGG 612
Cdd:PRK11819 392 VDQsrDALDPNKTVW------------EEI------SGGLDIIKvgnrEIPsrayvgrfnfKGGDQQkkVGV----LSGG 449

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 8928549   613 EKQRVAIARAILKDPPVILYDEATSSLDSiteETiLGAMKD 653
Cdd:PRK11819 450 ERNRLHLAKTLKQGGNVLLLDEPTNDLDV---ET-LRALEE 486
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
603-688 4.29e-04

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 43.19  E-value: 4.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549   603 GERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVD--ADEIIVLD 680
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEqlAHELTVID 218


                 ....*...
gi 8928549   681 QGKVAERG 688
Cdd:NF000106 219 RGRVIADG 226
PLN03140 PLN03140
ABC transporter G family member; Provisional
 502-718 1.05e-03

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 42.53  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    502 AIVGGSGSGKSTIVRLLfrfyEPQKGSIYLAGqniqDVSL-------ESLRRAVGVVPQDAVlfHN---TIYYNLLYGNI 571
Cdd:PLN03140  910 ALMGVSGAGKTTLMDVL----AGRKTGGYIEG----DIRIsgfpkkqETFARISGYCEQNDI--HSpqvTVRESLIYSAF 979

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    572 SASPEEVYAVAK------------LAGLHDAILRMPhgydtqvGERGlkLSGGEKQRVAIARAILKDPPVILYDEATSSL 639
Cdd:PLN03140  980 LRLPKEVSKEEKmmfvdevmelveLDNLKDAIVGLP-------GVTG--LSTEQRKRLTIAVELVANPSIIFMDEPTSGL 1050

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    640 DSITEETILGAMKDVVKH-RTSIFIAHRLST-VVDA-DEIIVLDQ-GKVAERGThhgLLANPHSI--YSEMWHtQSSRVQ 713
Cdd:PLN03140 1051 DARAAAIVMRTVRNTVDTgRTVVCTIHQPSIdIFEAfDELLLMKRgGQVIYSGP---LGRNSHKIieYFEAIP-GVPKIK 1126


                  ....*
gi 8928549    714 NHDNP 718
Cdd:PLN03140 1127 EKYNP 1131
PLN03140 PLN03140
ABC transporter G family member; Provisional
 599-695 1.12e-03

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 42.53  E-value: 1.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549    599 DTQVGERGLK-LSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDA---- 673
Cdd:PLN03140  326 DTIVGDEMIRgISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLMSLLQPAPETfdlf 405

                          90       100
                  ....*....|....*....|..
gi 8928549    674 DEIIVLDQGKVAERGTHHGLLA 695
Cdd:PLN03140  406 DDIILLSEGQIVYQGPRDHILE 427
ABC_6TM_YwjA_like cd18549
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ...
 152-411 1.80e-03

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: 40.90  E-value: 1.80e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  152 AMNIVVPFMFKYAVDSLNQmSGNMlnlsdapNTVATMATAVLIGYGVsRAGAAFFNEVRNAVFGKVAQNSIRRiakNVFL 231
Cdd:cd18549  16 ALDLVFPLIVRYIIDDLLP-SKNL-------RLILIIGAILLALYIL-RTLLNYFVTYWGHVMGARIETDMRR---DLFE 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  232 HLHNLDLGFHLSRQTGALSkaidrgTRGIS--FVLSALVFNLLpimfEVMLVSGVLYykCGA---------QFALVTLGT 300
Cdd:cd18549  84 HLQKLSFSFFDNNKTGQLM------SRITNdlFDISELAHHGP----EDLFISIITI--IGSfiilltinvPLTLIVFAL 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  301 LGTYTAFTVAVT-RWRTRFRieMNKADNDAGNAAI-DSLLNYETVKYFNNERYEAQRYDGFLKTYETAslKSTSTLAMLN 378
Cdd:cd18549 152 LPLMIIFTIYFNkKMKKAFR--RVREKIGEINAQLeDSLSGIRVVKAFANEEYEIEKFDEGNDRFLES--KKKAYKAMAY 227

                       250       260       270
                ....*....|....*....|....*....|....*
gi 8928549  379 FGQSAIFSVGLTAIMVLASQG--IVAGTLTVGDLV 411
Cdd:cd18549 228 FFSGMNFFTNLLNLVVLVAGGyfIIKGEITLGDLV 262
ABC_6TM_PrtD_LapB_HlyB_like cd18782
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ...
 189-421 5.95e-03

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


Pssm-ID: 350055 [Multi-domain]  Cd Length: 294  Bit Score: 39.50  E-value: 5.95e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  189 ATAVLIGYGVSRAGAAFFNEV----RNAVFGKVAQNSIRRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDR--------- 255
Cdd:cd18782  37 DLATLYVIGVVMLVAALLEAVltalRTYLFTDTANRIDLELGGTIIDHLLRLPLGFFDKRPVGELSTRISEldtirgflt 116

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  256 GTRGISFVLSALVFNLLPIMFevmLVSGVLyykcgaqfALVTLGTLGTYTAFTVAVTRwRTRFRIEMNKADNDAGNAA-I 334
Cdd:cd18782 117 GTALTTLLDVLFSVIYIAVLF---SYSPLL--------TLVVLATVPLQLLLTFLFGP-ILRRQIRRRAEASAKTQSYlV 184

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 8928549  335 DSLLNYETVKYFNNE---RYEAQ-RYDGFL-KTYETASLKSTS--TLAMLNFGQSAIFsVGLTAIMVLAsqgivaGTLTV 407
Cdd:cd18782 185 ESLTGIQTVKAQNAElkaRWRWQnRYARSLgEGFKLTVLGTTSgsLSQFLNKLSSLLV-LWVGAYLVLR------GELTL 257

                       250       260
                ....*....|....*....|.
gi 8928549  408 GDLV-------MVNGLLFQLS 421
Cdd:cd18782 258 GQLIafrilsgYVTGPILRLS 278
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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