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Conserved domains on  [gi|2569209806|ref|NP_001410903|]
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iron-sulfur clusters transporter ABCB7, mitochondrial [Danio rerio]

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 ...
 116-699 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: 887.24  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 116 FTYVWPKDRPDLRARVVISLSLLAGAKITNVMVPFMFKYAVDslnqmsghmlNLSDAPNTVVTMATAVLIGYGVSRTGSA 195
Cdd:COG5265    23 LLLLLLPPYLRRRRRALAALLLLLLAAALALVVPPLLKDAID----------ALLSGAAALLVVPVGLLLAYGLLRLLSV 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 196 LFNELRNAVFGKVAQSSIRRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGISFVLSALVFNLGPTLFEMMLVSGI 275
Cdd:COG5265    93 LFGELRDALFARVTQRAVRRLALEVFRHLHALSLRFHLERQTGGLSRDIERGTKGIEFLLRFLLFNILPTLLEIALVAGI 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 276 LYYKCGGHFALVTLGTLSAYTAFTVAVTQWRTQFRIEMNKADNEAGNAAIDSLLNYETVKYFNNEKYEAERYDGFLKVYE 355
Cdd:COG5265   173 LLVKYDWWFALITLVTVVLYIAFTVVVTEWRTKFRREMNEADSEANTRAVDSLLNYETVKYFGNEAREARRYDEALARYE 252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 356 SSSLKTTSTLAMLNFGQSAIFSVGLTAIMVLASKGIMSGTMTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDMNTL 435
Cdd:COG5265   253 RAAVKSQTSLALLNFGQALIIALGLTAMMLMAAQGVVAGTMTVGDFVLVNAYLIQLYIPLNFLGFVYREIRQALADMERM 332

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 436 FTLLSVDTKIKEKEMAPPLIVTPqeATIRFEDVYFEYLEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEP 515
Cdd:COG5265   333 FDLLDQPPEVADAPDAPPLVVGG--GEVRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDV 410

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 516 QQGNIYIAGQNIRDVGLESLRKAVGVVPQDAVLFHNTIFYNLMYGNINATAEDVYRVARLAGIHDAILKMPHKYDTQVGE 595
Cdd:COG5265   411 TSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGE 490

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 596 RGLKLSGGEKQRVAIARAILKNPPILLYDEATSSLDSVTEENILTSMKEMVKDRTSVFIAHRLSTIVDADEIIVLNQGKV 675
Cdd:COG5265   491 RGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRI 570

                         570       580
                  ....*....|....*....|....
gi 2569209806 676 AERGNHQTLLDTPGsLYANLWNTQ 699
Cdd:COG5265   571 VERGTHAELLAQGG-LYAQMWARQ 593
 
Name Accession Description Interval E-value
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
 116-699 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: 887.24  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 116 FTYVWPKDRPDLRARVVISLSLLAGAKITNVMVPFMFKYAVDslnqmsghmlNLSDAPNTVVTMATAVLIGYGVSRTGSA 195
Cdd:COG5265    23 LLLLLLPPYLRRRRRALAALLLLLLAAALALVVPPLLKDAID----------ALLSGAAALLVVPVGLLLAYGLLRLLSV 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 196 LFNELRNAVFGKVAQSSIRRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGISFVLSALVFNLGPTLFEMMLVSGI 275
Cdd:COG5265    93 LFGELRDALFARVTQRAVRRLALEVFRHLHALSLRFHLERQTGGLSRDIERGTKGIEFLLRFLLFNILPTLLEIALVAGI 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 276 LYYKCGGHFALVTLGTLSAYTAFTVAVTQWRTQFRIEMNKADNEAGNAAIDSLLNYETVKYFNNEKYEAERYDGFLKVYE 355
Cdd:COG5265   173 LLVKYDWWFALITLVTVVLYIAFTVVVTEWRTKFRREMNEADSEANTRAVDSLLNYETVKYFGNEAREARRYDEALARYE 252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 356 SSSLKTTSTLAMLNFGQSAIFSVGLTAIMVLASKGIMSGTMTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDMNTL 435
Cdd:COG5265   253 RAAVKSQTSLALLNFGQALIIALGLTAMMLMAAQGVVAGTMTVGDFVLVNAYLIQLYIPLNFLGFVYREIRQALADMERM 332

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 436 FTLLSVDTKIKEKEMAPPLIVTPqeATIRFEDVYFEYLEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEP 515
Cdd:COG5265   333 FDLLDQPPEVADAPDAPPLVVGG--GEVRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDV 410

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 516 QQGNIYIAGQNIRDVGLESLRKAVGVVPQDAVLFHNTIFYNLMYGNINATAEDVYRVARLAGIHDAILKMPHKYDTQVGE 595
Cdd:COG5265   411 TSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGE 490

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 596 RGLKLSGGEKQRVAIARAILKNPPILLYDEATSSLDSVTEENILTSMKEMVKDRTSVFIAHRLSTIVDADEIIVLNQGKV 675
Cdd:COG5265   491 RGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRI 570

                         570       580
                  ....*....|....*....|....
gi 2569209806 676 AERGNHQTLLDTPGsLYANLWNTQ 699
Cdd:COG5265   571 VERGTHAELLAQGG-LYAQMWARQ 593
ABC_6TM_ATM1_ABCB7 cd18582
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ...
 134-435 4.16e-168

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: 485.08  E-value: 4.16e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 134 SLSLLAGAKITNVMVPFMFKYAVDSLnqmsghmlnlSDAPNTVVTMATAVLIGYGVSRTGSALFNELRNAVFGKVAQSSI 213
Cdd:cd18582     1 ALLLLVLAKLLNVAVPFLLKYAVDAL----------SAPASALLAVPLLLLLAYGLARILSSLFNELRDALFARVSQRAV 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 214 RRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGISFVLSALVFNLGPTLFEMMLVSGILYYKCGGHFALVTLGTLS 293
Cdd:cd18582    71 RRLALRVFRHLHSLSLRFHLSRKTGALSRAIERGTRGIEFLLRFLLFNILPTILELLLVCGILWYLYGWSYALITLVTVA 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 294 AYTAFTVAVTQWRTQFRIEMNKADNEAGNAAIDSLLNYETVKYFNNEKYEAERYDGFLKVYESSSLKTTSTLAMLNFGQS 373
Cdd:cd18582   151 LYVAFTIKVTEWRTKFRREMNEADNEANAKAVDSLLNYETVKYFNNEEYEAERYDKALAKYEKAAVKSQTSLALLNIGQA 230

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2569209806 374 AIFSVGLTAIMVLASKGIMSGTMTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDMNTL 435
Cdd:cd18582   231 LIISLGLTAIMLLAAQGVVAGTLTVGDFVLVNTYLLQLYQPLNFLGFVYREIRQSLIDMEKL 292
MsbA_rel TIGR02204
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ...
 119-695 1.36e-100

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: 321.26  E-value: 1.36e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 119 VWPKDRPdLRARVVISL-SLLAGAKITnVMVPFMFKYAVD-SLNQMSGHMLNLSDAPNTVVTMATAVLIG---YGVSRTG 193
Cdd:TIGR02204   9 LWPFVRP-YRGRVLAALvALLITAAAT-LSLPYAVRLMIDhGFSKDSSGLLNRYFAFLLVVALVLALGTAarfYLVTWLG 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 194 SALFNELRNAVFGkvaqssirriaknvflHLHNLDLGFHLSRQTGALskaIDRGTRGISFVLSALVFNLGPTLFEMMLVS 273
Cdd:TIGR02204  87 ERVVADIRRAVFA----------------HLISLSPSFFDKNRSGEV---VSRLTTDTTLLQSVIGSSLSMALRNALMCI 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 274 G--ILYYKCGGHFALVTLGTLSAYTAFTVAVTQWRTQFRIEMNKADNEAGNAAIDSLLNYETVKYFNNEKYEAERYDGFL 351
Cdd:TIGR02204 148 GglIMMFITSPKLTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAV 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 352 -KVYESSSLKTTSTLAMLNFGQSAIFSvGLTAIMVLASKGIMSGTMTVGDL-------VMVNGLLFQLSlplnflgTVYR 423
Cdd:TIGR02204 228 eKAYEAARQRIRTRALLTAIVIVLVFG-AIVGVLWVGAHDVIAGKMSAGTLgqfvfyaVMVAGSIGTLS-------EVWG 299

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 424 ETRQALIDMNTLFTLLSVDTKIKEKEmAPPLIVTPQEATIRFEDVYFEYLE--GQKVLNGVSFEVPAGKKVAIVGGSGSG 501
Cdd:TIGR02204 300 ELQRAAGAAERLIELLQAEPDIKAPA-HPKTLPVPLRGEIEFEQVNFAYPArpDQPALDGLNLTVRPGETVALVGPSGAG 378

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 502 KSTIVRLLFRFYEPQQGNIYIAGQNIRDVGLESLRKAVGVVPQDAVLFHNTIFYNLMYGNINATAEDVYRVARLAGIHDA 581
Cdd:TIGR02204 379 KSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEF 458

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 582 ILKMPHKYDTQVGERGLKLSGGEKQRVAIARAILKNPPILLYDEATSSLDSVTEENILTSMKEMVKDRTSVFIAHRLSTI 661
Cdd:TIGR02204 459 ISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATV 538

                         570       580       590
                  ....*....|....*....|....*....|....
gi 2569209806 662 VDADEIIVLNQGKVAERGNHQTLLDTpGSLYANL 695
Cdd:TIGR02204 539 LKADRIVVMDQGRIVAQGTHAELIAK-GGLYARL 571
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
214-693 5.74e-94

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 304.19  E-value: 5.74e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 214 RRIA--KNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGISFV--------LSALV--FNLGPTLFEMMLVSGILyykcg 281
Cdd:PRK13657   87 RRLAvlTEYFERIIQLPLAWHSQRGSGRALHTLLRGTDALFGLwlefmrehLATLValVVLLPLALFMNWRLSLV----- 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 282 ghfaLVTLGTlsAYTAFTVAVTQwRT---QFRIEMNKADNEAgnAAIDSLLNYETVKYFNNEKYEAERYDGFLKVYESSS 358
Cdd:PRK13657  162 ----LVVLGI--VYTLITTLVMR-KTkdgQAAVEEHYHDLFA--HVSDAIGNVSVVQSYNRIEAETQALRDIADNLLAAQ 232

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 359 LKTTSTLAMLNFGQSAIFSVGLTAIMVLASKGIMSGTMTVGDLVMVNG---LLFQ-LSLPLNFLGTVYRETRQalidMNT 434
Cdd:PRK13657  233 MPVLSWWALASVLNRAASTITMLAILVLGAALVQKGQLRVGEVVAFVGfatLLIGrLDQVVAFINQVFMAAPK----LEE 308

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 435 LFTLLSVDTKIKEKEMAPPLivTPQEATIRFEDVYFEYLEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYE 514
Cdd:PRK13657  309 FFEVEDAVPDVRDPPGAIDL--GRVKGAVEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFD 386

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 515 PQQGNIYIAGQNIRDVGLESLRKAVGVVPQDAVLFHNTIFYNLMYGNINATAEDVYRVARLAGIHDAILKMPHKYDTQVG 594
Cdd:PRK13657  387 PQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVG 466

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 595 ERGLKLSGGEKQRVAIARAILKNPPILLYDEATSSLDSVTEENILTSMKEMVKDRTSVFIAHRLSTIVDADEIIVLNQGK 674
Cdd:PRK13657  467 ERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGR 546

                         490
                  ....*....|....*....
gi 2569209806 675 VAERGNHQTLLDTPGSLYA 693
Cdd:PRK13657  547 VVESGSFDELVARGGRFAA 565
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 479-628 1.02e-43

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: 154.34  E-value: 1.02e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 479 LNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGLESLRKAVGVVPQDAVLF-HNTIFYNL 557
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2569209806 558 MYGninATAEDVYRVARLAGIHDAI--LKMPHKYDTQVGERGLKLSGGEKQRVAIARAILKNPPILLYDEATS 628
Cdd:pfam00005  81 RLG---LLLKGLSKREKDARAEEALekLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
474-670 1.82e-15

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 75.35  E-value: 1.82e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 474 EGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGqnirdvgleslRKAVGVVPQ----DAVLf 549
Cdd:NF040873    3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQrsevPDSL- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 550 hntifynlmygniNATAEDVYRVARLAgiHDAILKMPHKYDTQVGERGLK--------------LSGGEKQRVAIARAIL 615
Cdd:NF040873   71 -------------PLTVRDLVAMGRWA--RRGLWRRLTRDDRAAVDDALErvgladlagrqlgeLSGGQRQRALLAQGLA 135

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2569209806 616 KNPPILLYDEATSSLDSVTEENILTSMKEMVKD-RTSVFIAHRLSTIVDADEIIVL 670
Cdd:NF040873  136 QEADLLLLDEPTTGLDAESRERIIALLAEEHARgATVVVVTHDLELVRRADPCVLL 191
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 489-668 4.63e-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: 61.62  E-value: 4.63e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806  489 GKKVAIVGGSGSGKSTIVRLLFRFYEPQQGN-IYIAGQNIRDVGLESLRKavgvvpqdavlfhntifynlmygninatae 567
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPGGGvIYIDGEDILEEVLDQLLL------------------------------ 51

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806  568 dvyrvarlagihdailkmphkydTQVGERGLKLSGGEKQRVAIARAILKNPPILLYDEATSSLDSVTEENIL------TS 641
Cdd:smart00382  52 -----------------------IIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleelrLL 108

                          170       180
                   ....*....|....*....|....*..
gi 2569209806  642 MKEMVKDRTSVFIAHRLSTIVDADEII 668
Cdd:smart00382 109 LLLKSEKNLTVILTTNDEKDLGPALLR 135
GguA NF040905
sugar ABC transporter ATP-binding protein;
475-677 3.53e-10

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 62.88  E-value: 3.53e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 475 GQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYePQ---QGNIYIAGQ-----NIRDvgleSLRKAVGVVPQD- 545
Cdd:NF040905   13 GVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGEvcrfkDIRD----SEALGIVIIHQEl 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 546 AVLFHNTIFYNLMYGNINATA-----EDVYRVAR--LA--GIHDAilkmPhkyDTQVGERGLklsgGEKQRVAIARAILK 616
Cdd:NF040905   88 ALIPYLSIAENIFLGNERAKRgvidwNETNRRARelLAkvGLDES----P---DTLVTDIGV----GKQQLVEIAKALSK 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2569209806 617 NPPILLYDEATSSL---DSvteENILTSMKEMvKDR--TSVFIAHRLSTIVD-ADEIIVLNQGKVAE 677
Cdd:NF040905  157 DVKLLILDEPTAALneeDS---AALLDLLLEL-KAQgiTSIIISHKLNEIRRvADSITVLRDGRTIE 219
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
594-679 1.06e-05

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 48.19  E-value: 1.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 594 GERGLKLSGGEKQRVAIARAILKNPPILLYDEATSSLDSVTEENILTSMKEMVKDRTSVFIAHRLSTIVD--ADEIIVLN 671
Cdd:NF000106  139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEqlAHELTVID 218


                  ....*...
gi 2569209806 672 QGKVAERG 679
Cdd:NF000106  219 RGRVIADG 226
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
463-631 3.00e-04

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 44.35  E-value: 3.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 463 IRFEDVYFEYleGQKV-LNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDvglESLRKAVG- 540
Cdd:NF033858    2 ARLEGVSHRY--GKTVaLDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAD---ARHRRAVCp 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 541 ---VVPQDavLFHN-----TIFYNLMYgninataedvyrVARLAGiHDAilkmphkydtqvGER-----------GL--- 598
Cdd:NF033858   77 riaYMPQG--LGKNlyptlSVFENLDF------------FGRLFG-QDA------------AERrrridellratGLapf 129

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2569209806 599 ------KLSGGEKQRVAIARAILKNPPILLYDEATSSLD 631
Cdd:NF033858  130 adrpagKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVD 168
GguA NF040905
sugar ABC transporter ATP-binding protein;
475-675 6.86e-04

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 42.85  E-value: 6.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 475 GQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLF-RFYEPQ-QGNIYIAGQNIR--------DVGL----ESlRKAVG 540
Cdd:NF040905  272 ERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFgRSYGRNiSGTVFKDGKEVDvstvsdaiDAGLayvtED-RKGYG 350

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 541 VVPQDAVLfHNTIFYNL----MYGNINATAEdvYRVARlaGIHDAI-LKMPhkydtQVGERGLKLSGGEKQRVAIARAIL 615
Cdd:NF040905  351 LNLIDDIK-RNITLANLgkvsRRGVIDENEE--IKVAE--EYRKKMnIKTP-----SVFQKVGNLSGGNQQKVVLSKWLF 420

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2569209806 616 KNPPILLYDEATSSLDSVTEENILTSMKEMVKD-RTSVFIAHRLSTIVD-ADEIIVLNQGKV 675
Cdd:NF040905  421 TDPDVLILDEPTRGIDVGAKYEIYTIINELAAEgKGVIVISSELPELLGmCDRIYVMNEGRI 482
 
Name Accession Description Interval E-value
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
 116-699 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: 887.24  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 116 FTYVWPKDRPDLRARVVISLSLLAGAKITNVMVPFMFKYAVDslnqmsghmlNLSDAPNTVVTMATAVLIGYGVSRTGSA 195
Cdd:COG5265    23 LLLLLLPPYLRRRRRALAALLLLLLAAALALVVPPLLKDAID----------ALLSGAAALLVVPVGLLLAYGLLRLLSV 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 196 LFNELRNAVFGKVAQSSIRRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGISFVLSALVFNLGPTLFEMMLVSGI 275
Cdd:COG5265    93 LFGELRDALFARVTQRAVRRLALEVFRHLHALSLRFHLERQTGGLSRDIERGTKGIEFLLRFLLFNILPTLLEIALVAGI 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 276 LYYKCGGHFALVTLGTLSAYTAFTVAVTQWRTQFRIEMNKADNEAGNAAIDSLLNYETVKYFNNEKYEAERYDGFLKVYE 355
Cdd:COG5265   173 LLVKYDWWFALITLVTVVLYIAFTVVVTEWRTKFRREMNEADSEANTRAVDSLLNYETVKYFGNEAREARRYDEALARYE 252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 356 SSSLKTTSTLAMLNFGQSAIFSVGLTAIMVLASKGIMSGTMTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDMNTL 435
Cdd:COG5265   253 RAAVKSQTSLALLNFGQALIIALGLTAMMLMAAQGVVAGTMTVGDFVLVNAYLIQLYIPLNFLGFVYREIRQALADMERM 332

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 436 FTLLSVDTKIKEKEMAPPLIVTPqeATIRFEDVYFEYLEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEP 515
Cdd:COG5265   333 FDLLDQPPEVADAPDAPPLVVGG--GEVRFENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDV 410

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 516 QQGNIYIAGQNIRDVGLESLRKAVGVVPQDAVLFHNTIFYNLMYGNINATAEDVYRVARLAGIHDAILKMPHKYDTQVGE 595
Cdd:COG5265   411 TSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGE 490

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 596 RGLKLSGGEKQRVAIARAILKNPPILLYDEATSSLDSVTEENILTSMKEMVKDRTSVFIAHRLSTIVDADEIIVLNQGKV 675
Cdd:COG5265   491 RGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRI 570

                         570       580
                  ....*....|....*....|....
gi 2569209806 676 AERGNHQTLLDTPGsLYANLWNTQ 699
Cdd:COG5265   571 VERGTHAELLAQGG-LYAQMWARQ 593
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
107-699 1.76e-177

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 520.11  E-value: 1.76e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 107 NSSKILGAMFTYVWPkdrpdLRARVVISLSLLAGAKITNVMVPFMFKYAVDSLnqmsghmlnLSDAPNTVVTMATAVLIG 186
Cdd:COG1132     4 SPRKLLRRLLRYLRP-----YRGLLILALLLLLLSALLELLLPLLLGRIIDAL---------LAGGDLSALLLLLLLLLG 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 187 YGVsrtGSALFNELRNAVFGKVAQSSIRRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGISFVLSALVFNLGPTL 266
Cdd:COG1132    70 LAL---LRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSV 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 267 FEMMLVSGILYYKcGGHFALVTLGTLSAYTAFTVAVTQWRTQFRIEMNKADNEAGNAAIDSLLNYETVKYFNNEKYEAER 346
Cdd:COG1132   147 VTLIGALVVLFVI-DWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELER 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 347 YDGFLKVYESSSLKTTSTLAMLNFGQSAIFSVGLTAIMVLASKGIMSGTMTVGDLVMVNGLLFQLSLPLNFLGTVYRETR 426
Cdd:COG1132   226 FREANEELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQ 305

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 427 QALIDMNTLFTLLSVDTKIKEKEMAPPLivTPQEATIRFEDVYFEYLEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIV 506
Cdd:COG1132   306 RALASAERIFELLDEPPEIPDPPGAVPL--PPVRGEIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLV 383

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 507 RLLFRFYEPQQGNIYIAGQNIRDVGLESLRKAVGVVPQDAVLFHNTIFYNLMYGNINATAEDVYRVARLAGIHDAILKMP 586
Cdd:COG1132   384 NLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALP 463

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 587 HKYDTQVGERGLKLSGGEKQRVAIARAILKNPPILLYDEATSSLDSVTEENILTSMKEMVKDRTSVFIAHRLSTIVDADE 666
Cdd:COG1132   464 DGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADR 543

                         570       580       590
                  ....*....|....*....|....*....|...
gi 2569209806 667 IIVLNQGKVAERGNHQTLLDTPGsLYANLWNTQ 699
Cdd:COG1132   544 ILVLDDGRIVEQGTHEELLARGG-LYARLYRLQ 575
ABC_6TM_ATM1_ABCB7 cd18582
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ...
 134-435 4.16e-168

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: 485.08  E-value: 4.16e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 134 SLSLLAGAKITNVMVPFMFKYAVDSLnqmsghmlnlSDAPNTVVTMATAVLIGYGVSRTGSALFNELRNAVFGKVAQSSI 213
Cdd:cd18582     1 ALLLLVLAKLLNVAVPFLLKYAVDAL----------SAPASALLAVPLLLLLAYGLARILSSLFNELRDALFARVSQRAV 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 214 RRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGISFVLSALVFNLGPTLFEMMLVSGILYYKCGGHFALVTLGTLS 293
Cdd:cd18582    71 RRLALRVFRHLHSLSLRFHLSRKTGALSRAIERGTRGIEFLLRFLLFNILPTILELLLVCGILWYLYGWSYALITLVTVA 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 294 AYTAFTVAVTQWRTQFRIEMNKADNEAGNAAIDSLLNYETVKYFNNEKYEAERYDGFLKVYESSSLKTTSTLAMLNFGQS 373
Cdd:cd18582   151 LYVAFTIKVTEWRTKFRREMNEADNEANAKAVDSLLNYETVKYFNNEEYEAERYDKALAKYEKAAVKSQTSLALLNIGQA 230

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2569209806 374 AIFSVGLTAIMVLASKGIMSGTMTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDMNTL 435
Cdd:cd18582   231 LIISLGLTAIMLLAAQGVVAGTLTVGDFVLVNTYLLQLYQPLNFLGFVYREIRQSLIDMEKL 292
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
 463-699 4.71e-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: 418.56  E-value: 4.71e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 463 IRFEDVYFEYLEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGLESLRKAVGVV 542
Cdd:cd03253     1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 543 PQDAVLFHNTIFYNLMYGNINATAEDVYRVARLAGIHDAILKMPHKYDTQVGERGLKLSGGEKQRVAIARAILKNPPILL 622
Cdd:cd03253    81 PQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2569209806 623 YDEATSSLDSVTEENILTSMKEMVKDRTSVFIAHRLSTIVDADEIIVLNQGKVAERGNHQTLLDtPGSLYANLWNTQ 699
Cdd:cd03253   161 LDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLA-KGGLYAEMWKAQ 236
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
 85-700 7.01e-143

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: 435.80  E-value: 7.01e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806  85 QCWHGNAgggLSADPKNVLKEVNSSKI-LGAMFTYVWPkDRPDLRArvVISLSLLAGakITNVMVPFMFKYAVDSLnqMS 163
Cdd:COG2274   119 ESWTGVA---LLLEPTPEFDKRGEKPFgLRWFLRLLRR-YRRLLLQ--VLLASLLIN--LLALATPLFTQVVIDRV--LP 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 164 GHMLNlsdapnTVVTMATAVLIGYGvsrtGSALFNELRNAVFGKVAQSSIRRIAKNVFLHLHNLDLGFHLSRQTGALSKA 243
Cdd:COG2274   189 NQDLS------TLWVLAIGLLLALL----FEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASR 258

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 244 IdRGTRGI-SFVLSALVFNLGPTLFemMLVSGIL--YYkcGGHFALVTLGTLSAYTAFTVAVTQWRTQFRIEMNKADNEA 320
Cdd:COG2274   259 F-RDVESIrEFLTGSLLTALLDLLF--VLIFLIVlfFY--SPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKR 333

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 321 GNAAIDSLLNYETVKYFNNEKYEAERYDGFLKVYESSSLKTTSTLAMLNFGQSAIFSVGLTAIMVLASKGIMSGTMTVGD 400
Cdd:COG2274   334 QSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTLGQ 413

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 401 LVMVNGLLFQLSLPLNFLGTVYRETRQALIDMNTLFTLLSVDTkikEKEMAPPLIVTPQ-EATIRFEDVYFEYLE-GQKV 478
Cdd:COG2274   414 LIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDILDLPP---EREEGRSKLSLPRlKGDIELENVSFRYPGdSPPV 490

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 479 LNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGLESLRKAVGVVPQDAVLFHNTIFYNLM 558
Cdd:COG2274   491 LDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENIT 570

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 559 YGNINATAEDVYRVARLAGIHDAILKMPHKYDTQVGERGLKLSGGEKQRVAIARAILKNPPILLYDEATSSLDSVTEENI 638
Cdd:COG2274   571 LGDPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAII 650

                         570       580       590       600       610       620
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2569209806 639 LTSMKEMVKDRTSVFIAHRLSTIVDADEIIVLNQGKVAERGNHQTLLDTPGsLYANLWNTQN 700
Cdd:COG2274   651 LENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKG-LYAELVQQQL 711
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
 463-696 1.41e-106

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: 324.57  E-value: 1.41e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 463 IRFEDVYFEYL-EGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGLESLRKAVGV 541
Cdd:cd03251     1 VEFKNVTFRYPgDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 542 VPQDAVLFHNTIFYNLMYGNINATAEDVYRVARLAGIHDAILKMPHKYDTQVGERGLKLSGGEKQRVAIARAILKNPPIL 621
Cdd:cd03251    81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2569209806 622 LYDEATSSLDSVTEENILTSMKEMVKDRTSVFIAHRLSTIVDADEIIVLNQGKVAERGNHQTLLDTpGSLYANLW 696
Cdd:cd03251   161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQ-GGVYAKLH 234
ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 cd18560
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ...
 134-435 1.20e-101

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: 314.16  E-value: 1.20e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 134 SLSLLAGAKITNVMVPFMFKYAVDSLnqmsghmlnlSDAPNTVVTMATAVLIGYGVSRTGSALFNELRNAVFGKVAQSSI 213
Cdd:cd18560     1 SLLLLILGKACNVLAPLFLGRAVNAL----------TLAKVKDLESAVTLILLYALLRFSSKLLKELRSLLYRRVQQNAY 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 214 RRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGISFVLSALVFNLGPTLFEMMLVSGILYYKCGGHFALVTLGTLS 293
Cdd:cd18560    71 RELSLKTFAHLHSLSLDWHLSKKTGEVVRIMDRGTESANTLLSYLVFYLVPTLLELIVVSVVFAFHFGAWLALIVFLSVL 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 294 AYTAFTVAVTQWRTQFRIEMNKADNEAGNAAIDSLLNYETVKYFNNEKYEAERYDGFLKVYESSSLKTTSTLAMLNFGQS 373
Cdd:cd18560   151 LYGVFTIKVTEWRTKFRRAANKKDNEAHDIAVDSLLNFETVKYFTNEKYEVDRYGEAVKEYQKSSVKVQASLSLLNVGQQ 230

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2569209806 374 AIFSVGLTAIMVLASKGIMSGTMTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDMNTL 435
Cdd:cd18560   231 LIIQLGLTLGLLLAGYRVVDGGLSVGDFVAVNTYIFQLFQPLNFLGTIYRMIIQSLTDMENL 292
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
 463-699 9.99e-101

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: 309.47  E-value: 9.99e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 463 IRFEDVYFEYLE--GQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGLESLRKAVG 540
Cdd:cd03249     1 IEFKNVSFRYPSrpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 541 VVPQDAVLFHNTIFYNLMYGNINATAEDVYRVARLAGIHDAILKMPHKYDTQVGERGLKLSGGEKQRVAIARAILKNPPI 620
Cdd:cd03249    81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2569209806 621 LLYDEATSSLDSVTEENILTSMKEMVKDRTSVFIAHRLSTIVDADEIIVLNQGKVAERGNHQTLLDTPGsLYANLWNTQ 699
Cdd:cd03249   161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKG-VYAKLVKAQ 238
MsbA_rel TIGR02204
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ...
 119-695 1.36e-100

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: 321.26  E-value: 1.36e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 119 VWPKDRPdLRARVVISL-SLLAGAKITnVMVPFMFKYAVD-SLNQMSGHMLNLSDAPNTVVTMATAVLIG---YGVSRTG 193
Cdd:TIGR02204   9 LWPFVRP-YRGRVLAALvALLITAAAT-LSLPYAVRLMIDhGFSKDSSGLLNRYFAFLLVVALVLALGTAarfYLVTWLG 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 194 SALFNELRNAVFGkvaqssirriaknvflHLHNLDLGFHLSRQTGALskaIDRGTRGISFVLSALVFNLGPTLFEMMLVS 273
Cdd:TIGR02204  87 ERVVADIRRAVFA----------------HLISLSPSFFDKNRSGEV---VSRLTTDTTLLQSVIGSSLSMALRNALMCI 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 274 G--ILYYKCGGHFALVTLGTLSAYTAFTVAVTQWRTQFRIEMNKADNEAGNAAIDSLLNYETVKYFNNEKYEAERYDGFL 351
Cdd:TIGR02204 148 GglIMMFITSPKLTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAV 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 352 -KVYESSSLKTTSTLAMLNFGQSAIFSvGLTAIMVLASKGIMSGTMTVGDL-------VMVNGLLFQLSlplnflgTVYR 423
Cdd:TIGR02204 228 eKAYEAARQRIRTRALLTAIVIVLVFG-AIVGVLWVGAHDVIAGKMSAGTLgqfvfyaVMVAGSIGTLS-------EVWG 299

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 424 ETRQALIDMNTLFTLLSVDTKIKEKEmAPPLIVTPQEATIRFEDVYFEYLE--GQKVLNGVSFEVPAGKKVAIVGGSGSG 501
Cdd:TIGR02204 300 ELQRAAGAAERLIELLQAEPDIKAPA-HPKTLPVPLRGEIEFEQVNFAYPArpDQPALDGLNLTVRPGETVALVGPSGAG 378

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 502 KSTIVRLLFRFYEPQQGNIYIAGQNIRDVGLESLRKAVGVVPQDAVLFHNTIFYNLMYGNINATAEDVYRVARLAGIHDA 581
Cdd:TIGR02204 379 KSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEF 458

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 582 ILKMPHKYDTQVGERGLKLSGGEKQRVAIARAILKNPPILLYDEATSSLDSVTEENILTSMKEMVKDRTSVFIAHRLSTI 661
Cdd:TIGR02204 459 ISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATV 538

                         570       580       590
                  ....*....|....*....|....*....|....
gi 2569209806 662 VDADEIIVLNQGKVAERGNHQTLLDTpGSLYANL 695
Cdd:TIGR02204 539 LKADRIVVMDQGRIVAQGTHAELIAK-GGLYARL 571
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
 325-689 1.39e-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: 320.94  E-value: 1.39e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 325 IDSLLNYETVKYFNNEKYEAERydgflkVYESS---SLKTTSTLAMlNFGQSA----IFSVGLTAIMVLASKGIMSGTMT 397
Cdd:COG4988   201 LDRLRGLTTLKLFGRAKAEAER------IAEASedfRKRTMKVLRV-AFLSSAvlefFASLSIALVAVYIGFRLLGGSLT 273

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 398 VGDLVMVngLLfqLS----LPLNFLGTVYRETRQALIDMNTLFTLLsvDTKIKEKEMAPPLIVTPQEATIRFEDVYFEYL 473
Cdd:COG4988   274 LFAALFV--LL--LApeffLPLRDLGSFYHARANGIAAAEKIFALL--DAPEPAAPAGTAPLPAAGPPSIELEDVSFSYP 347

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 474 EGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGLESLRKAVGVVPQDAVLFHNTI 553
Cdd:COG4988   348 GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTI 427

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 554 FYNLMYGNINATAEDVYRVARLAGIHDAILKMPHKYDTQVGERGLKLSGGEKQRVAIARAILKNPPILLYDEATSSLDSV 633
Cdd:COG4988   428 RENLRLGRPDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAE 507

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2569209806 634 TEENILTSMKEMVKDRTSVFIAHRLSTIVDADEIIVLNQGKVAERGNHQTLLDTPG 689
Cdd:COG4988   508 TEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKNG 563
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
 116-700 1.61e-100

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: 320.90  E-value: 1.61e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 116 FTYVWPKDRPdLRARVVISLSLLAGAKITNVMVPFMFKYAVDslnqmsgHMLNLSDaPNTVVTMAtAVLIGYGVSRtGSA 195
Cdd:TIGR02203   2 FRRLWSYVRP-YKAGLVLAGVAMILVAATESTLAALLKPLLD-------DGFGGRD-RSVLWWVP-LVVIGLAVLR-GIC 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 196 LFneLRNAVFGKVAQSSIRRIAKNVFLHLHNLDLGFHLSRQTGALskaIDRGTRGISFVLSALVFNLGPTLFEMMLVSG- 274
Cdd:TIGR02203  71 SF--VSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTL---LSRITFDSEQVASAATDAFIVLVRETLTVIGl 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 275 ---ILYYKCGGHFALVTLGTLSAYTAfTVAVTQWRTQFRiEMNKADNEAGNAAIDSLLNYETVKYFNNEKYEAERYDGFL 351
Cdd:TIGR02203 146 fivLLYYSWQLTLIVVVMLPVLSILM-RRVSKRLRRISK-EIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVS 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 352 KVYESSSLKTTSTLAMLNFGQSAIFSVGLTAIMVLASKGIMSGTMTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALID 431
Cdd:TIGR02203 224 NRNRRLAMKMTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAA 303

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 432 MNTLFTLL----SVDTKIKEKEMApplivtpqEATIRFEDVYFEYL-EGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIV 506
Cdd:TIGR02203 304 AESLFTLLdsppEKDTGTRAIERA--------RGDVEFRNVTFRYPgRDRPALDSISLVIEPGETVALVGRSGSGKSTLV 375

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 507 RLLFRFYEPQQGNIYIAGQNIRDVGLESLRKAVGVVPQDAVLFHNTIFYNLMYGNI-NATAEDVYRVARLAGIHDAILKM 585
Cdd:TIGR02203 376 NLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTeQADRAEIERALAAAYAQDFVDKL 455

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 586 PHKYDTQVGERGLKLSGGEKQRVAIARAILKNPPILLYDEATSSLDSVTEENILTSMKEMVKDRTSVFIAHRLSTIVDAD 665
Cdd:TIGR02203 456 PLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKAD 535

                         570       580       590
                  ....*....|....*....|....*....|....*
gi 2569209806 666 EIIVLNQGKVAERGNHQTLLDTPGsLYANLWNTQN 700
Cdd:TIGR02203 536 RIVVMDDGRIVERGTHNELLARNG-LYAQLHNMQF 569
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
 461-689 3.77e-100

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


Pssm-ID: 213221 [Multi-domain]  Cd Length: 229  Bit Score: 308.00  E-value: 3.77e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 461 ATIRFEDVYFEYLEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGLESLRKAVG 540
Cdd:cd03254     1 GEIEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 541 VVPQDAVLFHNTIFYNLMYGNINATAEDVYRVARLAGIHDAILKMPHKYDTQVGERGLKLSGGEKQRVAIARAILKNPPI 620
Cdd:cd03254    81 VVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2569209806 621 LLYDEATSSLDSVTEENILTSMKEMVKDRTSVFIAHRLSTIVDADEIIVLNQGKVAERGNHQTLLDTPG 689
Cdd:cd03254   161 LILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
214-693 5.74e-94

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 304.19  E-value: 5.74e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 214 RRIA--KNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGISFV--------LSALV--FNLGPTLFEMMLVSGILyykcg 281
Cdd:PRK13657   87 RRLAvlTEYFERIIQLPLAWHSQRGSGRALHTLLRGTDALFGLwlefmrehLATLValVVLLPLALFMNWRLSLV----- 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 282 ghfaLVTLGTlsAYTAFTVAVTQwRT---QFRIEMNKADNEAgnAAIDSLLNYETVKYFNNEKYEAERYDGFLKVYESSS 358
Cdd:PRK13657  162 ----LVVLGI--VYTLITTLVMR-KTkdgQAAVEEHYHDLFA--HVSDAIGNVSVVQSYNRIEAETQALRDIADNLLAAQ 232

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 359 LKTTSTLAMLNFGQSAIFSVGLTAIMVLASKGIMSGTMTVGDLVMVNG---LLFQ-LSLPLNFLGTVYRETRQalidMNT 434
Cdd:PRK13657  233 MPVLSWWALASVLNRAASTITMLAILVLGAALVQKGQLRVGEVVAFVGfatLLIGrLDQVVAFINQVFMAAPK----LEE 308

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 435 LFTLLSVDTKIKEKEMAPPLivTPQEATIRFEDVYFEYLEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYE 514
Cdd:PRK13657  309 FFEVEDAVPDVRDPPGAIDL--GRVKGAVEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFD 386

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 515 PQQGNIYIAGQNIRDVGLESLRKAVGVVPQDAVLFHNTIFYNLMYGNINATAEDVYRVARLAGIHDAILKMPHKYDTQVG 594
Cdd:PRK13657  387 PQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVG 466

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 595 ERGLKLSGGEKQRVAIARAILKNPPILLYDEATSSLDSVTEENILTSMKEMVKDRTSVFIAHRLSTIVDADEIIVLNQGK 674
Cdd:PRK13657  467 ERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGR 546

                         490
                  ....*....|....*....
gi 2569209806 675 VAERGNHQTLLDTPGSLYA 693
Cdd:PRK13657  547 VVESGSFDELVARGGRFAA 565
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
 250-697 4.20e-89

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: 290.90  E-value: 4.20e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 250 GISFVLSALVFNLGPTLFEMMLVSGILyykcgghfalVTLGTLSAYTAFTVAVTQWRTQFRIemnkadneagnAAIDSLL 329
Cdd:COG4987   145 AAVAFLAFFSPALALVLALGLLLAGLL----------LPLLAARLGRRAGRRLAAARAALRA-----------RLTDLLQ 203

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 330 NYETVKYFNNEKYEAERYDGFlkvyESSSLKTTSTLAMLN-FGQSAI-FSVGLTAIMVL--ASKGIMSGTMTVGDLVMVn 405
Cdd:COG4987   204 GAAELAAYGALDRALARLDAA----EARLAAAQRRLARLSaLAQALLqLAAGLAVVAVLwlAAPLVAAGALSGPLLALL- 278

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 406 gLLFQLSL--PLNFLGTVYRETRQALIDMNTLFTLLSVDTKIKEKEMAPPLivtPQEATIRFEDVYFEYL-EGQKVLNGV 482
Cdd:COG4987   279 -VLAALALfeALAPLPAAAQHLGRVRAAARRLNELLDAPPAVTEPAEPAPA---PGGPSLELEDVSFRYPgAGRPVLDGL 354

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 483 SFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGLESLRKAVGVVPQDAVLFHNTIFYNLMYGNI 562
Cdd:COG4987   355 SLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARP 434

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 563 NATAEDVYRVARLAGIHDAILKMPHKYDTQVGERGLKLSGGEKQRVAIARAILKNPPILLYDEATSSLDSVTEENILTSM 642
Cdd:COG4987   435 DATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADL 514

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2569209806 643 KEMVKDRTSVFIAHRLSTIVDADEIIVLNQGKVAERGNHQTLLDTPGSlYANLWN 697
Cdd:COG4987   515 LEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGR-YRQLYQ 568
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
204-699 1.98e-84

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 278.83  E-value: 1.98e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 204 VFGKVAQSsIRRiakNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGISFVLS-ALV-------FNLGptLFEMMLvsgi 275
Cdd:PRK11176   92 VSGKVVMT-MRR---RLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSgALItvvregaSIIG--LFIMMF---- 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 276 lYYKCGGHFALVTLGTLSAytaftVAVTQWRTQFRI---EMNKADNEAGNAAIDSLLNYETVKYFNNEKYEAERYDGFLK 352
Cdd:PRK11176  162 -YYSWQLSLILIVIAPIVS-----IAIRVVSKRFRNiskNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSN 235

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 353 VYESSSLKTTSTLAMLNFGQSAIFSVGLTAIMVLASKGIMSGTMTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDM 432
Cdd:PRK11176  236 RMRQQGMKMVSASSISDPIIQLIASLALAFVLYAASFPSVMDTLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAAC 315

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 433 NTLFTLLSVDTkikEKEMAPpLIVTPQEATIRFEDVYFEYLEGQK-VLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFR 511
Cdd:PRK11176  316 QTLFAILDLEQ---EKDEGK-RVIERAKGDIEFRNVTFTYPGKEVpALRNINFKIPAGKTVALVGRSGSGKSTIANLLTR 391

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 512 FYEPQQGNIYIAGQNIRDVGLESLRKAVGVVPQDAVLFHNTIFYNLMYGNINA-TAEDVYRVARLAGIHDAILKMPHKYD 590
Cdd:PRK11176  392 FYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAYAMDFINKMDNGLD 471

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 591 TQVGERGLKLSGGEKQRVAIARAILKNPPILLYDEATSSLDSVTEENILTSMKEMVKDRTSVFIAHRLSTIVDADEIIVL 670
Cdd:PRK11176  472 TVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVV 551

                         490       500
                  ....*....|....*....|....*....
gi 2569209806 671 NQGKVAERGNHQTLLDTPGSlYANLWNTQ 699
Cdd:PRK11176  552 EDGEIVERGTHAELLAQNGV-YAQLHKMQ 579
ABC_6TM_ABCB6 cd18581
Six-transmembrane helical domain of the ATP-binding cassette subfamily B member 6, ...
 135-432 8.95e-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: 262.57  E-value: 8.95e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 135 LSLLAGAKITNVMVPFMFKYAVDSLnqmsghmlnLSDAPNTVVTMATAVLIGY-------GVSRTGSALFNELRNAVFGK 207
Cdd:cd18581     2 LLLLAAGRVVNVLVPILYKKIVDSL---------TPDSADSPLAFPWALILLYvflkflqGGGSGSVGLLSNLRSFLWIP 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 208 VAQSSIRRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGISFVLSALVFNLGPTLFEMMLVSGILYYKCGGHFALV 287
Cdd:cd18581    73 VQQFTTREISVKLFAHLHSLSLRWHLSRKTGEVLRVMDRGTSSINSLLSYVLFNIGPTIADIIIAIIYFAIAFNPWFGLI 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 288 TLGTLSAYTAFTVAVTQWRTQFRIEMNKADNEAGNAAIDSLLNYETVKYFNNEKYEAERYDGFLKVYESSSLKTTSTLAM 367
Cdd:cd18581   153 VFVTMALYLILTIIITEWRTKFRREMNKLDNEKRAKAVDSLLNFETVKYYNAERFEVERYRRAIDDYQVAEWKSNASLNL 232

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2569209806 368 LNFGQSAIFSVGLTAIMVLASKGIMSGTMTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDM 432
Cdd:cd18581   233 LNTAQNLIITIGLLAGSLLCAYFVVEGKLTVGDFVLFLTYIIQLYAPLNFFGTYYRMIQQSFIDM 297
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
 463-674 1.97e-80

ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213195 [Multi-domain]  Cd Length: 171  Bit Score: 254.23  E-value: 1.97e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 463 IRFEDVYFEY-LEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGLESLRKAVGV 541
Cdd:cd03228     1 IEFKNVSFSYpGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 542 VPQDAVLFHNTIFYNLmygninataedvyrvarlagihdailkmphkydtqvgerglkLSGGEKQRVAIARAILKNPPIL 621
Cdd:cd03228    81 VPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPIL 118

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2569209806 622 LYDEATSSLDSVTEENILTSMKEMVKDRTSVFIAHRLSTIVDADEIIVLNQGK 674
Cdd:cd03228   119 ILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
 193-693 7.61e-80

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 270.05  E-value: 7.61e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 193 GSALFNELRNAVFgKVAQSSI-RRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGT----RGISFVLSALVFNLGptlf 267
Cdd:TIGR00958 213 ASSVSAGLRGGSF-NYTMARInLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTqtmsRSLSLNVNVLLRNLV---- 287

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 268 eMMLVSGILYYKCGGHFALVTLGTLSAYTAFTVAVTQWRTQFRIEMNKADNEAGNAAIDSLLNYETVKYFNNEKYEAERY 347
Cdd:TIGR00958 288 -MLLGLLGFMLWLSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRF 366

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 348 DGFLKvyESSSLKTTSTLA-MLNFGQSAIFSVGL-TAIMVLASKGIMSGTMTVGDLVMVngLLFQLSL--PLNFLGTVYR 423
Cdd:TIGR00958 367 KEALE--ETLQLNKRKALAyAGYLWTTSVLGMLIqVLVLYYGGQLVLTGKVSSGNLVSF--LLYQEQLgeAVRVLSYVYS 442

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 424 ETRQALIDMNTLFTLLSvdtkiKEKEMAPPLIVTPQ--EATIRFEDVYFEY--LEGQKVLNGVSFEVPAGKKVAIVGGSG 499
Cdd:TIGR00958 443 GMMQAVGASEKVFEYLD-----RKPNIPLTGTLAPLnlEGLIEFQDVSFSYpnRPDVPVLKGLTFTLHPGEVVALVGPSG 517

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 500 SGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGLESLRKAVGVVPQDAVLFHNTIFYNLMYGNINATAEDVYRVARLAGIH 579
Cdd:TIGR00958 518 SGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAH 597

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 580 DAILKMPHKYDTQVGERGLKLSGGEKQRVAIARAILKNPPILLYDEATSSLDSVTEENILTSMKEmvKDRTSVFIAHRLS 659
Cdd:TIGR00958 598 DFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSR--ASRTVLLIAHRLS 675

                         490       500       510
                  ....*....|....*....|....*....|....
gi 2569209806 660 TIVDADEIIVLNQGKVAERGNHQTLLDTPGSLYA 693
Cdd:TIGR00958 676 TVERADQILVLKKGSVVEMGTHKQLMEDQGCYKH 709
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
 463-699 1.53e-79

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: 254.33  E-value: 1.53e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 463 IRFEDVYFEY-LEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGLESLRKAVGV 541
Cdd:cd03252     1 ITFEHVRFRYkPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 542 VPQDAVLFHNTIFYNLMYGNINATAEDVYRVARLAGIHDAILKMPHKYDTQVGERGLKLSGGEKQRVAIARAILKNPPIL 621
Cdd:cd03252    81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2569209806 622 LYDEATSSLDSVTEENILTSMKEMVKDRTSVFIAHRLSTIVDADEIIVLNQGKVAERGNHQTLLDTpGSLYANLWNTQ 699
Cdd:cd03252   161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAE-NGLYAYLYQLQ 237
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
 463-680 1.54e-69

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: 227.38  E-value: 1.54e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 463 IRFEDVYFEYLEGQK-VLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGLESLRKAVGV 541
Cdd:cd03244     3 IEFKNVSLRYRPNLPpVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 542 VPQDAVLFHNTIFYNLMYGNInATAEDVYRVARLAGIHDAILKMPHKYDTQVGERGLKLSGGEKQRVAIARAILKNPPIL 621
Cdd:cd03244    83 IPQDPVLFSGTIRSNLDPFGE-YSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKIL 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2569209806 622 LYDEATSSLDSVTEENILTSMKEMVKDRTSVFIAHRLSTIVDADEIIVLNQGKVAERGN 680
Cdd:cd03244   162 VLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
ABC_6TM_HMT1 cd18583
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents ...
 137-435 8.61e-68

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: 225.10  E-value: 8.61e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 137 LLAGAKITNVMVPFMFKYAVDSLNQMSGHMlnlsdapntvVTMATAVLIGYGVSRtGSALFNELRNAVFGKVAQSSIRRI 216
Cdd:cd18583     4 CLLAERVLNVLVPRQLGIIVDSLSGGSGKS----------PWKEIGLYVLLRFLQ-SGGGLGLLRSWLWIPVEQYSYRAL 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 217 AKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTrGISFVLSALVFNLGPTLFEMMLVSGILYYKCGGHFALVTLGTLSAYT 296
Cdd:cd18583    73 STAAFNHVMNLSMDFHDSKKSGEVLKAIEQGS-SINDLLEQILFQIVPMIIDLVIAIVYLYYLFDPYMGLIVAVVMVLYV 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 297 AFTVAVTQWRTQFRIEMNKADNEAGNAAIDSLLNYETVKYFNNEKYEAERYDGFLKVYESSSLKTTSTLAMLNFGQSAIF 376
Cdd:cd18583   152 WSTIKLTSWRTKLRRDMIDADREERSILTESLLNWETVKYFNREPYEKERYREAVKNYQKAERKYLFSLNLLNAVQSLIL 231

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2569209806 377 SVGLTAIMVLASKGIMSGTMTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDMNTL 435
Cdd:cd18583   232 TLGLLAGCFLAAYQVSQGQATVGDFVTLLTYWAQLSGPLNFFATLYRSIQSDLIDAERL 290
chvA TIGR01192
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ...
 377-714 1.02e-67

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: 234.01  E-value: 1.02e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 377 SVGLTAIMVLASKGIMSGTMTVGDLVMVNG----LLFQLSLPLNFLGTVYrETRQALIDmntLFTLLSVDTKIKEKEMAP 452
Cdd:TIGR01192 251 TISMMCILVIGTVLVIKGELSVGEVIAFIGfanlLIGRLDQMSGFITQIF-EARAKLED---FFDLEDSVFQREEPADAP 326

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 453 PLivTPQEATIRFEDVYFEYLEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGL 532
Cdd:TIGR01192 327 EL--PNVKGAVEFRHITFEFANSSQGVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTR 404

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 533 ESLRKAVGVVPQDAVLFHNTIFYNLMYGNINATAEDVYRVARLAGIHDAILKMPHKYDTQVGERGLKLSGGEKQRVAIAR 612
Cdd:TIGR01192 405 ESLRKSIATVFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIAR 484

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 613 AILKNPPILLYDEATSSLDSVTEENILTSMKEMVKDRTSVFIAHRLSTIVDADEIIVLNQGKVAERGNHQTLLDTPGSLY 692
Cdd:TIGR01192 485 AILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQKDGRFY 564

                         330       340
                  ....*....|....*....|..
gi 2569209806 693 ANLwntQNSRILSNGSKPEPVP 714
Cdd:TIGR01192 565 KLL---RRSGLLTNQPATKPLR 583
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
 173-697 2.42e-67

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: 235.79  E-value: 2.42e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 173 PNTVVTMATAVLIGYGVSRTGSALFNELRNAVFGKVAQSSIRRIAKNVFLHLHNLDLGFHLSRQTGALskaIDRGTRGIS 252
Cdd:TIGR01193 188 PHKMMGTLGIISIGLIIAYIIQQILSYIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGEI---VSRFTDASS 264

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 253 FV--LSALVFNLGPTLFEMMLVSGILYYKCGGHFALVtlgtLSAYTAFTVAVTQWRTQFRiEMNKADNEAG----NAAID 326
Cdd:TIGR01193 265 IIdaLASTILSLFLDMWILVIVGLFLVRQNMLLFLLS----LLSIPVYAVIIILFKRTFN-KLNHDAMQANavlnSSIIE 339

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 327 SLLNYETVKYFNNEKYEAERYDGFLKVYESSSLKTTSTLAmlnfGQSAIFSV-GLTAIMVLASKG---IMSGTMTVGDLV 402
Cdd:TIGR01193 340 DLNGIETIKSLTSEAERYSKIDSEFGDYLNKSFKYQKADQ----GQQAIKAVtKLILNVVILWTGaylVMRGKLTLGQLI 415

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 403 MVNGLLFQLSLPLNFLGTVYRETRQALIDMNTLFTLLSVDTKIKEKEMAPPLIVTpqEATIRFEDVYFEYLEGQKVLNGV 482
Cdd:TIGR01193 416 TFNALLSYFLTPLENIINLQPKLQAARVANNRLNEVYLVDSEFINKKKRTELNNL--NGDIVINDVSYSYGYGSNILSDI 493

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 483 SFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGLESLRKAVGVVPQDAVLFHNTIFYNLMYGNI 562
Cdd:TIGR01193 494 SLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGAK 573

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 563 -NATAEDVYRVARLAGIHDAILKMPHKYDTQVGERGLKLSGGEKQRVAIARAILKNPPILLYDEATSSLDSVTEENILTS 641
Cdd:TIGR01193 574 eNVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNN 653

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2569209806 642 MKEMvKDRTSVFIAHRLSTIVDADEIIVLNQGKVAERGNHQTLLDTPGsLYANLWN 697
Cdd:TIGR01193 654 LLNL-QDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNG-FYASLIH 707
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
 463-675 5.62e-66

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: 217.84  E-value: 5.62e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 463 IRFEDVYFEYLEGQ-KVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGLESLRKAVGV 541
Cdd:cd03245     3 IEFRNVSFSYPNQEiPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGY 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 542 VPQDAVLFHNTIFYNLMYGNINATAEDVYRVARLAGIHDAILKMPHKYDTQVGERGLKLSGGEKQRVAIARAILKNPPIL 621
Cdd:cd03245    83 VPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPIL 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2569209806 622 LYDEATSSLDSVTEENILTSMKEMVKDRTSVFIAHRLSTIVDADEIIVLNQGKV 675
Cdd:cd03245   163 LLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
470-689 3.27e-62

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


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 218.43  E-value: 3.27e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 470 FEYLEGQK-VLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGLESLRKAVGVVPQDAVL 548
Cdd:PRK10789  321 FTYPQTDHpALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFL 400

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 549 FHNTIFYNLMYGNINATAEDVYRVARLAGIHDAILKMPHKYDTQVGERGLKLSGGEKQRVAIARAILKNPPILLYDEATS 628
Cdd:PRK10789  401 FSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALS 480

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2569209806 629 SLDSVTEENILTSMKEMVKDRTSVFIAHRLSTIVDADEIIVLNQGKVAERGNHQTLLDTPG 689
Cdd:PRK10789  481 AVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSG 541
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
 456-675 2.65e-61

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: 205.40  E-value: 2.65e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 456 VTPQ--EATIRFEDVYFEY--LEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVG 531
Cdd:cd03248     3 LAPDhlKGIVKFQNVTFAYptRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 532 LESLRKAVGVVPQDAVLFHNTIFYNLMYGNINATAEDVYRVARLAGIHDAILKMPHKYDTQVGERGLKLSGGEKQRVAIA 611
Cdd:cd03248    83 HKYLHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIA 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2569209806 612 RAILKNPPILLYDEATSSLDSVTEENILTSMKEMVKDRTSVFIAHRLSTIVDADEIIVLNQGKV 675
Cdd:cd03248   163 RALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
 285-670 6.80e-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: 210.99  E-value: 6.80e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 285 ALVTLGTLSAYTAFtVAVTQWRTQFRIEMN-KADNEAGNAAIDSLLNYETVKYFNNEKYEAERydgflkVYESSSL---K 360
Cdd:TIGR02857 147 GLILLLTAPLIPIF-MILIGWAAQAAARKQwAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAA------IRRSSEEyreR 219

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 361 TTSTLAMlNFGQSAIF------SVGLTAIMVlaskGImsgTMTVGDLVMVNGLLFQL-----SLPLNFLGTVYRETRQAL 429
Cdd:TIGR02857 220 TMRVLRI-AFLSSAVLelfatlSVALVAVYI----GF---RLLAGDLDLATGLFVLLlapefYLPLRQLGAQYHARADGV 291

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 430 IDMNTLFTLLSVDTKIkEKEMAPplIVTPQEATIRFEDVYFEYLEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLL 509
Cdd:TIGR02857 292 AAAEALFAVLDAAPRP-LAGKAP--VTAAPASSLEFSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLL 368

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 510 FRFYEPQQGNIYIAGQNIRDVGLESLRKAVGVVPQDAVLFHNTIFYNLMYGNINATAEDVYRVARLAGIHDAILKMPHKY 589
Cdd:TIGR02857 369 LGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGL 448

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 590 DTQVGERGLKLSGGEKQRVAIARAILKNPPILLYDEATSSLDSVTEENILTSMKEMVKDRTSVFIAHRLSTIVDADEIIV 669
Cdd:TIGR02857 449 DTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVV 528


                  .
gi 2569209806 670 L 670
Cdd:TIGR02857 529 L 529
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
 248-693 1.08e-57

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 206.21  E-value: 1.08e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 248 TRGISFVLSALVFNLGPTLFEMMLVSGILYYKCGghfalvtlgtlsayTAFTVAVTQWRTQFRIEMnkadneagnaaIDS 327
Cdd:PRK11160  152 TIGLSFFDLTLALTLGGILLLLLLLLPLLFYRLG--------------KKPGQDLTHLRAQYRVQL-----------TEW 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 328 LLNYETVKYFNNEkyeaERYDGFLKVYESSSLKTTSTLAMLN-FGQSA-IFSVGLTAIMVL--ASKGIMSG--------- 394
Cdd:PRK11160  207 LQGQAELTLFGAE----DRYRQQLEQTEQQWLAAQRRQANLTgLSQALmILANGLTVVLMLwlAAGGVGGNaqpgalial 282

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 395 ----TMTVGDLVMVNGLLFQlslplnFLGTVyretrqalidmntlftlLSVDTKIKEKEMAPPLIVTPQEAT-------I 463
Cdd:PRK11160  283 fvfaALAAFEALMPVAGAFQ------HLGQV-----------------IASARRINEITEQKPEVTFPTTSTaaadqvsL 339

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 464 RFEDVYFEYLEG-QKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGLESLRKAVGVV 542
Cdd:PRK11160  340 TLNNVSFTYPDQpQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVV 419

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 543 PQDAVLFHNTIFYNLMYGNINATAEDVYRVARLAGIhDAILKMPHKYDTQVGERGLKLSGGEKQRVAIARAILKNPPILL 622
Cdd:PRK11160  420 SQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGL-EKLLEDDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLL 498

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2569209806 623 YDEATSSLDSVTEENILTSMKEMVKDRTSVFIAHRLSTIVDADEIIVLNQGKVAERGNHQTLLDTPGSLYA 693
Cdd:PRK11160  499 LDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQ 569
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
 378-658 7.09e-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: 7.09e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 378 VGLTAIMVL--ASKGIMSGTMTVGDLVMVngLLFQLSL--PLNFLGTVYRETRQALIDMNTLFTLLSVDTKIKEKEMAPP 453
Cdd:TIGR02868 248 AGLAVLGALwaGGPAVADGRLAPVTLAVL--VLLPLAAfeAFAALPAAAQQLTRVRAAAERIVEVLDAAGPVAEGSAPAA 325

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 454 LIVTPQEATIRFEDVYFEYLEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGLE 533
Cdd:TIGR02868 326 GAVGLGKPTLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQD 405

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 534 SLRKAVGVVPQDAVLFHNTIFYNLMYGNINATAEDVYRVARLAGIHDAILKMPHKYDTQVGERGLKLSGGEKQRVAIARA 613
Cdd:TIGR02868 406 EVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARA 485

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2569209806 614 ILKNPPILLYDEATSSLDSVTEENILTSMKEMVKDRTSVFIAHRL 658
Cdd:TIGR02868 486 LLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
459-692 3.03e-54

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


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 196.86  E-value: 3.03e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 459 QEATIRFEDVYFEYLEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGLESLRKA 538
Cdd:PRK10790  337 QSGRIDIDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQG 416

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 539 VGVVPQDAVLFHNTIFYNLMYGNiNATAEDVYRVARLAGIHDAILKMPHKYDTQVGERGLKLSGGEKQRVAIARAILKNP 618
Cdd:PRK10790  417 VAMVQQDPVVLADTFLANVTLGR-DISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTP 495

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2569209806 619 PILLYDEATSSLDSVTEENILTSMKEMVKDRTSVFIAHRLSTIVDADEIIVLNQGKVAERGNHQTLLDTPGSLY 692
Cdd:PRK10790  496 QILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYW 569
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
 458-679 4.50e-54

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: 185.31  E-value: 4.50e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 458 PQEATIRFEDVYFEYL-EGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGLESLR 536
Cdd:cd03369     2 PEHGEIEVENLSVRYApDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 537 KAVGVVPQDAVLFHNTIFYNL----MYgninaTAEDVYRVARlagihdailkmphkydtqVGERGLKLSGGEKQRVAIAR 612
Cdd:cd03369    82 SSLTIIPQDPTLFSGTIRSNLdpfdEY-----SDEEIYGALR------------------VSEGGLNLSQGQRQLLCLAR 138

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2569209806 613 AILKNPPILLYDEATSSLDSVTEENILTSMKEMVKDRTSVFIAHRLSTIVDADEIIVLNQGKVAERG 679
Cdd:cd03369   139 ALLKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYD 205
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
 409-695 6.30e-54

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 195.83  E-value: 6.30e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 409 FQlslPLNFLGTVYRETRQALIDMNTLFTLLSVDTKIKEKEMAPPLIVTPqeATIRFEDVYFEYLEGQKVLNGVSFEVPA 488
Cdd:PRK11174  301 YQ---PLRDLGTFYHAKAQAVGAAESLVTFLETPLAHPQQGEKELASNDP--VTIEAEDLEILSPDGKTLAGPLNFTLPA 375

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 489 GKKVAIVGGSGSGKSTIVRLLFRFYePQQGNIYIAGQNIRDVGLESLRKAVGVVPQDAVLFHNTIFYNLMYGNINATAED 568
Cdd:PRK11174  376 GQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQ 454

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 569 VYRVARLAGIHDAILKMPHKYDTQVGERGLKLSGGEKQRVAIARAILKNPPILLYDEATSSLDSVTEENILTSMKEMVKD 648
Cdd:PRK11174  455 LQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRR 534

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 2569209806 649 RTSVFIAHRLSTIVDADEIIVLNQGKVAERGNHQTLLDTPGsLYANL 695
Cdd:PRK11174  535 QTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGG-LFATL 580
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
 282-676 1.32e-53

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: 194.58  E-value: 1.32e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 282 GHFALVTLGTLsayTAFTVAvTQWRTQFRI-EMNKADNEAGNAAIDSLLNYETVkyfnnekyEA------------ERYD 348
Cdd:COG4618   158 GLLALVGALVL---VALALL-NERLTRKPLkEANEAAIRANAFAEAALRNAEVI--------EAmgmlpalrrrwqRANA 225

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 349 GFLKVYESSSLKTTSTLAML----NFGQSAIFSVGltAIMVLasKGIMS-GTMTVGDLVMVNGLLfqlslPL-NFLGT-- 420
Cdd:COG4618   226 RALALQARASDRAGGFSALSkflrLLLQSAVLGLG--AYLVI--QGEITpGAMIAASILMGRALA-----PIeQAIGGwk 296

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 421 VYRETRQALIDMNTLFTLLSVDtkikEKEMAPPlivTPQeATIRFEDVYFEYLEGQK-VLNGVSFEVPAGKKVAIVGGSG 499
Cdd:COG4618   297 QFVSARQAYRRLNELLAAVPAE----PERMPLP---RPK-GRLSVENLTVVPPGSKRpILRGVSFSLEPGEVLGVIGPSG 368

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 500 SGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGLESLRKAVGVVPQDAVLFHNTIFynlmyGNI----NATAEDVYRVARL 575
Cdd:COG4618   369 SGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIA-----ENIarfgDADPEKVVAAAKL 443

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 576 AGIHDAILKMPHKYDTQVGERGLKLSGGEKQRVAIARAILKNPPILLYDEATSSLDSVTEENILTSMKEMvKDR--TSVF 653
Cdd:COG4618   444 AGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRAL-KARgaTVVV 522

                         410       420
                  ....*....|....*....|...
gi 2569209806 654 IAHRLSTIVDADEIIVLNQGKVA 676
Cdd:COG4618   523 ITHRPSLLAAVDKLLVLRDGRVQ 545
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
 463-685 1.87e-49

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


Pssm-ID: 440739 [Multi-domain]  Cd Length: 230  Bit Score: 173.29  E-value: 1.87e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 463 IRFEDVYFEYLEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGLESLRKAVGVV 542
Cdd:COG1122     1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 543 PQDAV--LFHNTIFYNLMYG--NINATAED----VYRVARLAGIHDAILKMPHkydtqvgerglKLSGGEKQRVAIARAI 614
Cdd:COG1122    81 FQNPDdqLFAPTVEEDVAFGpeNLGLPREEirerVEEALELVGLEHLADRPPH-----------ELSGGQKQRVAIAGVL 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2569209806 615 LKNPPILLYDEATSSLDSVTEENILTSMKEMVKDRTSVFIA-HRLSTIVD-ADEIIVLNQGKVAERGNHQTLL 685
Cdd:COG1122   150 AMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVtHDLDLVAElADRVIVLDDGRIVADGTPREVF 222
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
 463-679 2.36e-48

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: 168.26  E-value: 2.36e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 463 IRFEDVYFEYLE-GQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGlESLRKAVGV 541
Cdd:cd03247     1 LSINNVSFSYPEqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 542 VPQDAVLFHNTIFYNLmygninataedvyrvarlagihdailkmphkydtqvgerGLKLSGGEKQRVAIARAILKNPPIL 621
Cdd:cd03247    80 LNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPIV 120

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2569209806 622 LYDEATSSLDSVTEENILTSMKEMVKDRTSVFIAHRLSTIVDADEIIVLNQGKVAERG 679
Cdd:cd03247   121 LLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
PLN03232 PLN03232
ABC transporter C family member; Provisional
 362-706 1.57e-47

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 182.48  E-value: 1.57e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806  362 TSTLAMLNFGQSAiFSVGLTAIMVLaskgIMSGTMTVGDLVmvNGLLFQLSLPLNFLGTVYRetrqalidMNTLFTLLSV 441
Cdd:PLN03232  1151 TATFAVLRNGNAE-NQAGFASTMGL----LLSYTLNITTLL--SGVLRQASKAENSLNSVER--------VGNYIDLPSE 1215

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806  442 DTKIKEKEMapPLIVTPQEATIRFEDVYFEYLEG-QKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNI 520
Cdd:PLN03232  1216 ATAIIENNR--PVSGWPSRGSIKFEDVHLRYRPGlPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRI 1293

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806  521 YIAGQNIRDVGLESLRKAVGVVPQDAVLFHNTIFYNLMYGNINATAeDVYRVARLAGIHDAILKMPHKYDTQVGERGLKL 600
Cdd:PLN03232  1294 MIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDA-DLWEALERAHIKDVIDRNPFGLDAEVSEGGENF 1372

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806  601 SGGEKQRVAIARAILKNPPILLYDEATSSLDSVTEENILTSMKEMVKDRTSVFIAHRLSTIVDADEIIVLNQGKVAERGN 680
Cdd:PLN03232  1373 SVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDS 1452

                          330       340
                   ....*....|....*....|....*....
gi 2569209806  681 HQTLLDTPGSLYANLWNT---QNSRILSN 706
Cdd:PLN03232  1453 PQELLSRDTSAFFRMVHStgpANAQYLSN 1481
PLN03130 PLN03130
ABC transporter C family member; Provisional
 406-726 1.98e-47

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 182.25  E-value: 1.98e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806  406 GLLfqLSLPLNFLGTVYRETRQALIDMNTLFTLLSVDTKIKEKEMAPPLIVT-------PQEATIRFEDVYFEYL-EGQK 477
Cdd:PLN03130  1176 GLL--LSYALNITSLLTAVLRLASLAENSLNAVERVGTYIDLPSEAPLVIENnrpppgwPSSGSIKFEDVVLRYRpELPP 1253

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806  478 VLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGLESLRKAVGVVPQDAVLFHNTIFYNL 557
Cdd:PLN03130  1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNL 1333

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806  558 MYGNINATAeDVYRVARLAGIHDAILKMPHKYDTQVGERGLKLSGGEKQRVAIARAILKNPPILLYDEATSSLDSVTEEN 637
Cdd:PLN03130  1334 DPFNEHNDA-DLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDAL 1412

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806  638 ILTSMKEMVKDRTSVFIAHRLSTIVDADEIIVLNQGKVAERGNHQTLLDTPGSLYANL------WNTQNSRILSNGSKPE 711
Cdd:PLN03130  1413 IQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFSKMvqstgaANAQYLRSLVFGGDED 1492

                          330
                   ....*....|....*
gi 2569209806  712 PVPERVSQKEEERKK 726
Cdd:PLN03130  1493 RLAREESKALDGQRK 1507
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
 458-688 9.74e-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: 166.31  E-value: 9.74e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 458 PQEATIRFEDVYFEYlEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNI---RDVGLES 534
Cdd:COG1127     1 MSEPMIEVRNLTKSF-GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDItglSEKELYE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 535 LRKAVGVVPQDAVLFHN-TIFYNLMYG---NINATAEDVYRVAR----LAGIHDAILKMPhkydtqvGErglkLSGGEKQ 606
Cdd:COG1127    80 LRRRIGMLFQGGALFDSlTVFENVAFPlreHTDLSEAEIRELVLekleLVGLPGAADKMP-------SE----LSGGMRK 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 607 RVAIARAILKNPPILLYDEATSSLDSVTEENILTSMKEMVKDR--TSVFIAHRLSTIVD-ADEIIVLNQGKVAERGNHQT 683
Cdd:COG1127   149 RVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELglTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEE 228


                  ....*
gi 2569209806 684 LLDTP 688
Cdd:COG1127   229 LLASD 233
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
 463-679 2.05e-46

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: 164.98  E-value: 2.05e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 463 IRFEDVYFEYlEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVG---LESLRKAV 539
Cdd:cd03261     1 IELRGLTKSF-GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSeaeLYRLRRRM 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 540 GVVPQDAVLF-HNTIFYNLMYG---NINATAEDVYRVARL----AGIHDAILKMPHkydtqvgerglKLSGGEKQRVAIA 611
Cdd:cd03261    80 GMLFQSGALFdSLTVFENVAFPlreHTRLSEEEIREIVLEkleaVGLRGAEDLYPA-----------ELSGGMKKRVALA 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2569209806 612 RAILKNPPILLYDEATSSLDSVTEENILTSMKEM--VKDRTSVFIAHRLSTIVD-ADEIIVLNQGKVAERG 679
Cdd:cd03261   149 RALALDPELLLYDEPTAGLDPIASGVIDDLIRSLkkELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEG 219
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
463-677 4.16e-46

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 163.68  E-value: 4.16e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 463 IRFEDVYFEYLEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDV---GLESLRKAV 539
Cdd:COG2884     2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLkrrEIPYLRRRI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 540 GVVPQDA-VLFHNTIFYNLMYG------NINATAEDVYRVARLAGIHDAILKMPHkydtqvgerglKLSGGEKQRVAIAR 612
Cdd:COG2884    82 GVVFQDFrLLPDRTVYENVALPlrvtgkSRKEIRRRVREVLDLVGLSDKAKALPH-----------ELSGGEQQRVAIAR 150

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2569209806 613 AILKNPPILLYDEATSSLDSVTEENILTSMKEMVKDRTSVFIA-HRLStIVDA--DEIIVLNQGKVAE 677
Cdd:COG2884   151 ALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIAtHDLE-LVDRmpKRVLELEDGRLVR 217
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
 463-675 2.31e-45

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: 160.07  E-value: 2.31e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 463 IRFEDVYFEYLEGQK-VLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGLESLRKAVGV 541
Cdd:cd03246     1 LEVENVSFRYPGAEPpVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 542 VPQDAVLFHNTIfynlmygninatAEDVyrvarlagihdailkmphkydtqvgerglkLSGGEKQRVAIARAILKNPPIL 621
Cdd:cd03246    81 LPQDDELFSGSI------------AENI------------------------------LSGGQRQRLGLARALYGNPRIL 118

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2569209806 622 LYDEATSSLDSVTEENILTSMKEM-VKDRTSVFIAHRLSTIVDADEIIVLNQGKV 675
Cdd:cd03246   119 VLDEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
463-675 8.90e-45

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 159.60  E-value: 8.90e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 463 IRFEDVYFEYlEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGLESLRKAVGVV 542
Cdd:COG4619     1 LELEGLSFRV-GGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 543 PQDAVLFHNTIFYNL----MYGNINATAEDVYRVARLAGIHDAILkmphkyDTQVGErglkLSGGEKQRVAIARAILKNP 618
Cdd:COG4619    80 PQEPALWGGTVRDNLpfpfQLRERKFDRERALELLERLGLPPDIL------DKPVER----LSGGERQRLALIRALLLQP 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2569209806 619 PILLYDEATSSLDSVTEENILTSMKEMV--KDRTSVFIAH------RLstivdADEIIVLNQGKV 675
Cdd:COG4619   150 DVLLLDEPTSALDPENTRRVEELLREYLaeEGRAVLWVSHdpeqieRV-----ADRVLTLEAGRL 209
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
 451-693 1.07e-44

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


Pssm-ID: 440740 [Multi-domain]  Cd Length: 514  Bit Score: 168.16  E-value: 1.07e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 451 APPLIVTPQEATIRFEDVYFEYL----EGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQN 526
Cdd:COG1123   249 RAAPAAAAAEPLLEVRNLSKRYPvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKD 328

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 527 IRDVG---LESLRKAVGVVPQD--AVLF-HNTIFYNLMYGNIN-------ATAEDVYRVARLAGIHDAIL-KMPHkydtq 592
Cdd:COG1123   329 LTKLSrrsLRELRRRVQMVFQDpySSLNpRMTVGDIIAEPLRLhgllsraERRERVAELLERVGLPPDLAdRYPH----- 403

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 593 vgerglKLSGGEKQRVAIARAILKNPPILLYDEATSSLDSVTEENILTSMKEMVKDR--TSVFIAHRLSTIVD-ADEIIV 669
Cdd:COG1123   404 ------ELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELglTYLFISHDLAVVRYiADRVAV 477

                         250       260
                  ....*....|....*....|....
gi 2569209806 670 LNQGKVAERGNHQTLLDTPGSLYA 693
Cdd:COG1123   478 MYDGRIVEDGPTEEVFANPQHPYT 501
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
 464-674 1.29e-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: 159.17  E-value: 1.29e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 464 RFEDVYFEYLEG-QKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGLESLRKAVGVV 542
Cdd:cd03225     1 ELKNLSFSYPDGaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 543 PQDA--VLFHNTIFYNLMYG--NINATAEDVYRVArlagihDAILKMphkydtqVGERGLK------LSGGEKQRVAIAR 612
Cdd:cd03225    81 FQNPddQFFGPTVEEEVAFGleNLGLPEEEIEERV------EEALEL-------VGLEGLRdrspftLSGGQKQRVAIAG 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2569209806 613 AILKNPPILLYDEATSSLDSVTEENILTSMKEMVKDRTSVFIA-HRLSTIVD-ADEIIVLNQGK 674
Cdd:cd03225   148 VLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVtHDLDLLLElADRVIVLEDGK 211
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
 463-692 2.26e-44

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 172.91  E-value: 2.26e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806  463 IRFEDVYFEYLEGQKV--LNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFY---------------------EPQQGN 519
Cdd:PTZ00265  1166 IEIMDVNFRYISRPNVpiYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYdlkndhhivfknehtndmtneQDYQGD 1245

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806  520 ---------------------------------IYIAGQNIRDVGLESLRKAVGVVPQDAVLFHNTIFYNLMYGNINATA 566
Cdd:PTZ00265  1246 eeqnvgmknvnefsltkeggsgedstvfknsgkILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATR 1325

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806  567 EDVYRVARLAGIHDAILKMPHKYDTQVGERGLKLSGGEKQRVAIARAILKNPPILLYDEATSSLDSVTE---ENILTSMK 643
Cdd:PTZ00265  1326 EDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEkliEKTIVDIK 1405

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2569209806  644 EMVkDRTSVFIAHRLSTIVDADEIIVLNQGK-----VAERGNHQTLLDTPGSLY 692
Cdd:PTZ00265  1406 DKA-DKTIITIAHRIASIKRSDKIVVFNNPDrtgsfVQAHGTHEELLSVQDGVY 1458
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
 463-679 4.99e-44

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: 158.11  E-value: 4.99e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 463 IRFEDVYFEYLEGQkVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYE-----PQQGNIYIAGQNIR--DVGLESL 535
Cdd:cd03260     1 IELRDLNVYYGDKH-ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYdlDVDVLEL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 536 RKAVGVVPQDAVLFHNTIFYNLMYG-------NINATAEDVYRVARLAGIHDAILKMPHkydtqvgerGLKLSGGEKQRV 608
Cdd:cd03260    80 RRRVGMVFQKPNPFPGSIYDNVAYGlrlhgikLKEELDERVEEALRKAALWDEVKDRLH---------ALGLSGGQQQRL 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2569209806 609 AIARAILKNPPILLYDEATSSLDSVTEENILTSMKEMVKDRTSVFIAH------RLstivdADEIIVLNQGKVAERG 679
Cdd:cd03260   151 CLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHnmqqaaRV-----ADRTAFLLNGRLVEFG 222
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
 463-679 5.41e-44

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: 158.05  E-value: 5.41e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 463 IRFEDVYFEYLEGQ---KVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNI---RDVGLESLR 536
Cdd:cd03257     2 LEVKNLSVSFPTGGgsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLlklSRRLRKIRR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 537 KAVGVVPQDAVLFHN---TIFYNLM------YGNINATAEDVYRVARLAGIHDAiLKMPHKYDTQvgerglkLSGGEKQR 607
Cdd:cd03257    82 KEIQMVFQDPMSSLNprmTIGEQIAeplrihGKLSKKEARKEAVLLLLVGVGLP-EEVLNRYPHE-------LSGGQRQR 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2569209806 608 VAIARAILKNPPILLYDEATSSLDSVTEENILTSMKEMVKDR--TSVFIAHRLSTIVD-ADEIIVLNQGKVAERG 679
Cdd:cd03257   154 VAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELglTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 479-628 1.02e-43

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: 154.34  E-value: 1.02e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 479 LNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGLESLRKAVGVVPQDAVLF-HNTIFYNL 557
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2569209806 558 MYGninATAEDVYRVARLAGIHDAI--LKMPHKYDTQVGERGLKLSGGEKQRVAIARAILKNPPILLYDEATS 628
Cdd:pfam00005  81 RLG---LLLKGLSKREKDARAEEALekLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
 474-693 2.00e-42

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: 154.58  E-value: 2.00e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 474 EGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGLESLRKAVGVVPQD--AVL--F 549
Cdd:COG1124    16 RRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVFQDpyASLhpR 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 550 HN---TIFYNLMYGNINATAEDVYRVARLAGIHDAIL-KMPHKydtqvgerglkLSGGEKQRVAIARAILKNPPILLYDE 625
Cdd:COG1124    96 HTvdrILAEPLRIHGLPDREERIAELLEQVGLPPSFLdRYPHQ-----------LSGGQRQRVAIARALILEPELLLLDE 164

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2569209806 626 ATSSLDSVTEENILTSMKEMVKDR--TSVFIAHRLStIVD--ADEIIVLNQGKVAERGNHQTLLDTPGSLYA 693
Cdd:COG1124   165 PTSALDVSVQAEILNLLKDLREERglTYLFVSHDLA-VVAhlCDRVAVMQNGRIVEELTVADLLAGPKHPYT 235
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
 448-693 2.09e-42

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: 166.66  E-value: 2.09e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806  448 KEMAPPLiVTPQEATIRFEDVYFEYLEGQK-VLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQN 526
Cdd:TIGR00957 1271 QETAPPS-GWPPRGRVEFRNYCLRYREDLDlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLN 1349

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806  527 IRDVGLESLRKAVGVVPQDAVLFHNTIFYNL-MYGNInaTAEDVYRVARLAGIHDAILKMPHKYDTQVGERGLKLSGGEK 605
Cdd:TIGR00957 1350 IAKIGLHDLRFKITIIPQDPVLFSGSLRMNLdPFSQY--SDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQR 1427

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806  606 QRVAIARAILKNPPILLYDEATSSLDSVTEENILTSMKEMVKDRTSVFIAHRLSTIVDADEIIVLNQGKVAERGNHQTLL 685
Cdd:TIGR00957 1428 QLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLL 1507


                   ....*...
gi 2569209806  686 DTPGSLYA 693
Cdd:TIGR00957 1508 QQRGIFYS 1515
ECF_ATPase_1 TIGR04520
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
 463-679 2.28e-42

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: 154.90  E-value: 2.28e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 463 IRFEDVYFEYLEGQK-VLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVG-LESLRKAVG 540
Cdd:TIGR04520   1 IEVENVSFSYPESEKpALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEEnLWEIRKKVG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 541 VVPQ--DavlfhNTIfynlmygnINATAED-------------------VYRVARLAGIHDAILKMPHkydtqvgerglK 599
Cdd:TIGR04520  81 MVFQnpD-----NQF--------VGATVEDdvafglenlgvpreemrkrVDEALKLVGMEDFRDREPH-----------L 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 600 LSGGEKQRVAIARAILKNPPILLYDEATSSLDSVTEENILTSMKEMVKDR--TSVFIAHRLSTIVDADEIIVLNQGKVAE 677
Cdd:TIGR04520 137 LSGGQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEgiTVISITHDMEEAVLADRVIVMNKGKIVA 216


                  ..
gi 2569209806 678 RG 679
Cdd:TIGR04520 217 EG 218
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
463-686 1.31e-41

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 151.75  E-value: 1.31e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 463 IRFEDVYFEYlEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGLEsLRKAVGVV 542
Cdd:COG1131     1 IEVRGLTKRY-GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAE-VRRRIGYV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 543 PQDAVLFHN-TIFYNL-----MYGNINATAEDvyRVARLAgihdAILKMPHKYDTQVGerglKLSGGEKQRVAIARAILK 616
Cdd:COG1131    79 PQEPALYPDlTVRENLrffarLYGLPRKEARE--RIDELL----ELFGLTDAADRKVG----TLSGGMKQRLGLALALLH 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2569209806 617 NPPILLYDEATSSLDSVTEENILTSMKEMVKDRTSVFIA-HRLSTIVD-ADEIIVLNQGKVAERGNHQTLLD 686
Cdd:COG1131   149 DPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLStHYLEEAERlCDRVAIIDKGRIVADGTPDELKA 220
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
 463-674 1.74e-41

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: 149.26  E-value: 1.74e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 463 IRFEDVYFEYlEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGLES--LRKAVG 540
Cdd:cd03229     1 LELKNVSKRY-GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRRIG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 541 VVPQDAVLF-HNTIFYNLMYGninataedvyrvarlagihdailkmphkydtqvgerglkLSGGEKQRVAIARAILKNPP 619
Cdd:cd03229    80 MVFQDFALFpHLTVLENIALG---------------------------------------LSGGQQQRVALARALAMDPD 120

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2569209806 620 ILLYDEATSSLDSVTEENILTSMKEMVKD--RTSVFIAHRLSTIVD-ADEIIVLNQGK 674
Cdd:cd03229   121 VLLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARlADRVVVLRDGK 178
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
 460-679 5.45e-41

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 151.30  E-value: 5.45e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 460 EATIRFEDVYFEYLEGQK-VLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGLESLRKA 538
Cdd:PRK13632    5 SVMIKVENVSFSYPNSENnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKK 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 539 VGVvpqdavlfhntIFYNLMYGNINATAED-------------------VYRVARLAGIHDAILKMPHkydtqvgerglK 599
Cdd:PRK13632   85 IGI-----------IFQNPDNQFIGATVEDdiafglenkkvppkkmkdiIDDLAKKVGMEDYLDKEPQ-----------N 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 600 LSGGEKQRVAIARAILKNPPILLYDEATSSLDSVTEENILTSMKEM--VKDRTSVFIAHRLSTIVDADEIIVLNQGKVAE 677
Cdd:PRK13632  143 LSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLrkTRKKTLISITHDMDEAILADKVIVFSEGKLIA 222


                  ..
gi 2569209806 678 RG 679
Cdd:PRK13632  223 QG 224
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
 464-674 9.45e-41

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: 146.62  E-value: 9.45e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 464 RFEDVYFEYlEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGLESLRKAVGVVP 543
Cdd:cd00267     1 EIENLSFRY-GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 544 QdavlfhntifynlmygninataedvyrvarlagihdailkmphkydtqvgerglkLSGGEKQRVAIARAILKNPPILLY 623
Cdd:cd00267    80 Q-------------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2569209806 624 DEATSSLDSVTEENILTSMKEMVKD-RTSVFIAHRLSTIVDA-DEIIVLNQGK 674
Cdd:cd00267   105 DEPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAELAaDRVIVLKDGK 157
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
460-677 1.24e-40

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 148.65  E-value: 1.24e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 460 EATIRFEDVYFEYLEGQ---KVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNI---RDVGLE 533
Cdd:COG1136     2 SPLLELRNLTKSYGTGEgevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDIsslSERELA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 534 SLR-KAVGVVPQdavlFHN-----TIFYN----LMYGNINAtAEDVYRVARLA---GIHDAILKMPHKydtqvgerglkL 600
Cdd:COG1136    82 RLRrRHIGFVFQ----FFNllpelTALENvalpLLLAGVSR-KERRERARELLervGLGDRLDHRPSQ-----------L 145

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2569209806 601 SGGEKQRVAIARAILKNPPILLYDEATSSLDSVTEENILTSMKEMVKD--RTSVFIAHRLSTIVDADEIIVLNQGKVAE 677
Cdd:COG1136   146 SGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRElgTTIVMVTHDPELAARADRVIRLRDGRIVS 224
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
 463-679 2.88e-40

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: 147.28  E-value: 2.88e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 463 IRFEDVYFEYlEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGLEslRKAVGVV 542
Cdd:cd03259     1 LELKGLSKTY-GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 543 PQDAVLF-HNTIFYNLMYG-NINATAED-----VYRVARLAGIHDAILKMPHkydtqvgerglKLSGGEKQRVAIARAIL 615
Cdd:cd03259    78 FQDYALFpHLTVAENIAFGlKLRGVPKAeirarVRELLELVGLEGLLNRYPH-----------ELSGGQQQRVALARALA 146

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2569209806 616 KNPPILLYDEATSSLDSVTEENILTSMKEMVKDR--TSVFIAHRLSTIVD-ADEIIVLNQGKVAERG 679
Cdd:cd03259   147 REPSLLLLDEPLSALDAKLREELREELKELQRELgiTTIYVTHDQEEALAlADRIAVMNEGRIVQVG 213
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
 424-684 3.92e-40

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 159.81  E-value: 3.92e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806  424 ETRQALIDMNTLFTLLSVDTKIKEKEMAPPLivtPQEATIRFEDVYFEY--LEGQKVLNGVSFEVPAGKKVAIVGGSGSG 501
Cdd:PTZ00265   347 EYMKSLEATNSLYEIINRKPLVENNDDGKKL---KDIKKIQFKNVRFHYdtRKDVEIYKDLNFTLTEGKTYAFVGESGCG 423

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806  502 KSTIVRLLFRFYEPQQGNIYIA-GQNIRDVGLESLRKAVGVVPQDAVLFHNTIFYNLMYG----------------NINA 564
Cdd:PTZ00265   424 KSTILKLIERLYDPTEGDIIINdSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSlyslkdlealsnyyneDGND 503

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806  565 TAE-----------------------------------------DVYRVARLAGIHDAILKMPHKYDTQVGERGLKLSGG 603
Cdd:PTZ00265   504 SQEnknkrnscrakcagdlndmsnttdsneliemrknyqtikdsEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGG 583

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806  604 EKQRVAIARAILKNPPILLYDEATSSLDSVTEENILTSMKEMV--KDRTSVFIAHRLSTIVDADEIIVLNQgkvAERGNH 681
Cdd:PTZ00265   584 QKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIIIAHRLSTIRYANTIFVLSN---RERGST 660


                   ...
gi 2569209806  682 QTL 684
Cdd:PTZ00265   661 VDV 663
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
 463-690 1.91e-39

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


Pssm-ID: 213262 [Multi-domain]  Cd Length: 242  Bit Score: 145.91  E-value: 1.91e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 463 IRFEDVYFEYLEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGLESLRKAVGVV 542
Cdd:cd03295     1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 543 PQDAVLF-HNTIFYNL-----MYGNINATAED-VYRVARLAGIHDAILKmpHKYDTQvgerglkLSGGEKQRVAIARAIL 615
Cdd:cd03295    81 IQQIGLFpHMTVEENIalvpkLLKWPKEKIRErADELLALVGLDPAEFA--DRYPHE-------LSGGQQQRVGVARALA 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2569209806 616 KNPPILLYDEATSSLDSVTEENILTSMKEMVKD--RTSVFIAHRL-STIVDADEIIVLNQGKVAERGNHQTLLDTPGS 690
Cdd:cd03295   152 ADPPLLLMDEPFGALDPITRDQLQEEFKRLQQElgKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILRSPAN 229
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
 463-689 2.69e-39

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: 145.03  E-value: 2.69e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 463 IRFEDVYFEYLEGQK---VLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGLESLRKA- 538
Cdd:cd03258     2 IELKNVSKVFGDTGGkvtALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKAr 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 539 --VGVVPQDAVLFHN-TIFYNLMY---------GNINATAEDVYRVARLAGIHDAilkmphkYDTQvgerglkLSGGEKQ 606
Cdd:cd03258    82 rrIGMIFQHFNLLSSrTVFENVALpleiagvpkAEIEERVLELLELVGLEDKADA-------YPAQ-------LSGGQKQ 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 607 RVAIARAILKNPPILLYDEATSSLDSVTEENILTSMKEMVKDR--TSVFIAHRLSTIVD-ADEIIVLNQGKVAERGNHQT 683
Cdd:cd03258   148 RVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELglTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEE 227


                  ....*.
gi 2569209806 684 LLDTPG 689
Cdd:cd03258   228 VFANPQ 233
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
 463-693 3.65e-39

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


Pssm-ID: 440740 [Multi-domain]  Cd Length: 514  Bit Score: 151.98  E-value: 3.65e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 463 IRFEDVYFEYLEGQK-VLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQ---QGNIYIAGQNIRDVGLESLRKA 538
Cdd:COG1123     5 LEVRDLSVRYPGGDVpAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 539 VGVVPQD--AVLFHNTIFYNLMYGNINATA------EDVYRVARLAGIHDAILKMPHKydtqvgerglkLSGGEKQRVAI 610
Cdd:COG1123    85 IGMVFQDpmTQLNPVTVGDQIAEALENLGLsraearARVLELLEAVGLERRLDRYPHQ-----------LSGGQRQRVAI 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 611 ARAILKNPPILLYDEATSSLDSVTEENILTSMKEMVKDR--TSVFIAHRLSTIVD-ADEIIVLNQGKVAERGNHQTLLDT 687
Cdd:COG1123   154 AMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILAA 233


                  ....*.
gi 2569209806 688 PGSLYA 693
Cdd:COG1123   234 PQALAA 239
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
 463-675 3.66e-39

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


Pssm-ID: 213222 [Multi-domain]  Cd Length: 218  Bit Score: 144.17  E-value: 3.66e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 463 IRFEDVYFEYLEG---QKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIR---DVGLESLR 536
Cdd:cd03255     1 IELKNLSKTYGGGgekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISklsEKELAAFR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 537 -KAVGVVPQdavlFHN-----TIFYNLMY-----GNINATAEDVYR-VARLAGIHDAILKMPHKydtqvgerglkLSGGE 604
Cdd:cd03255    81 rRHIGFVFQ----SFNllpdlTALENVELplllaGVPKKERRERAEeLLERVGLGDRLNHYPSE-----------LSGGQ 145

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2569209806 605 KQRVAIARAILKNPPILLYDEATSSLDSVTEENILTSMKEMVKDR--TSVFIAHRLSTIVDADEIIVLNQGKV 675
Cdd:cd03255   146 QQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAgtTIVVVTHDPELAEYADRIIELRDGKI 218
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
 458-677 1.19e-38

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 143.69  E-value: 1.19e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 458 PQEATIRFEDVYFEYlEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVgleslRK 537
Cdd:COG1121     2 MMMPAIELENLTVSY-GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-----RR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 538 AVGVVPQdavlfhntifynlmYGNIN----ATAEDV--------------YRVARLAGIHDAI--LKMPHKYDTQVGErg 597
Cdd:COG1121    76 RIGYVPQ--------------RAEVDwdfpITVRDVvlmgrygrrglfrrPSRADREAVDEALerVGLEDLADRPIGE-- 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 598 lkLSGGEKQRVAIARAILKNPPILLYDEATSSLDSVTEENILTSMKEMVK-DRTSVFIAHRLSTIVD-ADEIIVLNQGKV 675
Cdd:COG1121   140 --LSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRReGKTILVVTHDLGAVREyFDRVLLLNRGLV 217


                  ..
gi 2569209806 676 AE 677
Cdd:COG1121   218 AH 219
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
 463-688 2.71e-38

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


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 142.44  E-value: 2.71e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 463 IRFEDVYFEYlEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNI--RDVGLESLRKAVG 540
Cdd:COG1126     2 IEIENLHKSF-GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKLRRKVG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 541 VVPQDAVLF-HNTIFYNLMYGNI---NATAEDVYRVAR--LA--GIHDAILKMPHKydtqvgerglkLSGGEKQRVAIAR 612
Cdd:COG1126    81 MVFQQFNLFpHLTVLENVTLAPIkvkKMSKAEAEERAMelLErvGLADKADAYPAQ-----------LSGGQQQRVAIAR 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 613 AILKNPPILLYDEATSSLD--SVTEenILTSMKEMVKD-RTSVFIAHRLSTIVD-ADEIIVLNQGKVAERGNHQTLLDTP 688
Cdd:COG1126   150 ALAMEPKVMLFDEPTSALDpeLVGE--VLDVMRDLAKEgMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGPPEEFFENP 227
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
 463-675 3.48e-37

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: 137.14  E-value: 3.48e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 463 IRFEDVYFEYlEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGlESLRKAVGVV 542
Cdd:cd03230     1 IEVRNLSKRY-GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEP-EEVKRRIGYL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 543 PQDAVLFHNtifynlmygninATAEDVyrvarlagihdailkmphkydtqvgergLKLSGGEKQRVAIARAILKNPPILL 622
Cdd:cd03230    79 PEEPSLYEN------------LTVREN----------------------------LKLSGGMKQRLALAQALLHDPELLI 118

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2569209806 623 YDEATSSLDSVTEENILTSMKEMVKDRTSVFIA-HRLSTIVD-ADEIIVLNQGKV 675
Cdd:cd03230   119 LDEPTSGLDPESRREFWELLRELKKEGKTILLSsHILEEAERlCDRVAILNNGRI 173
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
 463-691 1.90e-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: 137.87  E-value: 1.90e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 463 IRFEDVYFEYlEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGLESLRKAVGVV 542
Cdd:COG1120     2 LEAENLSVGY-GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 543 PQDAVL-FHNTIFYNLMYGNI-------NATAED---VYRVARLAGIHDaiLKmphkyDTQVGErglkLSGGEKQRVAIA 611
Cdd:COG1120    81 PQEPPApFGLTVRELVALGRYphlglfgRPSAEDreaVEEALERTGLEH--LA-----DRPVDE----LSGGERQRVLIA 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 612 RAILKNPPILLYDEATSSLDSVTEENILTSMKEMVKD--RTSVFIAHrlstivD-------ADEIIVLNQGKVAERGNHQ 682
Cdd:COG1120   150 RALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARErgRTVVMVLH------DlnlaaryADRLVLLKDGRIVAQGPPE 223


                  ....*....
gi 2569209806 683 TLLdTPGSL 691
Cdd:COG1120   224 EVL-TPELL 231
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
 475-675 2.93e-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: 135.74  E-value: 2.93e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 475 GQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNI--RDVGLESLRKAVGVVPQDAVLF-HN 551
Cdd:cd03262    12 DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKVGMVFQQFNLFpHL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 552 TIFYNLMYGNINA---TAEDVYRVAR--LA--GIHDAILKMPHkydtqvgerglKLSGGEKQRVAIARAILKNPPILLYD 624
Cdd:cd03262    92 TVLENITLAPIKVkgmSKAEAEERALelLEkvGLADKADAYPA-----------QLSGGQQQRVAIARALAMNPKVMLFD 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2569209806 625 EATSSLDSVTEENILTSMKEMVKD-RTSVFIAHRLSTIVD-ADEIIVLNQGKV 675
Cdd:cd03262   161 EPTSALDPELVGEVLDVMKDLAEEgMTMVVVTHEMGFAREvADRVIFMDDGRI 213
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
 459-693 3.17e-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: 139.85  E-value: 3.17e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 459 QEATIRFEDVYFEYlEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGLEslRKA 538
Cdd:COG3842     2 AMPALELENVSKRY-GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE--KRN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 539 VGVVPQDAVLF-HNTIFYNLMYG---------NINATAEDVYRVARLAGIHDailKMPHKydtqvgerglkLSGGEKQRV 608
Cdd:COG3842    79 VGMVFQDYALFpHLTVAENVAFGlrmrgvpkaEIRARVAELLELVGLEGLAD---RYPHQ-----------LSGGQQQRV 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 609 AIARAILKNPPILLYDEATSSLDSVTEENILTSMKEMVKDR--TSVFIAHRLS---TIvdADEIIVLNQGKVAERGNHQT 683
Cdd:COG3842   145 ALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELgiTFIYVTHDQEealAL--ADRIAVMNDGRIEQVGTPEE 222

                         250
                  ....*....|
gi 2569209806 684 LLDTPGSLYA 693
Cdd:COG3842   223 IYERPATRFV 232
PhnC COG3638
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ...
 463-675 1.58e-35

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


Pssm-ID: 442855 [Multi-domain]  Cd Length: 249  Bit Score: 134.80  E-value: 1.58e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 463 IRFEDVYFEYLEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGLESLRKA---V 539
Cdd:COG3638     3 LELRNLSKRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLrrrI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 540 GVVPQDavlfHN-----TIFYNLMYGNINAT-----------AEDVYRVarlagiHDAI--LKMPHKYDTQVGErglkLS 601
Cdd:COG3638    83 GMIFQQ----FNlvprlSVLTNVLAGRLGRTstwrsllglfpPEDRERA------LEALerVGLADKAYQRADQ----LS 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 602 GGEKQRVAIARAILKNPPILLYDEATSSLDSVTEENILTSMKEMVKDR--TSVFIAHRlstiVD-----ADEIIVLNQGK 674
Cdd:COG3638   149 GGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDgiTVVVNLHQ----VDlarryADRIIGLRDGR 224


                  .
gi 2569209806 675 V 675
Cdd:COG3638   225 V 225
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
 463-678 1.74e-35

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: 133.75  E-value: 1.74e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 463 IRFEDVYFEYLEGQ---KVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGleslrKAV 539
Cdd:cd03293     1 LEVRNVSKTYGGGGgavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG-----PDR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 540 GVVPQDAVLF-HNTIFYNLMYG---NINATAEDVYRVARL---AGIHDAILKMPHkydtqvgerglKLSGGEKQRVAIAR 612
Cdd:cd03293    76 GYVFQQDALLpWLTVLDNVALGlelQGVPKAEARERAEELlelVGLSGFENAYPH-----------QLSGGMRQRVALAR 144

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2569209806 613 AILKNPPILLYDEATSSLDSVTEENILTSMKEMVKDR--TSVFIAHRLS-TIVDADEIIVLNQ--GKVAER 678
Cdd:cd03293   145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETgkTVLLVTHDIDeAVFLADRVVVLSArpGRIVAE 215
PTZ00243 PTZ00243
ABC transporter; Provisional
 441-695 1.78e-35

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 144.92  E-value: 1.78e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806  441 VDTKIKEKEMAPP----LIVTP-----------QEATIRFEDVYFEYLEGQK-VLNGVSFEVPAGKKVAIVGGSGSGKST 504
Cdd:PTZ00243  1272 VDALERRTGMAADvtgtVVIEPasptsaaphpvQAGSLVFEGVQMRYREGLPlVLRGVSFRIAPREKVGIVGRTGSGKST 1351

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806  505 IVRLLFRFYEPQQGNIYIAGQNIRDVGLESLRKAVGVVPQDAVLFHNTIFYNLMyGNINATAEDVYRVARLAGIHDAILK 584
Cdd:PTZ00243  1352 LLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNVD-PFLEASSAEVWAALELVGLRERVAS 1430

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806  585 MPHKYDTQVGERGLKLSGGEKQRVAIARAILK-NPPILLYDEATSSLDSVTEENILTSMKEMVKDRTSVFIAHRLSTIVD 663
Cdd:PTZ00243  1431 ESEGIDSRVLEGGSNYSVGQRQLMCMARALLKkGSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQ 1510

                          250       260       270
                   ....*....|....*....|....*....|..
gi 2569209806  664 ADEIIVLNQGKVAERGNHQTLLDTPGSLYANL 695
Cdd:PTZ00243  1511 YDKIIVMDHGAVAEMGSPRELVMNRQSIFHSM 1542
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
 460-691 2.29e-35

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 135.26  E-value: 2.29e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 460 EATIRFEDVYFEYLEGQK-VLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGLESLRKA 538
Cdd:PRK13648    5 NSIIVFKNVSFQYQSDASfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKH 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 539 VGVVPQ--DAVLFHNTIFYNLMYG--NINATAEDVYRVARLAgIHDAILKMPHKYDTQvgerglKLSGGEKQRVAIARAI 614
Cdd:PRK13648   85 IGIVFQnpDNQFVGSIVKYDVAFGleNHAVPYDEMHRRVSEA-LKQVDMLERADYEPN------ALSGGQKQRVAIAGVL 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2569209806 615 LKNPPILLYDEATSSLDSVTEENILTSMKEM--VKDRTSVFIAHRLSTIVDADEIIVLNQGKVAERGNHQTLLDTPGSL 691
Cdd:PRK13648  158 ALNPSVIILDEATSMLDPDARQNLLDLVRKVksEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAEEL 236
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
 463-675 2.65e-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: 133.30  E-value: 2.65e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 463 IRFEDVYFEYLEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNI---RDVGLESLRKAV 539
Cdd:cd03292     1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsdlRGRAIPYLRRKI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 540 GVVPQDA-VLFHNTIFYNLM------YGNINATAEDVYRVARLAGIHDAILKMPHKydtqvgerglkLSGGEKQRVAIAR 612
Cdd:cd03292    81 GVVFQDFrLLPDRNVYENVAfalevtGVPPREIRKRVPAALELVGLSHKHRALPAE-----------LSGGEQQRVAIAR 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2569209806 613 AILKNPPILLYDEATSSLDSVTEENILTSMKEMVKDRTSVFIAHRLSTIVDA--DEIIVLNQGKV 675
Cdd:cd03292   150 AIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTtrHRVIALERGKL 214
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
 478-690 3.22e-35

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


Pssm-ID: 213266 [Multi-domain]  Cd Length: 235  Bit Score: 133.62  E-value: 3.22e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 478 VLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGLEslRKAVGVVPQDAVLF-HNTIFYN 556
Cdd:cd03299    14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFpHMTVYKN 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 557 LMYGNINAT------AEDVYRVARLAGIHDAILKMPhkydtqvgergLKLSGGEKQRVAIARAILKNPPILLYDEATSSL 630
Cdd:cd03299    92 IAYGLKKRKvdkkeiERKVLEIAEMLGIDHLLNRKP-----------ETLSGGEQQRVAIARALVVNPKILLLDEPFSAL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2569209806 631 DSVTEENILTSMKEMVK--DRTSVFIAHRLSTI-VDADEIIVLNQGKVAERGNHQTLLDTPGS 690
Cdd:cd03299   161 DVRTKEKLREELKKIRKefGVTVLHVTHDFEEAwALADKVAIMLNGKLIQVGKPEEVFKKPKN 223
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
 463-696 6.21e-35

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: 132.75  E-value: 6.21e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 463 IRFEDVYFEYlEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIrdVGLESLRKAVGVV 542
Cdd:cd03300     1 IELENVSKFY-GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--TNLPPHKRPVNTV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 543 PQDAVLF-HNTIFYNLMYG------NINATAEDVYRVARLAGIHDAILKMPHkydtqvgerglKLSGGEKQRVAIARAIL 615
Cdd:cd03300    78 FQNYALFpHLTVFENIAFGlrlkklPKAEIKERVAEALDLVQLEGYANRKPS-----------QLSGGQQQRVAIARALV 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 616 KNPPILLYDEATSSLDSVTEENILTSMKEMVKDR--TSVFIAHRLS-TIVDADEIIVLNQGKVAERGNHQTLLDTPgsly 692
Cdd:cd03300   147 NEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELgiTFVFVTHDQEeALTMSDRIAVMNKGKIQQIGTPEEIYEEP---- 222


                  ....
gi 2569209806 693 ANLW 696
Cdd:cd03300   223 ANRF 226
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
 463-674 6.46e-35

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


Pssm-ID: 213217 [Multi-domain]  Cd Length: 204  Bit Score: 131.82  E-value: 6.46e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 463 IRFEDVYFEYLEGQ----KVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQnirdvgleslrka 538
Cdd:cd03250     1 ISVEDASFTWDSGEqetsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 539 VGVVPQDAVLFHNTIFYNLMYGN-INataEDVYR-VARLAGIHDAILKMPHKYDTQVGERGLKLSGGEKQRVAIARAILK 616
Cdd:cd03250    68 IAYVSQEPWIQNGTIRENILFGKpFD---EERYEkVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYS 144

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 617 NPPILLYDEATSSLDSVTEENILTS--MKEMVKDRTSVFIAHRLSTIVDADEIIVLNQGK 674
Cdd:cd03250   145 DADIYLLDDPLSAVDAHVGRHIFENciLGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
 468-688 8.70e-35

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: 134.80  E-value: 8.70e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 468 VYFEYLEGQ-KVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQ---QGNIYIAGQNIRDVGLESLRKA----V 539
Cdd:COG0444     9 VYFPTRRGVvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKLSEKELRKIrgreI 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 540 GVVPQDA------VLfhnTIFYNLM-----YGNINATA--EDVYRVARLAGIHDA--ILKM-PHkydtQvgerglkLSGG 603
Cdd:COG0444    89 QMIFQDPmtslnpVM---TVGDQIAeplriHGGLSKAEarERAIELLERVGLPDPerRLDRyPH----E-------LSGG 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 604 EKQRVAIARAILKNPPILLYDEATSSLDSVTEENILTSMKEMVKDR--TSVFIAHRLSTIVD-ADEIIVLNQGKVAERGN 680
Cdd:COG0444   155 MRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELglAILFITHDLGVVAEiADRVAVMYAGRIVEEGP 234


                  ....*...
gi 2569209806 681 HQTLLDTP 688
Cdd:COG0444   235 VEELFENP 242
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
 466-679 8.92e-35

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: 130.25  E-value: 8.92e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 466 EDVYFEYlEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGLESLRKAVGVVPQd 545
Cdd:cd03214     3 ENLSVGY-GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 546 avlfhntifynlmygninataedvyrVARLAGIHDaiLKmphkydtqvgERGLK-LSGGEKQRVAIARAILKNPPILLYD 624
Cdd:cd03214    81 --------------------------ALELLGLAH--LA----------DRPFNeLSGGERQRVLLARALAQEPPILLLD 122

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2569209806 625 EATSSLDSVTEENILTSMKEMVKDR--TSVFIAHRLSTIVD-ADEIIVLNQGKVAERG 679
Cdd:cd03214   123 EPTSHLDIAHQIELLELLRRLARERgkTVVMVLHDLNLAARyADRVILLKDGRIVAQG 180
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
 464-676 1.35e-34

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: 131.12  E-value: 1.35e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 464 RFEDVYFEYlEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVgleslRKAVGVVP 543
Cdd:cd03235     1 EVEDLTVSY-GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGYVP 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 544 QDAVLfhNTIFynlmygniNATAEDVY---RVARLAGIH----------DAILK---MPHKYDTQVGErglkLSGGEKQR 607
Cdd:cd03235    75 QRRSI--DRDF--------PISVRDVVlmgLYGHKGLFRrlskadkakvDEALErvgLSELADRQIGE----LSGGQQQR 140

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2569209806 608 VAIARAILKNPPILLYDEATSSLDSVTEENILTSMKEM-VKDRTSVFIAHRLSTIVD-ADEIIVLNQGKVA 676
Cdd:cd03235   141 VLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLVLEyFDRVLLLNRTVVA 211
cbiO PRK13637
energy-coupling factor transporter ATPase;
462-680 1.94e-34

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 132.86  E-value: 1.94e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 462 TIRFEDVYFEYLEG----QKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRD--VGLESL 535
Cdd:PRK13637    2 SIKIENLTHIYMEGtpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDkkVKLSDI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 536 RKAVGVVPQ--DAVLFHNTIFYNLMYGNINATAED------VYRVARLAGIhdailkmphKYDTQVGERGLKLSGGEKQR 607
Cdd:PRK13637   82 RKKVGLVFQypEYQLFEETIEKDIAFGPINLGLSEeeienrVKRAMNIVGL---------DYEDYKDKSPFELSGGQKRR 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2569209806 608 VAIARAILKNPPILLYDEATSSLDSVTEENILTSMKEMVKDR--TSVFIAHRLSTIVD-ADEIIVLNQGKVAERGN 680
Cdd:PRK13637  153 VAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYnmTIILVSHSMEDVAKlADRIIVMNKGKCELQGT 228
ABC_membrane pfam00664
ABC transporter transmembrane region; This family represents a unit of six transmembrane ...
 131-415 2.46e-34

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: 132.38  E-value: 2.46e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 131 VVISLSLLAGAKITNVMVPFMFKYAVDSLNQmsghmlNLSDAPNTVVTMATAVLIGYGvsrtGSALFNELRNAVFGKVAQ 210
Cdd:pfam00664   1 LILAILLAILSGAISPAFPLVLGRILDVLLP------DGDPETQALNVYSLALLLLGL----AQFILSFLQSYLLNHTGE 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 211 SSIRRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGISFVLSALVFNLGPTLFEMMLVSGILYYKcGGHFALVTLG 290
Cdd:pfam00664  71 RLSRRLRRKLFKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYY-GWKLTLVLLA 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 291 TLSAYTAFTVAVTQWRTQFRIEMNKADNEAGNAAIDSLLNYETVKYFNNEKYEAERYDGFLKVYESSSLKTTSTLAMLNF 370
Cdd:pfam00664 150 VLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFG 229

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2569209806 371 GQSAIFSVGLTAIMVLASKGIMSGTMTVGDLVMVNGLLFQLSLPL 415
Cdd:pfam00664 230 ITQFIGYLSYALALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
459-679 1.01e-33

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 130.52  E-value: 1.01e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 459 QEATIRFEDVYFEYLEGQK-VLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGLESLRK 537
Cdd:PRK13635    2 KEEIIRVEHISFRYPDAATyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 538 AVGVVPQ------------DAVLF---HNTIFYNLMygninatAEDVYRVARLAGIHDAILKMPHKydtqvgerglkLSG 602
Cdd:PRK13635   82 QVGMVFQnpdnqfvgatvqDDVAFgleNIGVPREEM-------VERVDQALRQVGMEDFLNREPHR-----------LSG 143

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2569209806 603 GEKQRVAIARAILKNPPILLYDEATSSLDSVTEENILTSMKEMVKDR--TSVFIAHRLSTIVDADEIIVLNQGKVAERG 679
Cdd:PRK13635  144 GQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKgiTVLSITHDLDEAAQADRVIVMNKGEILEEG 222
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
 467-729 2.25e-33

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: 129.59  E-value: 2.25e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 467 DVYFEYLE-GQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEpQQGNIYIAGQNIRDVGLESLRKAVGVVPQD 545
Cdd:cd03289     7 DLTAKYTEgGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAFGVIPQK 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 546 AVLFHNTIFYNL-MYGNINAtaEDVYRVARLAGIHDAILKMPHKYDTQVGERGLKLSGGEKQRVAIARAILKNPPILLYD 624
Cdd:cd03289    86 VFIFSGTFRKNLdPYGKWSD--EEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLD 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 625 EATSSLDSVTEENILTSMKEMVKDRTSVFIAHRLSTIVDADEIIVLNQGKVAERGNHQTLLDTPGSLYANLWNTQNSRIL 704
Cdd:cd03289   164 EPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQAISPSDRLKLF 243

                         250       260
                  ....*....|....*....|....*....
gi 2569209806 705 ----SNGSKPEPVPERVSQKEEERKKLQE 729
Cdd:cd03289   244 prrnSSKSKRKPRPQIQALQEETEEEVQD 272
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
463-680 1.14e-32

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 129.43  E-value: 1.14e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 463 IRFEDVYFEYLEGQK---VLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNI---RDVGLESLR 536
Cdd:COG1135     2 IELENLSKTFPTKGGpvtALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLtalSERELRAAR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 537 KAVGVVPQdavlfHntifYNLM-----YGNI-----------NATAEDVYRVARLAGIHDAIlkmpHKYDTQvgerglkL 600
Cdd:COG1135    82 RKIGMIFQ-----H----FNLLssrtvAENValpleiagvpkAEIRKRVAELLELVGLSDKA----DAYPSQ-------L 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 601 SGGEKQRVAIARAILKNPPILLYDEATSSLDSVTEENILTSMKEmVKDR---TSVFIAHRLSTIVD-ADEIIVLNQGKVA 676
Cdd:COG1135   142 SGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKD-INRElglTIVLITHEMDVVRRiCDRVAVLENGRIV 220


                  ....
gi 2569209806 677 ERGN 680
Cdd:COG1135   221 EQGP 224
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
 463-676 1.56e-32

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: 126.14  E-value: 1.56e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 463 IRFEDVYFEYLEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVG---LESLRKAV 539
Cdd:cd03256     1 IEVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKgkaLRQLRRQI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 540 GVVPQDavlfhntifYNLMyGNINAtAEDVYrVARLAGIH--DAILKMPHKYDTQ--------VG------ERGLKLSGG 603
Cdd:cd03256    81 GMIFQQ---------FNLI-ERLSV-LENVL-SGRLGRRStwRSLFGLFPKEEKQralaalerVGlldkayQRADQLSGG 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2569209806 604 EKQRVAIARAILKNPPILLYDEATSSLDSVTEENILTSMKE--MVKDRTSVFIAHRLSTIVD-ADEIIVLNQGKVA 676
Cdd:cd03256   149 QQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRinREEGITVIVSLHQVDLAREyADRIVGLKDGRIV 224
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
 411-742 1.97e-32

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


Pssm-ID: 188098 [Multi-domain]  Cd Length: 1522  Bit Score: 135.46  E-value: 1.97e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806  411 LSLPLNFLGTVYRETRQALIDMNTLFTLLSvdtkikEKEMAPPLI----VTPQEA-TIRFEDVYFEYLEGQK-VLNGVSF 484
Cdd:TIGR00957  586 LRFPLNILPMVISSIVQASVSLKRLRIFLS------HEELEPDSIerrtIKPGEGnSITVHNATFTWARDLPpTLNGITF 659

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806  485 EVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGqnirdvgleslrkAVGVVPQDAVLFHNTIFYNLMYGNinA 564
Cdd:TIGR00957  660 SIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-------------SVAYVPQQAWIQNDSLRENILFGK--A 724

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806  565 TAEDVYRVARLAGIHDAILKM-PHKYDTQVGERGLKLSGGEKQRVAIARAILKNPPILLYDEATSSLDSVTEENILTSM- 642
Cdd:TIGR00957  725 LNEKYYQQVLEACALLPDLEIlPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVi 804

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806  643 --KEMVKDRTSVFIAHRLSTIVDADEIIVLNQGKVAERGNHQTLLDTPGSL------YANLWNTQNSR------ILSNGS 708
Cdd:TIGR00957  805 gpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFaeflrtYAPDEQQGHLEdswtalVSGEGK 884

                          330       340       350
                   ....*....|....*....|....*....|....
gi 2569209806  709 KPEPVPERVSQKEEERKKLQEEIMNSVKGCGNCS 742
Cdd:TIGR00957  885 EAKLIENGMLVTDVVGKQLQRQLSASSSDSGDQS 918
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
 482-688 1.98e-32

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: 129.08  E-value: 1.98e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 482 VSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVG----LESLRKAVGVVPQDAVLF-HNTIFYN 556
Cdd:TIGR02142  16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRkgifLPPEKRRIGYVFQEARLFpHLSVRGN 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 557 LMYGNINATAEdvYRVARLAGIHDaILKMPHKYDTQVGerglKLSGGEKQRVAIARAILKNPPILLYDEATSSLDSVTEE 636
Cdd:TIGR02142  96 LRYGMKRARPS--ERRISFERVIE-LLGIGHLLGRLPG----RLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKY 168

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2569209806 637 NILTSMkEMVKDRTS---VFIAHRLSTIVD-ADEIIVLNQGKVAERGNHQTLLDTP 688
Cdd:TIGR02142 169 EILPYL-ERLHAEFGipiLYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWASP 223
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
 475-692 2.77e-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: 126.22  E-value: 2.77e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 475 GQKV-LNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGLESL----RKAVGVVPQDAVLF 549
Cdd:cd03294    35 GQTVgVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALL 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 550 -HNTIFYNLMYG------NINATAEDVYRVARLAGIHDAILKMPHkydtqvgerglKLSGGEKQRVAIARAILKNPPILL 622
Cdd:cd03294   115 pHRTVLENVAFGlevqgvPRAEREERAAEALELVGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILL 183

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2569209806 623 YDEATSSLDSVteenILTSMKEMVKD------RTSVFIAHRLSTIVD-ADEIIVLNQGKVAERGNHQTLLDTPGSLY 692
Cdd:cd03294   184 MDEAFSALDPL----IRREMQDELLRlqaelqKTIVFITHDLDEALRlGDRIAIMKDGRLVQVGTPEEILTNPANDY 256
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
 457-677 4.62e-32

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


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 125.20  E-value: 4.62e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 457 TPQEATIRFEDVYFEYLEGQK---VLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGLE 533
Cdd:COG1116     2 SAAAPALELRGVSKRFPTGGGgvtALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 534 slrkaVGVVPQDAVLF-HNTIFYNLMYG------NINATAEDVYRVARLAGIHDAILKMPHkydtQvgerglkLSGGEKQ 606
Cdd:COG1116    82 -----RGVVFQEPALLpWLTVLDNVALGlelrgvPKAERRERARELLELVGLAGFEDAYPH----Q-------LSGGMRQ 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 607 RVAIARAILKNPPILLYDEATSSLDSVTEENIltsMKEMVK-----DRTSVFIAH------RLstivdADEIIVL--NQG 673
Cdd:COG1116   146 RVAIARALANDPEVLLMDEPFGALDALTRERL---QDELLRlwqetGKTVLFVTHdvdeavFL-----ADRVVVLsaRPG 217


                  ....
gi 2569209806 674 KVAE 677
Cdd:COG1116   218 RIVE 221
ABCC_SUR2 cd03288
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...
 463-695 5.17e-32

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: 125.02  E-value: 5.17e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 463 IRFEDVYFEYLEGQK-VLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGLESLRKAVGV 541
Cdd:cd03288    20 IKIHDLCVRYENNLKpVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 542 VPQDAVLFHNTIFYNLMyGNINATAEDVYRVARLAGIHDAILKMPHKYDTQVGERGLKLSGGEKQRVAIARAILKNPPIL 621
Cdd:cd03288   100 ILQDPILFSGSIRFNLD-PECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSIL 178

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2569209806 622 LYDEATSSLDSVTEeNILTSM-KEMVKDRTSVFIAHRLSTIVDADEIIVLNQGKVAERGNHQTLLDTPGSLYANL 695
Cdd:cd03288   179 IMDEATASIDMATE-NILQKVvMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVFASL 252
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
 462-692 5.48e-32

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: 124.37  E-value: 5.48e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 462 TIRFEDVYFEYlEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGLEslRKAVGV 541
Cdd:cd03296     2 SIEVRNVSKRF-GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVGF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 542 VPQDAVLF-HNTIFYNLMYG-------------NINATAEDVYRVARLAGIHDailkmphKYDTQvgerglkLSGGEKQR 607
Cdd:cd03296    79 VFQHYALFrHMTVFDNVAFGlrvkprserppeaEIRAKVHELLKLVQLDWLAD-------RYPAQ-------LSGGQRQR 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 608 VAIARAILKNPPILLYDEATSSLDSVTEENILTSMKEmVKDR---TSVFIAHRLSTIVD-ADEIIVLNQGKVAERGNHQT 683
Cdd:cd03296   145 VALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRR-LHDElhvTTVFVTHDQEEALEvADRVVVMNKGRIEQVGTPDE 223


                  ....*....
gi 2569209806 684 LLDTPGSLY 692
Cdd:cd03296   224 VYDHPASPF 232
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
 477-679 6.79e-32

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: 122.66  E-value: 6.79e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 477 KVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLL--FRFYEPQQGNIYIAGQNIRdvgLESLRKAVGVVPQDAVLF-HNTI 553
Cdd:cd03213    23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLD---KRSFRKIIGYVPQDDILHpTLTV 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 554 FYNLMYgninataedvyrVARLAGIhdailkmphkydtqvgerglklSGGEKQRVAIARAILKNPPILLYDEATSSLDSV 633
Cdd:cd03213   100 RETLMF------------AAKLRGL----------------------SGGERKRVSIALELVSNPSLLFLDEPTSGLDSS 145

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2569209806 634 TEENILTSMKEMVKD-RTSVFIAHRLSTIV--DADEIIVLNQGKVAERG 679
Cdd:cd03213   146 SALQVMSLLRRLADTgRTIICSIHQPSSEIfeLFDKLLLLSQGRVIYFG 194
ABC_6TM_exporters cd07346
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ...
 131-432 7.81e-32

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: 125.74  E-value: 7.81e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 131 VVISLSLLAGAKITNVMVPFMFKYAVDSLnqmsghmlnLSDAPNTVVTMATAVLIGYGVSRtgsALFNELRNAVFGKVAQ 210
Cdd:cd07346     1 LLLALLLLLLATALGLALPLLTKLLIDDV---------IPAGDLSLLLWIALLLLLLALLR---ALLSYLRRYLAARLGQ 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 211 SSIRRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGISFVLSALVFNLGPTLFEMMLVSGILYY---KcgghFALV 287
Cdd:cd07346    69 RVVFDLRRDLFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYlnwK----LTLV 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 288 TLGTLSAYTAFTVAVTQW-RTQFRIEMNKADNEAGNAAiDSLLNYETVKYFNNEKYEAERYDGFLKVYESSSLKTTSTLA 366
Cdd:cd07346   145 ALLLLPLYVLILRYFRRRiRKASREVRESLAELSAFLQ-ESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSA 223

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2569209806 367 MLNFGQSAIFSVGLTAIMVLASKGIMSGTMTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDM 432
Cdd:cd07346   224 LFSPLIGLLTALGTALVLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASL 289
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
 464-675 3.90e-31

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: 120.82  E-value: 3.90e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 464 RFEDVYFEYLEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGqniRDVGLESLRKAVGVVP 543
Cdd:cd03226     1 RIENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG---KPIKAKERRKSIGYVM 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 544 QDA--VLFHNTIFYNLMYGNINATA--EDVYRVARLAGIHDAILKMPHKydtqvgerglkLSGGEKQRVAIARAILKNPP 619
Cdd:cd03226    78 QDVdyQLFTDSVREELLLGLKELDAgnEQAETVLKDLDLYALKERHPLS-----------LSGGQKQRLAIAAALLSGKD 146

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2569209806 620 ILLYDEATSSLDSVTEENILTSMKEMVKDRTSVF-IAHRLSTIVD-ADEIIVLNQGKV 675
Cdd:cd03226   147 LLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIvITHDYEFLAKvCDRVLLLANGAI 204
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
 450-688 4.91e-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: 4.91e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 450 MAPPliVTPQEATIRFEDVYFEYleGQK-VLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYE--PQQ---GNIYIA 523
Cdd:COG1117     1 MTAP--ASTLEPKIEVRNLNVYY--GDKqALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPGArveGEILLD 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 524 GQNI--RDVGLESLRKAVGVVPQDAVLFHNTIFYNLMYGninataedvyrvARLAGIH-----DAI----LKMPHKYDtQ 592
Cdd:COG1117    77 GEDIydPDVDVVELRRRVGMVFQKPNPFPKSIYDNVAYG------------LRLHGIKskselDEIveesLRKAALWD-E 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 593 VGER----GLKLSGGEKQRVAIARAILKNPPILLYDEATSSLDSVTEENILTSMKEMVKDRTSVFIAH------RLStiv 662
Cdd:COG1117   144 VKDRlkksALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHnmqqaaRVS--- 220

                         250       260
                  ....*....|....*....|....*.
gi 2569209806 663 daDEIIVLNQGKVAERGNHQTLLDTP 688
Cdd:COG1117   221 --DYTAFFYLGELVEFGPTEQIFTNP 244
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
463-690 1.25e-30

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 120.24  E-value: 1.25e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 463 IRFEDVYFEYleGQKVLNgVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDvgLESLRKAVGVV 542
Cdd:COG3840     2 LRLDDLTYRY--GDFPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTA--LPPAERPVSML 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 543 PQDAVLF-HNTIFYNLMYG---NINATAEDVYRVARLAGihdailkmphkydtQVGERGLK------LSGGEKQRVAIAR 612
Cdd:COG3840    77 FQENNLFpHLTVAQNIGLGlrpGLKLTAEQRAQVEQALE--------------RVGLAGLLdrlpgqLSGGQRQRVALAR 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 613 AILKNPPILLYDEATSSLDSVTEENILTSMKEMVKDR--TSVFIAHRLSTIVD-ADEIIVLNQGKVAERGNHQTLLDTPG 689
Cdd:COG3840   143 CLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERglTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDGEP 222


                  .
gi 2569209806 690 S 690
Cdd:COG3840   223 P 223
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
 463-686 1.34e-30

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 121.38  E-value: 1.34e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 463 IRFEDVYFEYLEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGLESLRKAVGVV 542
Cdd:PRK13647    5 IEVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 543 PQDA--VLFHNTIFYNLMYGNIN---ATAEDVYRVA---RLAGIHDAILKMPHkydtqvgerglKLSGGEKQRVAIARAI 614
Cdd:PRK13647   85 FQDPddQVFSSTVWDDVAFGPVNmglDKDEVERRVEealKAVRMWDFRDKPPY-----------HLSYGQKKRVAIAGVL 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2569209806 615 LKNPPILLYDEATSSLDSVTEENILTSMKEMVKDRTSVFIA-HRLSTIVD-ADEIIVLNQGKVAERGNHQTLLD 686
Cdd:PRK13647  154 AMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDLAAEwADQVIVLKEGRVLAEGDKSLLTD 227
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
 477-693 1.59e-30

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


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 123.33  E-value: 1.59e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 477 KVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIrDVGLESLRKAVGVVPQDAVLF-HNTIFY 555
Cdd:COG1118    16 TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDL-FTNLPPRERRVGFVFQHYALFpHMTVAE 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 556 NLMYG---------NINATAEDVYRVARLAGIHDailkmphKYDTQvgerglkLSGGEKQRVAIARAILKNPPILLYDEA 626
Cdd:COG1118    95 NIAFGlrvrppskaEIRARVEELLELVQLEGLAD-------RYPSQ-------LSGGQRQRVALARALAVEPEVLLLDEP 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2569209806 627 TSSLDS-VTEEnILTSMKEMVKD--RTSVFIAH------RLstivdADEIIVLNQGKVAERGNHQTLLDTPGSLYA 693
Cdd:COG1118   161 FGALDAkVRKE-LRRWLRRLHDElgGTTVFVTHdqeealEL-----ADRVVVMNQGRIEQVGTPDEVYDRPATPFV 230
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
 458-729 2.82e-30

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: 128.49  E-value: 2.82e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806  458 PQEATIRFEDVYFEYLE-GQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEpQQGNIYIAGQNIRDVGLESLR 536
Cdd:TIGR01271 1213 PSGGQMDVQGLTAKYTEaGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWR 1291

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806  537 KAVGVVPQDAVLFHNTIFYNL----MYGNinataEDVYRVARLAGIHDAILKMPHKYDTQVGERGLKLSGGEKQRVAIAR 612
Cdd:TIGR01271 1292 KAFGVIPQKVFIFSGTFRKNLdpyeQWSD-----EEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLAR 1366

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806  613 AILKNPPILLYDEATSSLDSVTEENILTSMKEMVKDRTSVFIAHRLSTIVDADEIIVLNQGKVAERGNHQTLLDTPGSLY 692
Cdd:TIGR01271 1367 SILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLFK 1446

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 2569209806  693 ANLWNTQNSRILS----NGSKPEPVPERVSQKEEERKKLQE 729
Cdd:TIGR01271 1447 QAMSAADRLKLFPlhrrNSSKRKPQPKITALREEAEEEVQN 1487
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
 463-679 3.12e-30

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


Pssm-ID: 213268 [Multi-domain]  Cd Length: 213  Bit Score: 118.51  E-value: 3.12e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 463 IRFEDVYFEYlEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGqniRDV-GLESLRKAVGV 541
Cdd:cd03301     1 VELENVTKRF-GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGG---RDVtDLPPKDRDIAM 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 542 VPQDAVLF-HNTIFYNLMYG---------NINataEDVYRVARLAGIhDAILkmpHKYDTQvgerglkLSGGEKQRVAIA 611
Cdd:cd03301    77 VFQNYALYpHMTVYDNIAFGlklrkvpkdEID---ERVREVAELLQI-EHLL---DRKPKQ-------LSGGQRQRVALG 142

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2569209806 612 RAILKNPPILLYDEATSSLDSVTEENILTSMKEMVK--DRTSVFIAH-RLSTIVDADEIIVLNQGKVAERG 679
Cdd:cd03301   143 RAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQrlGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
 475-688 3.16e-30

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 119.85  E-value: 3.16e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 475 GQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNI---RDVG-----LESLRKAVGVVPQDA 546
Cdd:PRK11264   15 GQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtaRSLSqqkglIRQLRQHVGFVFQNF 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 547 VLF-HNTIFYNLMYGNINATAEDvyrvarlagiHDAILKMPHKYDTQVGERG------LKLSGGEKQRVAIARAILKNPP 619
Cdd:PRK11264   95 NLFpHRTVLENIIEGPVIVKGEP----------KEEATARARELLAKVGLAGketsypRRLSGGQQQRVAIARALAMRPE 164

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2569209806 620 ILLYDEATSSLDSVTEENILTSMKEMVKD-RTSVFIAHRLSTIVD-ADEIIVLNQGKVAERGNHQTLLDTP 688
Cdd:PRK11264  165 VILFDEPTSALDPELVGEVLNTIRQLAQEkRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFADP 235
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
463-690 3.46e-30

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 119.43  E-value: 3.46e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 463 IRFEDVYFEYleGQ-KVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRD--VGLESLRKAV 539
Cdd:PRK09493    2 IEFKNVSKHF--GPtQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDpkVDERLIRQEA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 540 GVVPQDAVLF-HNTIFYNLMYGNIN---ATAEDVYRVAR--LAGIhdAILKMPHKYDTQvgerglkLSGGEKQRVAIARA 613
Cdd:PRK09493   80 GMVFQQFYLFpHLTALENVMFGPLRvrgASKEEAEKQARelLAKV--GLAERAHHYPSE-------LSGGQQQRVAIARA 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2569209806 614 ILKNPPILLYDEATSSLDSVTEENILTSMKEMVKD-RTSVFIAHRLSTIVD-ADEIIVLNQGKVAERGNHQTLLDTPGS 690
Cdd:PRK09493  151 LAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEgMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLIKNPPS 229
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
 461-696 3.92e-30

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


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 122.10  E-value: 3.92e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 461 ATIRFEDVYFEYlEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGqniRDV-GLESLRKAV 539
Cdd:COG3839     2 ASLELENVSKSY-GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGG---RDVtDLPPKDRNI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 540 GVVPQDAVLF-HNTIFYNLMYG--NINATAEDVY-RVARLAgihdAILKMPHKYDTQVGErglkLSGGEKQRVAIARAIL 615
Cdd:COG3839    78 AMVFQSYALYpHMTVYENIAFPlkLRKVPKAEIDrRVREAA----ELLGLEDLLDRKPKQ----LSGGQRQRVALGRALV 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 616 KNPPILLYDEATSSLDSVTEENILTSMKEMVKDR--TSVFIAHrlstivD-------ADEIIVLNQGKVAergnhQtlLD 686
Cdd:COG3839   150 REPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLgtTTIYVTH------DqveamtlADRIAVMNDGRIQ-----Q--VG 216

                         250
                  ....*....|...
gi 2569209806 687 TPGSLY---ANLW 696
Cdd:COG3839   217 TPEELYdrpANLF 229
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
 463-679 3.98e-30

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 121.83  E-value: 3.98e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 463 IRFEDVYFEYLEGQK---VLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNI---RDVGLESLR 536
Cdd:PRK11153    2 IELKNISKVFPQGGRtihALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLtalSEKELRKAR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 537 KAVGVVPQdavlfHntifYNLM-----YGNI-------NATAEDVY-RVARL---AGIHDailKMpHKYDTQvgerglkL 600
Cdd:PRK11153   82 RQIGMIFQ-----H----FNLLssrtvFDNValplelaGTPKAEIKaRVTELlelVGLSD---KA-DRYPAQ-------L 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 601 SGGEKQRVAIARAILKNPPILLYDEATSSLDSVTEENILTSMKEMVKDR--TSVFIAHRLSTIVD-ADEIIVLNQGKVAE 677
Cdd:PRK11153  142 SGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRELglTIVLITHEMDVVKRiCDRVAVIDAGRLVE 221


                  ..
gi 2569209806 678 RG 679
Cdd:PRK11153  222 QG 223
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
 475-676 6.69e-30

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: 115.99  E-value: 6.69e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 475 GQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQ--NIRDVGlESLRKAVGVVPQdavlfhnt 552
Cdd:cd03216    12 GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKevSFASPR-DARRAGIAMVYQ-------- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 553 ifynlmygninataedvyrvarlagihdailkmphkydtqvgerglkLSGGEKQRVAIARAILKNPPILLYDEATSSLDS 632
Cdd:cd03216    83 -----------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTP 115

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2569209806 633 VTEENILTSMKEMVKD-RTSVFIAHRLSTIVD-ADEIIVLNQGKVA 676
Cdd:cd03216   116 AEVERLFKVIRRLRAQgVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
 477-738 8.02e-30

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 120.84  E-value: 8.02e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 477 KVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRD---VGLESLRKAVGVVpqdavlFHNTi 553
Cdd:PRK11308   29 KALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKadpEAQKLLRQKIQIV------FQNP- 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 554 fynlmYGNINATAedvyRVArlagihdAILKMPHKYDTQVG--ER-----------GLK----------LSGGEKQRVAI 610
Cdd:PRK11308  102 -----YGSLNPRK----KVG-------QILEEPLLINTSLSaaERrekalammakvGLRpehydryphmFSGGQRQRIAI 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 611 ARAILKNPPILLYDEATSSLDSVTEENILTSMKEMVKD-RTS-VFIAHRLStIVD--ADEIIVLNQGKVAERGNHQTLLD 686
Cdd:PRK11308  166 ARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQElGLSyVFISHDLS-VVEhiADEVMVMYLGRCVEKGTKEQIFN 244

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2569209806 687 TPGSLYanlwnTQnsRILSNGSKPEPVPERvsqkeeERKKLQEEI---MNSVKGC 738
Cdd:PRK11308  245 NPRHPY-----TQ--ALLSATPRLNPDDRR------ERIKLTGELpspLNPPPGC 286
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
 477-688 8.04e-30

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


Pssm-ID: 443658 [Multi-domain]  Cd Length: 329  Bit Score: 120.61  E-value: 8.04e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 477 KVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVG---LESLRKAVGVVPQD--AVLfhN 551
Cdd:COG4608    32 KAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSgreLRPLRRRMQMVFQDpyASL--N 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 552 ---TIfynlmyGNINATAEDVYRVARLAGIHDAILKM--------------PHkydtqvgerglKLSGGEKQRVAIARAI 614
Cdd:COG4608   110 prmTV------GDIIAEPLRIHGLASKAERRERVAELlelvglrpehadryPH-----------EFSGGQRQRIGIARAL 172

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2569209806 615 LKNPPILLYDEATSSLD-SVtEENILTSMKEMVKDR--TSVFIAHRLStIVD--ADEIIVLNQGKVAERGNHQTLLDTP 688
Cdd:COG4608   173 ALNPKLIVCDEPVSALDvSI-QAQVLNLLEDLQDELglTYLFISHDLS-VVRhiSDRVAVMYLGKIVEIAPRDELYARP 249
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
 482-679 8.52e-29

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


Pssm-ID: 213264 [Multi-domain]  Cd Length: 214  Bit Score: 114.31  E-value: 8.52e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 482 VSFEVPAGKkVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRD----VGLESLRKAVGVVPQDAVLF-HNTIFYN 556
Cdd:cd03297    17 IDFDLNEEV-TGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDsrkkINLPPQQRKIGLVFQQYALFpHLNVREN 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 557 LMYG-NINATAEDVYRVARLAGIHDAilkmphkydTQVGERG-LKLSGGEKQRVAIARAILKNPPILLYDEATSSLDSVT 634
Cdd:cd03297    96 LAFGlKRKRNREDRISVDELLDLLGL---------DHLLNRYpAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRAL 166

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2569209806 635 EENILTSMKEMVKD--RTSVFIAHRLSTIVD-ADEIIVLNQGKVAERG 679
Cdd:cd03297   167 RLQLLPELKQIKKNlnIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
PLN03232 PLN03232
ABC transporter C family member; Provisional
 328-730 1.26e-28

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 123.55  E-value: 1.26e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806  328 LLNYETVKYFNNEKYEAERYDGfLKVYESSSLKTTSTLAMLNfgqsaIFSVGLTAIMV-LASKGIMsgTMTVGDLVMVNG 406
Cdd:PLN03232   486 LASMDTVKCYAWEKSFESRIQG-IRNEELSWFRKAQLLSAFN-----SFILNSIPVVVtLVSFGVF--VLLGGDLTPARA 557

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806  407 L----LFQ-LSLPLNFLGTVYRETRQALIDMNTLFTLLSVDTKIKEKEmaPPLivTPQEATIRFEDVYFEY-LEGQK-VL 479
Cdd:PLN03232   558 FtslsLFAvLRSPLNMLPNLLSQVVNANVSLQRIEELLLSEERILAQN--PPL--QPGAPAISIKNGYFSWdSKTSKpTL 633

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806  480 NGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIagqnirdvglesLRKAVGVVPQDAVLFHNTIFYNLMY 559
Cdd:PLN03232   634 SDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVV------------IRGSVAYVPQVSWIFNATVRENILF 701

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806  560 GNiNATAEDVYRVARLAGIHDAILKMPHKYDTQVGERGLKLSGGEKQRVAIARAILKNPPILLYDEATSSLDSVTEENIL 639
Cdd:PLN03232   702 GS-DFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVF 780

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806  640 TS-MKEMVKDRTSVFIAHRLSTIVDADEIIVLNQGKVAERGNHQTLLDTpGSLYANLW------------NTQNSRILSN 706
Cdd:PLN03232   781 DScMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKS-GSLFKKLMenagkmdatqevNTNDENILKL 859

                          410       420       430
                   ....*....|....*....|....*....|.
gi 2569209806  707 GSKPE-PVPER---VSQKEEERKKL---QEE 730
Cdd:PLN03232   860 GPTVTiDVSERnlgSTKQGKRGRSVlvkQEE 890
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
 477-688 1.70e-28

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: 120.56  E-value: 1.70e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 477 KVLNGVSFEVPAGKKVAIVGGSGSGKST----IVRLLfrfyePQQGNIYIAGQNIRDVG---LESLRKAVGVVPQDAvlf 549
Cdd:COG4172   300 KAVDGVSLTLRRGETLGLVGESGSGKSTlglaLLRLI-----PSEGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDP--- 371

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 550 hntifynlmYGNIN-------------------ATAEDVY-RVARL---AGIH-DAILKMPHKydtqvgerglkLSGGEK 605
Cdd:COG4172   372 ---------FGSLSprmtvgqiiaeglrvhgpgLSAAERRaRVAEAleeVGLDpAARHRYPHE-----------FSGGQR 431

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 606 QRVAIARAILKNPPILLYDEATSSLDSVTEENILTSMKEMVKDR--TSVFIAHRLStIVDA--DEIIVLNQGKVAERGNH 681
Cdd:COG4172   432 QRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHglAYLFISHDLA-VVRAlaHRVMVMKDGKVVEQGPT 510


                  ....*..
gi 2569209806 682 QTLLDTP 688
Cdd:COG4172   511 EQVFDAP 517
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
 463-679 4.40e-28

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: 113.64  E-value: 4.40e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 463 IRFEDVYFEYlEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGN-IYIAGQ-----NIRDvglesLR 536
Cdd:COG1119     4 LELRNVTVRR-GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGErrggeDVWE-----LR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 537 KAVGVV-PQ------------DAVL--FHNTI-FYNlmygniNATAEDVYRVARLAgihdAILKMPHKYDTQVGErglkL 600
Cdd:COG1119    78 KRIGLVsPAlqlrfprdetvlDVVLsgFFDSIgLYR------EPTDEQRERARELL----ELLGLAHLADRPFGT----L 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 601 SGGEKQRVAIARAILKNPPILLYDEATSSLDSVTEENILTSMKEMVKD--RTSVFIAHRLSTIVDA-DEIIVLNQGKVAE 677
Cdd:COG1119   144 SQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEgaPTLVLVTHHVEEIPPGiTHVLLLKDGRVVA 223


                  ..
gi 2569209806 678 RG 679
Cdd:COG1119   224 AG 225
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
 463-679 6.36e-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: 111.82  E-value: 6.36e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 463 IRFEDVYFEYLEGQKVLngvSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQnirDVG-LESLRKAVGV 541
Cdd:cd03298     1 VRLDKIRFSYGEQPMHF---DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGV---DVTaAPPADRPVSM 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 542 VPQDAVLF-HNTIFYNLMYG---NINATAEDVYRVARLAGihdailkmphkydtQVGERGL------KLSGGEKQRVAIA 611
Cdd:cd03298    75 LFQENNLFaHLTVEQNVGLGlspGLKLTAEDRQAIEVALA--------------RVGLAGLekrlpgELSGGERQRVALA 140

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2569209806 612 RAILKNPPILLYDEATSSLDSVTEENILTSMKEMVKDR--TSVFIAHRLSTIVD-ADEIIVLNQGKVAERG 679
Cdd:cd03298   141 RVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETkmTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
 476-675 1.97e-27

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: 110.67  E-value: 1.97e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 476 QKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDvGLESLRKAVGVVPQdavlfHNTIFY 555
Cdd:cd03263    15 KPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGYCPQ-----FDALFD 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 556 NLmygninaTAED-VYRVARLAGIHDAI-----------LKMPHKYDTQVGErglkLSGGEKQRVAIARAILKNPPILLY 623
Cdd:cd03263    89 EL-------TVREhLRFYARLKGLPKSEikeevelllrvLGLTDKANKRART----LSGGMKRKLSLAIALIGGPSVLLL 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2569209806 624 DEATSSLDSVTEENILTSMKEMVKDRTSVFIAHRLSTI-VDADEIIVLNQGKV 675
Cdd:cd03263   158 DEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAeALCDRIAIMSDGKL 210
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
 482-688 2.49e-27

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: 114.04  E-value: 2.49e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 482 VSFEVPAGKKVAIVGGSGSGKSTIVRL---LFRfyePQQGNIYIAGQ------NIRDVGLEslRKAVGVVPQDAVLF-HN 551
Cdd:COG4148    18 VDFTLPGRGVTALFGPSGSGKTTLLRAiagLER---PDSGRIRLGGEvlqdsaRGIFLPPH--RRRIGYVFQEARLFpHL 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 552 TIFYNLMYG----NINATAEDVYRVARLAGIhDAILK-MPHKydtqvgerglkLSGGEKQRVAIARAILKNPPILLYDEA 626
Cdd:COG4148    93 SVRGNLLYGrkraPRAERRISFDEVVELLGI-GHLLDrRPAT-----------LSGGERQRVAIGRALLSSPRLLLMDEP 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2569209806 627 TSSLDSVTEENILTSMkEMVKDRTS---VFIAH------RLstivdADEIIVLNQGKVAERGNHQTLLDTP 688
Cdd:COG4148   161 LAALDLARKAEILPYL-ERLRDELDipiLYVSHsldevaRL-----ADHVVLLEQGRVVASGPLAEVLSRP 225
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
463-681 4.87e-27

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 109.58  E-value: 4.87e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 463 IRFEDVYFEYLEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNI---RDVGLESLRKAV 539
Cdd:PRK10908    2 IRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlKNREVPFLRRQI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 540 GVVPQD-AVLFHNTIFYNLMYGNI--NATAEDVYRVARLAGIHDAILKMPHKYDTQvgerglkLSGGEKQRVAIARAILK 616
Cdd:PRK10908   82 GMIFQDhHLLMDRTVYDNVAIPLIiaGASGDDIRRRVSAALDKVGLLDKAKNFPIQ-------LSGGEQQRVGIARAVVN 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2569209806 617 NPPILLYDEATSSLDSVTEENILTSMKEMVKDRTSVFIA-HRLSTIVDAD-EIIVLNQGKVAerGNH 681
Cdd:PRK10908  155 KPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMAtHDIGLISRRSyRMLTLSDGHLH--GGV 219
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
478-692 8.89e-27

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 112.51  E-value: 8.89e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 478 VLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGLEslRKAVGVVPQDAVLF-HNTIFYN 556
Cdd:PRK11432   21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ--QRDICMVFQSYALFpHMSLGEN 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 557 LMYG----NINAtAEDVYRVAR------LAGIHDailkmphKYDTQVgerglklSGGEKQRVAIARAILKNPPILLYDEA 626
Cdd:PRK11432   99 VGYGlkmlGVPK-EERKQRVKEalelvdLAGFED-------RYVDQI-------SGGQQQRVALARALILKPKVLLFDEP 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2569209806 627 TSSLDSvteeNILTSMKEMVKDR------TSVFIAHRLS-TIVDADEIIVLNQGKVAERGNHQTLLDTPGSLY 692
Cdd:PRK11432  164 LSNLDA----NLRRSMREKIRELqqqfniTSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRF 232
PLN03130 PLN03130
ABC transporter C family member; Provisional
 408-726 2.01e-26

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 116.38  E-value: 2.01e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806  408 LFQ-LSLPLNFLGTVYRETRQALIDMNTLFTLLSVDtkikEKEMAPPLIVTPQEATIRFEDVYFEY-LEGQK-VLNGVSF 484
Cdd:PLN03130   563 LFAvLRFPLFMLPNLITQAVNANVSLKRLEELLLAE----ERVLLPNPPLEPGLPAISIKNGYFSWdSKAERpTLSNINL 638

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806  485 EVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIagqnirdvglesLRKAVGVVPQDAVLFHNTIFYNLMYGNiNA 564
Cdd:PLN03130   639 DVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV------------IRGTVAYVPQVSWIFNATVRDNILFGS-PF 705

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806  565 TAEDVYRVARLAGIHDAILKMPHKYDTQVGERGLKLSGGEKQRVAIARAILKNPPILLYDEATSSLDS-VTEENILTSMK 643
Cdd:PLN03130   706 DPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAhVGRQVFDKCIK 785

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806  644 EMVKDRTSVFIAHRLSTIVDADEIIVLNQGKVAERGNHQTLLDTpGSLYanlwntqnSRILSNGSKPEPVPERVSQKEEE 723
Cdd:PLN03130   786 DELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNN-GPLF--------QKLMENAGKMEEYVEENGEEEDD 856


                   ...
gi 2569209806  724 RKK 726
Cdd:PLN03130   857 QTS 859
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
446-692 2.30e-26

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 111.58  E-value: 2.30e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 446 KEKEMAPPLIVTPqeaTIRFEDVYFEYlEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQ 525
Cdd:PRK09452    1 SKKLNKQPSSLSP---LVELRGISKSF-DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQ 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 526 NIRDVGLEslRKAVGVVPQDAVLF-HNTIFYNLMYG---------NINATAEDVYRVARLAGIHDailKMPHKydtqvge 595
Cdd:PRK09452   77 DITHVPAE--NRHVNTVFQSYALFpHMTVFENVAFGlrmqktpaaEITPRVMEALRMVQLEEFAQ---RKPHQ------- 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 596 rglkLSGGEKQRVAIARAILKNPPILLYDEATSSLDSVTEENILTSMKEMVKDR--TSVFIAH-RLSTIVDADEIIVLNQ 672
Cdd:PRK09452  145 ----LSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLgiTFVFVTHdQEEALTMSDRIVVMRD 220

                         250       260
                  ....*....|....*....|
gi 2569209806 673 GKVAERGNHQTLLDTPGSLY 692
Cdd:PRK09452  221 GRIEQDGTPREIYEEPKNLF 240
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
 478-686 4.00e-26

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


Pssm-ID: 213191 [Multi-domain]  Cd Length: 222  Bit Score: 107.13  E-value: 4.00e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 478 VLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRdvGLES---LRKAVGVVPQDAVLFHN-TI 553
Cdd:cd03224    15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDIT--GLPPherARAGIGYVPEGRRIFPElTV 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 554 FYNLMYG-------NINATAEDVY--------RVARLAGihdailkmphkydtqvgerglKLSGGEKQRVAIARAILKNP 618
Cdd:cd03224    93 EENLLLGayarrraKRKARLERVYelfprlkeRRKQLAG---------------------TLSGGEQQMLAIARALMSRP 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2569209806 619 PILLYDEATSSLDSVTEENILTSMKEMVKDRTSVFI----AHRLSTIvdADEIIVLNQGKVAERGNHQTLLD 686
Cdd:cd03224   152 KLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLveqnARFALEI--ADRAYVLERGRVVLEGTAAELLA 221
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
 368-678 4.65e-26

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 113.36  E-value: 4.65e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 368 LNFGQSAIFSVGLTAIMVLASKGIMSGTMTVGDLVMVNGLLFQLSLPLNFLGTVYRE--TRQALIDmnTLFTLLSVDTKI 445
Cdd:COG4178   268 LTFFTTGYGQLAVIFPILVAAPRYFAGEITLGGLMQAASAFGQVQGALSWFVDNYQSlaEWRATVD--RLAGFEEALEAA 345

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 446 KEKEMAPPLIVTPQEATIRFEDVYFEYLEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIyiagq 525
Cdd:COG4178   346 DALPEAASRIETSEDGALALEDLTLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRI----- 420

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 526 nIRDVGLESLrkavgVVPQDAVLFHNTIFYNLMYGNINATAED--VYRVARLAGIHDAIlkmpHKYDTQVgERGLKLSGG 603
Cdd:COG4178   421 -ARPAGARVL-----FLPQRPYLPLGTLREALLYPATAEAFSDaeLREALEAVGLGHLA----ERLDEEA-DWDQVLSLG 489

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2569209806 604 EKQRVAIARAILKNPPILLYDEATSSLDSVTEENILTSMKEMVKDRTSVFIAHRLSTIVDADEIIVLNQGKVAER 678
Cdd:COG4178   490 EQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLELTGDGSWQL 564
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
 478-677 6.04e-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: 106.75  E-value: 6.04e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 478 VLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNI----RDvGLESLRKA-VGVVPQDavlFHnt 552
Cdd:COG4181    27 ILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLfaldED-ARARLRARhVGFVFQS---FQ-- 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 553 ifynLMyGNINATaEDVYRVARLAGIHDA------ILKmphkydtQVG--ERgLK-----LSGGEKQRVAIARAILKNPP 619
Cdd:COG4181   101 ----LL-PTLTAL-ENVMLPLELAGRRDArararaLLE-------RVGlgHR-LDhypaqLSGGEQQRVALARAFATEPA 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 620 ILLYDEATSSLDSVTEENILTSMKEMVKDR--TSVFIAHRLSTIVDADEIIVLNQGKVAE 677
Cdd:COG4181   167 ILFADEPTGNLDAATGEQIIDLLFELNRERgtTLVLVTHDPALAARCDRVLRLRAGRLVE 226
cbiO PRK13641
energy-coupling factor transporter ATPase;
462-737 6.42e-26

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 108.38  E-value: 6.42e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 462 TIRFEDVYFEYLEG----QKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIR----DVGLE 533
Cdd:PRK13641    2 SIKFENVDYIYSPGtpmeKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 534 SLRKAVGVVPQ--DAVLFHNTIFYNLMYGNIN-ATAEDVYRVARLAGIHDAILkmphkyDTQVGERG-LKLSGGEKQRVA 609
Cdd:PRK13641   82 KLRKKVSLVFQfpEAQLFENTVLKDVEFGPKNfGFSEDEAKEKALKWLKKVGL------SEDLISKSpFELSGGQMRRVA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 610 IARAILKNPPILLYDEATSSLDSVTEENILTSMKEMVKD-RTSVFIAHRLSTIVD-ADEIIVLNQGKVAERgnhqtllDT 687
Cdd:PRK13641  156 IAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAgHTVILVTHNMDDVAEyADDVLVLEHGKLIKH-------AS 228

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2569209806 688 PGSLYAnlwntqNSRILSNGSKPEPVPERVSQKEEER-----------KKLQEEIMNSVKG 737
Cdd:PRK13641  229 PKEIFS------DKEWLKKHYLDEPATSRFASKLEKGgfkfsempltiDELVDGIKNNLKG 283
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
 475-679 7.85e-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: 105.74  E-value: 7.85e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 475 GQKVLNGVSFEVPAGKkVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGlESLRKAVGVVPQDavlfhntif 554
Cdd:cd03264    12 KKRALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQP-QKLRRRIGYLPQE--------- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 555 yNLMYGNInaTAED-VYRVARLAGIHDAilKMPHKYDTQVGERGL---------KLSGGEKQRVAIARAILKNPPILLYD 624
Cdd:cd03264    81 -FGVYPNF--TVREfLDYIAWLKGIPSK--EVKARVDEVLELVNLgdrakkkigSLSGGMRRRVGIAQALVGDPSILIVD 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2569209806 625 EATSSLDSVTEENILTSMKEMVKDRTSVFIAHRLSTIVD-ADEIIVLNQGKVAERG 679
Cdd:cd03264   156 EPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
 463-688 1.02e-25

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 107.58  E-value: 1.02e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 463 IRFEDVYFEYLEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGLESLRKAVGVV 542
Cdd:PRK13652    4 IETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 543 PQ--DAVLFHNTIFYNLMYGNIN------ATAEDVYRVARLAGIHDAILKMPHkydtqvgerglKLSGGEKQRVAIARAI 614
Cdd:PRK13652   84 FQnpDDQIFSPTVEQDIAFGPINlgldeeTVAHRVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGVI 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2569209806 615 LKNPPILLYDEATSSLDSVTEENILTSMKEMVKD--RTSVFIAHRLSTIVD-ADEIIVLNQGKVAERGNHQTLLDTP 688
Cdd:PRK13652  153 AMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETygMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFLQP 229
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
 475-691 2.17e-25

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 106.01  E-value: 2.17e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 475 GQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGLESLRKAVGVVPQDAVL---Fhn 551
Cdd:PRK13548   14 GRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsfpF-- 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 552 tifynlmygninaTAEDVYRVARLAG----IHDAILkmPHKYDTQVGERGLK------LSGGEKQRVAIARAIL------ 615
Cdd:PRK13548   92 -------------TVEEVVAMGRAPHglsrAEDDAL--VAAALAQVDLAHLAgrdypqLSGGEQQRVQLARVLAqlwepd 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2569209806 616 KNPPILLYDEATSSLDSVTEENILTSMKEMVKDR--TSVFIAHRLS-TIVDADEIIVLNQGKVAERGNHQTLLdTPGSL 691
Cdd:PRK13548  157 GPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERglAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPAEVL-TPETL 234
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
476-690 2.31e-25

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 105.82  E-value: 2.31e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 476 QKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDV-------------GLESLRKAVGVV 542
Cdd:PRK10619   18 HEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlkvadknQLRLLRTRLTMV 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 543 PQDAVLF-HNTIFYNLMYGNINataedVYRVARLAGIHDAIlkmphKYDTQVG--ERG-----LKLSGGEKQRVAIARAI 614
Cdd:PRK10619   98 FQHFNLWsHMTVLENVMEAPIQ-----VLGLSKQEARERAV-----KYLAKVGidERAqgkypVHLSGGQQQRVSIARAL 167

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2569209806 615 LKNPPILLYDEATSSLDSVTEENILTSMKEMVKD-RTSVFIAHRLSTIVD-ADEIIVLNQGKVAERGNHQTLLDTPGS 690
Cdd:PRK10619  168 AMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEgKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLFGNPQS 245
COG4559 COG4559
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
475-688 3.21e-25

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


Pssm-ID: 443620 [Multi-domain]  Cd Length: 258  Bit Score: 105.58  E-value: 3.21e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 475 GQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGLESLRKAVGVVPQDAVL---Fhn 551
Cdd:COG4559    13 GRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVLPQHSSLafpF-- 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 552 tifynlmygninaTAEDVYRVARLAGI--HDAILKMPHKYDTQVGERGLK------LSGGEKQRVAIARAI--LKNPP-- 619
Cdd:COG4559    91 -------------TVEEVVALGRAPHGssAAQDRQIVREALALVGLAHLAgrsyqtLSGGEQQRVQLARVLaqLWEPVdg 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2569209806 620 ---ILLYDEATSSLDSVTEENILTSMKEMVKDRTSVF-IAHRLS-TIVDADEIIVLNQGKVAERGNHQTLLDTP 688
Cdd:COG4559   158 gprWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVaVLHDLNlAAQYADRILLLHQGRLVAQGTPEEVLTDE 231
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
477-690 3.34e-25

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 107.86  E-value: 3.34e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 477 KVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQnirDVGLESLR-KAVGVVPQDAVLF-HNTIF 554
Cdd:PRK10851   16 QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGT---DVSRLHARdRKVGFVFQHYALFrHMTVF 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 555 YNLMYG--------NINATAEDvYRVARLAgihdAILKMPH---KYDTQvgerglkLSGGEKQRVAIARAILKNPPILLY 623
Cdd:PRK10851   93 DNIAFGltvlprreRPNAAAIK-AKVTQLL----EMVQLAHladRYPAQ-------LSGGQKQRVALARALAVEPQILLL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2569209806 624 DEATSSLDS-VTEE--NILTSMKEMVKdRTSVFIAHRLSTIVD-ADEIIVLNQGKVAERGNHQTLLDTPGS 690
Cdd:PRK10851  161 DEPFGALDAqVRKElrRWLRQLHEELK-FTSVFVTHDQEEAMEvADRVVVMSQGNIEQAGTPDQVWREPAT 230
cbiO PRK13644
energy-coupling factor transporter ATPase;
463-695 3.62e-25

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 105.84  E-value: 3.62e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 463 IRFEDVYFEYLEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVG-LESLRKAVGV 541
Cdd:PRK13644    2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVGI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 542 VPQ--DAVLFHNTIFYNLMYG--NINATAEDVYRVARLAGIHDAILKMPHKYDTQvgerglkLSGGEKQRVAIARAILKN 617
Cdd:PRK13644   82 VFQnpETQFVGRTVEEDLAFGpeNLCLPPIEIRKRVDRALAEIGLEKYRHRSPKT-------LSGGQGQCVALAGILTME 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2569209806 618 PPILLYDEATSSLDSVTEENILTSMKEM-VKDRTSVFIAHRLSTIVDADEIIVLNQGKVAERGNHQTLLDTPGSLYANL 695
Cdd:PRK13644  155 PECLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDVSLQTLGL 233
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
 475-677 4.39e-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: 104.44  E-value: 4.39e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 475 GQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRdvGLESLRKA---VGVVPQDAVLFHN 551
Cdd:cd03219    12 GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDIT--GLPPHEIArlgIGRTFQIPRLFPE 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 552 -TIFYNLMYGNINATAEDVYRVARLAGIHDA---------ILKMPHKYDTQVGErglkLSGGEKQRVAIARAILKNPPIL 621
Cdd:cd03219    90 lTVLENVMVAAQARTGSGLLLARARREEREAreraeelleRVGLADLADRPAGE----LSYGQQRRLEIARALATDPKLL 165

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2569209806 622 LYDEATSSLDSV-TEE--NILTSMKEmvKDRTSVFIAHRLSTIVD-ADEIIVLNQGKV-AE 677
Cdd:cd03219   166 LLDEPAAGLNPEeTEElaELIRELRE--RGITVLLVEHDMDVVMSlADRVTVLDQGRViAE 224
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
 461-674 4.48e-25

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: 103.33  E-value: 4.48e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 461 ATIRFEDVYFEYlEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGlESLRKAVG 540
Cdd:COG4133     1 MMLEAENLSCRR-GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAR-EDYRRRLA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 541 VVPQDAVLFH------NTIFYNLMYGnINATAEDVYRVARLAGIHDAIlkmphkyDTQVGerglKLSGGEKQRVAIARAI 614
Cdd:COG4133    79 YLGHADGLKPeltvreNLRFWAALYG-LRADREAIDEALEAVGLAGLA-------DLPVR----QLSAGQKRRVALARLL 146

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2569209806 615 LKNPPILLYDEATSSLDSVTEENILTSMKEMVKDRTSVFIA-HRLSTIvDADEIIVLNQGK 674
Cdd:COG4133   147 LSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTtHQPLEL-AAARVLDLGDFK 206
cbiO PRK13650
energy-coupling factor transporter ATPase;
463-675 1.06e-24

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 104.43  E-value: 1.06e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 463 IRFEDVYFEYLEGQK--VLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGLESLRKAVG 540
Cdd:PRK13650    5 IEVKNLTFKYKEDQEkyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 541 VVPQ--DAVLFHNTIFYNLMYGNIN---ATAEDVYRVAR---LAGIHDAILKMPHKydtqvgerglkLSGGEKQRVAIAR 612
Cdd:PRK13650   85 MVFQnpDNQFVGATVEDDVAFGLENkgiPHEEMKERVNEaleLVGMQDFKEREPAR-----------LSGGQKQRVAIAG 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2569209806 613 AILKNPPILLYDEATSSLDSVTEENILTSMKEMVKDR--TSVFIAHRLSTIVDADEIIVLNQGKV 675
Cdd:PRK13650  154 AVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYqmTVISITHDLDEVALSDRVLVMKNGQV 218
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
 455-679 1.14e-24

ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.


Pssm-ID: 213233 [Multi-domain]  Cd Length: 218  Bit Score: 102.83  E-value: 1.14e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 455 IVTPQEATIRFEDVYFEYlegqKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGLES 534
Cdd:cd03266     1 MITADALTKRFRDVKKTV----QAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 535 LRKaVGVVPQDAVLF------HNTIFYNLMYGNINATAEDvyRVARLAGIhdaiLKMPHKYDTQVGErglkLSGGEKQRV 608
Cdd:cd03266    77 RRR-LGFVSDSTGLYdrltarENLEYFAGLYGLKGDELTA--RLEELADR----LGMEELLDRRVGG----FSTGMRQKV 145

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2569209806 609 AIARAILKNPPILLYDEATSSLDSVTEENILTSMKEMvKD--RTSVFIAHRLSTIVD-ADEIIVLNQGKVAERG 679
Cdd:cd03266   146 AIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQL-RAlgKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
475-680 1.56e-24

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 107.80  E-value: 1.56e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 475 GQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVG-LESLRKAVGVVPQDAVLFHN-T 552
Cdd:COG1129    16 GVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSpRDAQAAGIAIIHQELNLVPNlS 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 553 IFYNLMYGN------------INATAEDVyrVARLaGIH-DAilkmphkyDTQVGErglkLSGGEKQRVAIARAILKNPP 619
Cdd:COG1129    96 VAENIFLGReprrgglidwraMRRRAREL--LARL-GLDiDP--------DTPVGD----LSVAQQQLVEIARALSRDAR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2569209806 620 ILLYDEATSSLDSVTEENILTSMKEMvKDR--TSVFIAHRLSTIVD-ADEIIVLNQGKVAERGN 680
Cdd:COG1129   161 VLILDEPTASLTEREVERLFRIIRRL-KAQgvAIIYISHRLDEVFEiADRVTVLRDGRLVGTGP 223
cbiO PRK13640
energy-coupling factor transporter ATPase;
458-679 2.65e-24

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 103.34  E-value: 2.65e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 458 PQEATIRFEDVYFEYLEGQK-VLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGN---IYIAGQNIRDVGLE 533
Cdd:PRK13640    1 MKDNIVEFKHVSFTYPDSKKpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAKTVW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 534 SLRKAVGVVpqdavlfhntiFYNLMYGNINATAED--VYRVARLAGIHDAILKMPHKYDTQVG------ERGLKLSGGEK 605
Cdd:PRK13640   81 DIREKVGIV-----------FQNPDNQFVGATVGDdvAFGLENRAVPRPEMIKIVRDVLADVGmldyidSEPANLSGGQK 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2569209806 606 QRVAIARAILKNPPILLYDEATSSLDSVTEENILTSMKEMVKDR--TSVFIAHRLSTIVDADEIIVLNQGKVAERG 679
Cdd:PRK13640  150 QRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLLAQG 225
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
 463-680 3.97e-24

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 103.00  E-value: 3.97e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 463 IRFEDVYFEYLEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNI--RDVGLESLRKAVG 540
Cdd:PRK13636    6 LKVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdySRKGLMKLRESVG 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 541 VVPQ--DAVLFHNTIFYNLMYG--NINATAEDVYRVARLAGIHDAILKMPHKyDTQVgerglkLSGGEKQRVAIARAILK 616
Cdd:PRK13636   86 MVFQdpDNQLFSASVYQDVSFGavNLKLPEDEVRKRVDNALKRTGIEHLKDK-PTHC------LSFGQKKRVAIAGVLVM 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2569209806 617 NPPILLYDEATSSLDSVTEENILTSMKEMVK--DRTSVFIAHRLSTI-VDADEIIVLNQGKVAERGN 680
Cdd:PRK13636  159 EPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVpLYCDNVFVMKEGRVILQGN 225
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
462-681 1.07e-23

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


Pssm-ID: 443326 [Multi-domain]  Cd Length: 242  Bit Score: 100.47  E-value: 1.07e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 462 TIRFEDVYFEYlEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAG------QNIRDVGLESL 535
Cdd:COG4161     2 SIQLKNINCFY-GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIRLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 536 RKAVGVVPQDAVLF-HNTIFYNLMYGNIN--------ATAEDVYRVARLaGIHDAILKMPhkydtqvgergLKLSGGEKQ 606
Cdd:COG4161    81 RQKVGMVFQQYNLWpHLTVMENLIEAPCKvlglskeqAREKAMKLLARL-RLTDKADRFP-----------LHLSGGQQQ 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 607 RVAIARAILKNPPILLYDEATSSLD-SVTEE--NILTSMKEMvkDRTSVFIAHRlstiVD-----ADEIIVLNQGKVAER 678
Cdd:COG4161   149 RVAIARALMMEPQVLLFDEPTAALDpEITAQvvEIIRELSQT--GITQVIVTHE----VEfarkvASQVVYMEKGRIIEQ 222


                  ...
gi 2569209806 679 GNH 681
Cdd:COG4161   223 GDA 225
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
 459-670 1.36e-23

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 99.79  E-value: 1.36e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 459 QEATIRFEDVYFEyLEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGLESLRKA 538
Cdd:PRK10247    4 NSPLLQLQNVGYL-AGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 539 VGVVPQDAVLFHNTIFYNLMYG-NINATAEDVYRVAR-LA--GIHDAILKMPhkydtqVGErglkLSGGEKQRVAIARAI 614
Cdd:PRK10247   83 VSYCAQTPTLFGDTVYDNLIFPwQIRNQQPDPAIFLDdLErfALPDTILTKN------IAE----LSGGEKQRISLIRNL 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2569209806 615 LKNPPILLYDEATSSLDSVTEENILTSMKEMVKDR--TSVFIAHRLSTIVDADEIIVL 670
Cdd:PRK10247  153 QFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQniAVLWVTHDKDEINHADKVITL 210
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
 463-694 2.24e-23

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 100.86  E-value: 2.24e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 463 IRFEDVYFEYLEG----QKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNI----RDVGLES 534
Cdd:PRK13634    3 ITFQKVEHRYQYKtpfeRRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkKNKKLKP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 535 LRKAVGVVPQ--DAVLFHNTIFYNLMYGNIN--ATAEDVYRVAR----LAGIHDAIL-KMPhkydtqvgergLKLSGGEK 605
Cdd:PRK13634   83 LRKKVGIVFQfpEHQLFEETVEKDICFGPMNfgVSEEDAKQKARemieLVGLPEELLaRSP-----------FELSGGQM 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 606 QRVAIARAILKNPPILLYDEATSSLDSVTEENILTSMKEMVKDR--TSVFIAHRLSTIVD-ADEIIVLNQGKVAERGNHQ 682
Cdd:PRK13634  152 RRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKglTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPR 231

                         250
                  ....*....|..
gi 2569209806 683 TLLDTPGSLYAN 694
Cdd:PRK13634  232 EIFADPDELEAI 243
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
483-686 3.22e-23

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 98.89  E-value: 3.22e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 483 SFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVglESLRKAVGVVPQDAVLF-HNTIFYNLMYG- 560
Cdd:PRK10771   19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTT--PPSRRPVSMLFQENNLFsHLTVAQNIGLGl 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 561 ----NINATAED-VYRVARLAGIHDAILKMPHKydtqvgerglkLSGGEKQRVAIARAILKNPPILLYDEATSSLDSVTE 635
Cdd:PRK10771   97 npglKLNAAQREkLHAIARQMGIEDLLARLPGQ-----------LSGGQRQRVALARCLVREQPILLLDEPFSALDPALR 165

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2569209806 636 ENILTSMKEMVKDR--TSVFIAHRLStivDADEI----IVLNQGKVAERGNHQTLLD 686
Cdd:PRK10771  166 QEMLTLVSQVCQERqlTLLMVSHSLE---DAARIaprsLVVADGRIAWDGPTDELLS 219
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
 473-670 5.12e-23

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


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 97.55  E-value: 5.12e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 473 LEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQ---QGNIYIAGQNIRDvgLESLRKAVGVVPQDAVLF 549
Cdd:COG4136    11 LGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTA--LPAEQRRIGILFQDDLLF 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 550 -HNTIFYNLMYgninATAEDVYRVARLAGIHDAI--LKMPHKYDTQVGErglkLSGGEKQRVAIARAILKNPPILLYDEA 626
Cdd:COG4136    89 pHLSVGENLAF----ALPPTIGRAQRRARVEQALeeAGLAGFADRDPAT----LSGGQRARVALLRALLAEPRALLLDEP 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2569209806 627 TSSLDSVTEENILTSMKEMVKDRT--SVFIAHRLSTIVDADEIIVL 670
Cdd:COG4136   161 FSKLDAALRAQFREFVFEQIRQRGipALLVTHDEEDAPAAGRVLDL 206
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
 467-694 5.67e-23

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 99.38  E-value: 5.67e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 467 DVYFEYLEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIR--DVGLESLRKAVGVVPQ 544
Cdd:PRK13639    6 DLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydKKSLLEVRKTVGIVFQ 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 545 --DAVLFHNTIFYNLMYG--NINATAEDVYRVARLA----GIHDAILKMPHKydtqvgerglkLSGGEKQRVAIARAILK 616
Cdd:PRK13639   86 npDDQLFAPTVEEDVAFGplNLGLSKEEVEKRVKEAlkavGMEGFENKPPHH-----------LSGGQKKRVAIAGILAM 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 617 NPPILLYDEATSSLDSVTEENILTSMKEMVKDRTSVFIA-HRLSTI-VDADEIIVLNQGKVAERGnhqtlldTPGSLYAN 694
Cdd:PRK13639  155 KPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIIStHDVDLVpVYADKVYVMSDGKIIKEG-------TPKEVFSD 227
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
 476-692 6.78e-23

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: 103.23  E-value: 6.78e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 476 QKVLNGVSFEVPAGKKVAIVGGSGSGKS----TIVRLLFRFYEPQQGNIYIAGQNIRDVGLESLRK----AVGVVPQD-- 545
Cdd:COG4172    23 VEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRirgnRIAMIFQEpm 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 546 ---------------AVLFHNTifynlMYGninATAEDvyRVARL---AGIHDAILKM---PHKydtqvgerglkLSGGE 604
Cdd:COG4172   103 tslnplhtigkqiaeVLRLHRG-----LSG---AAARA--RALELlerVGIPDPERRLdayPHQ-----------LSGGQ 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 605 KQRVAIARAILKNPPILLYDEATSSLDSVTEENILTSMKEMVKDR-TSV-FIAHRLsTIVD--ADEIIVLNQGKVAERGN 680
Cdd:COG4172   162 RQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELgMALlLITHDL-GVVRrfADRVAVMRQGEIVEQGP 240

                         250
                  ....*....|..
gi 2569209806 681 HQTLLDTPGSLY 692
Cdd:COG4172   241 TAELFAAPQHPY 252
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
 477-688 7.44e-23

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 98.45  E-value: 7.44e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 477 KVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYE--PQ---QGNIYIAGQNIRDVGLESLRKAVGVVPQDAVLFHN 551
Cdd:PRK14247   17 EVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEarvSGEVYLDGQDIFKMDVIELRRRVQMVFQIPNPIPN 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 552 -TIFYNLMYGN-----INATAEDVYRVaRLAgIHDAIL--KMPHKYDTQVGerglKLSGGEKQRVAIARAILKNPPILLY 623
Cdd:PRK14247   97 lSIFENVALGLklnrlVKSKKELQERV-RWA-LEKAQLwdEVKDRLDAPAG----KLSGGQQQRLCIARALAFQPEVLLA 170

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2569209806 624 DEATSSLDSVTEENILTSMKEMVKDRTSVFIAH------RLStivdaDEIIVLNQGKVAERGNHQTLLDTP 688
Cdd:PRK14247  171 DEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRIS-----DYVAFLYKGQIVEWGPTREVFTNP 236
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
475-675 7.53e-23

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 100.72  E-value: 7.53e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 475 GQKVLNgVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRD----VGLESLRKAVGVVPQDAVLF- 549
Cdd:PRK11144   11 GDLCLT-VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDaekgICLPPEKRRIGYVFQDARLFp 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 550 HNTIFYNLMYGNINATAEDVYRVARLAGIHDAILKMPHKydtqvgerglkLSGGEKQRVAIARAILKNPPILLYDEATSS 629
Cdd:PRK11144   90 HYKVRGNLRYGMAKSMVAQFDKIVALLGIEPLLDRYPGS-----------LSGGEKQRVAIGRALLTAPELLLMDEPLAS 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2569209806 630 LDSVTEENILTSMKEMVKDRTS--VFIAHRLSTIVD-ADEIIVLNQGKV 675
Cdd:PRK11144  159 LDLPRKRELLPYLERLAREINIpiLYVSHSLDEILRlADRVVVLEQGKV 207
cbiO PRK13642
energy-coupling factor transporter ATPase;
463-687 7.96e-23

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 99.01  E-value: 7.96e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 463 IRFEDVYFEYLEGQKV--LNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGLESLRKAVG 540
Cdd:PRK13642    5 LEVENLVFKYEKESDVnqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 541 VVPQ--DAVLFHNTIFYNLMYGNINataEDVYRVARLAGIHDAILKMpHKYDTQVGERGlKLSGGEKQRVAIARAILKNP 618
Cdd:PRK13642   85 MVFQnpDNQFVGATVEDDVAFGMEN---QGIPREEMIKRVDEALLAV-NMLDFKTREPA-RLSGGQKQRVAVAGIIALRP 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2569209806 619 PILLYDEATSSLDSVTEENILTSMKEmVKDR---TSVFIAHRLSTIVDADEIIVLNQGKVAERGNHQTLLDT 687
Cdd:PRK13642  160 EIIILDESTSMLDPTGRQEIMRVIHE-IKEKyqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFAT 230
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
 462-682 8.29e-23

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 98.16  E-value: 8.29e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 462 TIRFEDVYFEYLEGQkVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAG------QNIRDVGLESL 535
Cdd:PRK11124    2 SIQLNGINCFYGAHQ-ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAIREL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 536 RKAVGVVPQDAVLF-HNTIFYNLmygnINATAEdVYRVARLAGIHDA--ILKMPHKydTQVGER-GLKLSGGEKQRVAIA 611
Cdd:PRK11124   81 RRNVGMVFQQYNLWpHLTVQQNL----IEAPCR-VLGLSKDQALARAekLLERLRL--KPYADRfPLHLSGGQQQRVAIA 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2569209806 612 RAILKNPPILLYDEATSSLDSVTEENILTSMKEMVKDR-TSVFIAHRlstiVD-----ADEIIVLNQGKVAERGNHQ 682
Cdd:PRK11124  154 RALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGiTQVIVTHE----VEvarktASRVVYMENGHIVEQGDAS 226
PTZ00243 PTZ00243
ABC transporter; Provisional
 457-695 8.94e-23

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 104.48  E-value: 8.94e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806  457 TPQEATirfeDVYFEyLEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAgqnirdvgleslr 536
Cdd:PTZ00243   659 TPKMKT----DDFFE-LEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE------------- 720

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806  537 KAVGVVPQDAVLFHNTIFYNLMYGNINATAE--DVYRVARLAGihdAILKMPHKYDTQVGERGLKLSGGEKQRVAIARAI 614
Cdd:PTZ00243   721 RSIAYVPQQAWIMNATVRGNILFFDEEDAARlaDAVRVSQLEA---DLAQLGGGLETEIGEKGVNLSGGQKARVSLARAV 797

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806  615 LKNPPILLYDEATSSLDS-----VTEENILTSMkemvKDRTSVFIAHRLSTIVDADEIIVLNQGKVAERGNHQTLLDTPg 689
Cdd:PTZ00243   798 YANRDVYLLDDPLSALDAhvgerVVEECFLGAL----AGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMRTS- 872


                   ....*.
gi 2569209806  690 sLYANL 695
Cdd:PTZ00243   873 -LYATL 877
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
 478-634 9.06e-23

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


Pssm-ID: 443809 [Multi-domain]  Cd Length: 229  Bit Score: 97.50  E-value: 9.06e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 478 VLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYI--AGQNI-------RDVgLESLRKAVGVVPQdavl 548
Cdd:COG4778    26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVdlaqaspREI-LALRRRTIGYVSQ---- 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 549 FHNTIfynlmygnINATAEDVyrVA---RLAGIHDAILKmphkydtqvgERGLKL------------------SGGEKQR 607
Cdd:COG4778   101 FLRVI--------PRVSALDV--VAeplLERGVDREEAR----------ARARELlarlnlperlwdlppatfSGGEQQR 160

                         170       180
                  ....*....|....*....|....*..
gi 2569209806 608 VAIARAILKNPPILLYDEATSSLDSVT 634
Cdd:COG4778   161 VNIARGFIADPPLLLLDEPTASLDAAN 187
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
460-680 1.20e-22

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 98.62  E-value: 1.20e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 460 EATIRFEDVYFEYLEGQK-----VLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVG-LE 533
Cdd:PRK13633    2 NEMIKCKNVSYKYESNEEsteklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnLW 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 534 SLRKAVGVVPQ--DAVLFHNTIFYNLMYG--NINATAEDVY-RVarlagihDAILKMPHKYDTQVGERGLkLSGGEKQRV 608
Cdd:PRK13633   82 DIRNKAGMVFQnpDNQIVATIVEEDVAFGpeNLGIPPEEIReRV-------DESLKKVGMYEYRRHAPHL-LSGGQKQRV 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2569209806 609 AIARAILKNPPILLYDEATSSLDSVTEENILTSMKEMVKDR--TSVFIAHRLSTIVDADEIIVLNQGKVAERGN 680
Cdd:PRK13633  154 AIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEAVEADRIIVMDSGKVVMEGT 227
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
 463-661 1.51e-22

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 97.80  E-value: 1.51e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 463 IRFEDVYFEYlEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQ-----QGNIYIAGQNI--RDVGLESL 535
Cdd:PRK14258    8 IKVNNLSFYY-DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVEFFNQNIyeRRVNLNRL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 536 RKAVGVVPQDAVLFHNTIFYNLMYG----------NINATAEDVYRVARLagiHDAILKMPHKydtqvgeRGLKLSGGEK 605
Cdd:PRK14258   87 RRQVSMVHPKPNLFPMSVYDNVAYGvkivgwrpklEIDDIVESALKDADL---WDEIKHKIHK-------SALDLSGGQQ 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2569209806 606 QRVAIARAILKNPPILLYDEATSSLD---SVTEENILTSMKeMVKDRTSVFIAHRLSTI 661
Cdd:PRK14258  157 QRLCIARALAVKPKVLLMDEPCFGLDpiaSMKVESLIQSLR-LRSELTMVIVSHNLHQV 214
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
 478-688 1.72e-22

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: 96.97  E-value: 1.72e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 478 VLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGLESL-RKAVGVVPQDAVLFHN-TIFY 555
Cdd:COG0410    18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIaRLGIGYVPEGRRIFPSlTVEE 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 556 NLMYG--------NINATAEDVY--------RVARLAGihdailkmphkydtqvgerglKLSGGEKQRVAIARAILKNPP 619
Cdd:COG0410    98 NLLLGayarrdraEVRADLERVYelfprlkeRRRQRAG---------------------TLSGGEQQMLAIGRALMSRPK 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2569209806 620 ILLYDEATSSLD-SVTEEnILTSMKEMVKDRTSVFI----AHRLSTIvdADEIIVLNQGKVAERGNHQTLLDTP 688
Cdd:COG0410   157 LLLLDEPSLGLApLIVEE-IFEIIRRLNREGVTILLveqnARFALEI--ADRAYVLERGRIVLEGTAAELLADP 227
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
 475-679 1.80e-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: 96.13  E-value: 1.80e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 475 GQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDvgLESLRKAVGVVpqdavlfhntIF 554
Cdd:cd03268    12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK--NIEALRRIGAL----------IE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 555 YNLMYGNINATaEDVYRVARLAGIHDAILK-------MPHKYDTQVGerglKLSGGEKQRVAIARAILKNPPILLYDEAT 627
Cdd:cd03268    80 APGFYPNLTAR-ENLRLLARLLGIRKKRIDevldvvgLKDSAKKKVK----GFSLGMKQRLGIALALLGNPDLLILDEPT 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2569209806 628 SSLDSVteeniltSMKEM------VKDR-TSVFIA-HRLSTIVD-ADEIIVLNQGKVAERG 679
Cdd:cd03268   155 NGLDPD-------GIKELrelilsLRDQgITVLISsHLLSEIQKvADRIGIINKGKLIEEG 208
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
 477-679 1.81e-22

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 99.15  E-value: 1.81e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 477 KVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYI----AGQNIRDVG------------LESLRKAVG 540
Cdd:PRK13631   40 VALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyIGDKKNNHElitnpyskkiknFKELRRRVS 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 541 VVPQ--DAVLFHNTIFYNLMYGNInATAEDVYRVARLAGIHdaILKMPHKYDTQvgERG-LKLSGGEKQRVAIARAILKN 617
Cdd:PRK13631  120 MVFQfpEYQLFKDTIEKDIMFGPV-ALGVKKSEAKKLAKFY--LNKMGLDDSYL--ERSpFGLSGGQKRRVAIAGILAIQ 194

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2569209806 618 PPILLYDEATSSLDSVTEENILTSMKEMVKDRTSVF-IAHRLSTIVD-ADEIIVLNQGKVAERG 679
Cdd:PRK13631  195 PEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFvITHTMEHVLEvADEVIVMDKGKILKTG 258
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
 479-685 2.82e-22

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 97.16  E-value: 2.82e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 479 LNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYE-----PQQGNIYIAGQNIRDVGLE--SLRKAVGVVPQDAVLFHN 551
Cdd:PRK14243   26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNLYAPDVDpvEVRRRIGMVFQKPNPFPK 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 552 TIFYNLMYG-NINATAED----VYRVARLAGIHDAIlkmphkyDTQVGERGLKLSGGEKQRVAIARAILKNPPILLYDEA 626
Cdd:PRK14243  106 SIYDNIAYGaRINGYKGDmdelVERSLRQAALWDEV-------KDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEP 178

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2569209806 627 TSSLDSVTEENILTSMKEMVKDRTSVFIAHRLSTIVDADEIIVLNQGKVAERGNHQTLL 685
Cdd:PRK14243  179 CSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFNVELTEGGGRYGYL 237
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
 463-673 3.85e-22

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: 95.48  E-value: 3.85e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 463 IRFEDVYFEYLEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGLESL----RKA 538
Cdd:cd03290     1 VQVTNGYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATrsrnRYS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 539 VGVVPQDAVLFHNTIFYNLMYGNinataedVYRVARLAGIHDA------ILKMPHKYDTQVGERGLKLSGGEKQRVAIAR 612
Cdd:cd03290    81 VAYAAQKPWLLNATVEENITFGS-------PFNKQRYKAVTDAcslqpdIDLLPFGDQTEIGERGINLSGGQRQRICVAR 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2569209806 613 AILKNPPILLYDEATSSL-----DSVTEENILTSMKEmvKDRTSVFIAHRLSTIVDADEIIVLNQG 673
Cdd:cd03290   154 ALYQNTNIVFLDDPFSALdihlsDHLMQEGILKFLQD--DKRTLVLVTHKLQYLPHADWIIAMKDG 217
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
476-677 6.16e-22

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 96.29  E-value: 6.16e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 476 QKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNI---RDVGLESLRKAVGVVPQDAVlfhnt 552
Cdd:PRK10419   25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLaklNRAQRKAFRRDIQMVFQDSI----- 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 553 ifynlmyGNINA-------TAE------DVYRVARLAGIhDAILKMPHKYDTQVGERGLKLSGGEKQRVAIARAILKNPP 619
Cdd:PRK10419  100 -------SAVNPrktvreiIREplrhllSLDKAERLARA-SEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPK 171

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2569209806 620 ILLYDEATSSLDSVTEENILTSMKEMVKDRTS--VFIAHRLStIVD--ADEIIVLNQGKVAE 677
Cdd:PRK10419  172 LLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTacLFITHDLR-LVErfCQRVMVMDNGQIVE 232
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
 478-692 1.04e-21

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 99.39  E-value: 1.04e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 478 VLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYePQQGNIYIAGQNIRDVG---LESLRKAVGVVPQDAvlfhntif 554
Cdd:PRK15134  301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNrrqLLPVRHRIQVVFQDP-------- 371

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 555 ynlmYGNINATAEDVYRVARLAGIHDAILKmPHKYDTQV----GERGL----------KLSGGEKQRVAIARAILKNPPI 620
Cdd:PRK15134  372 ----NSSLNPRLNVLQIIEEGLRVHQPTLS-AAQREQQViavmEEVGLdpetrhrypaEFSGGQRQRIAIARALILKPSL 446

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2569209806 621 LLYDEATSSLDSVTEENILTSMKEMVKDR--TSVFIAHRLStIVDA--DEIIVLNQGKVAERGNHQTLLDTPGSLY 692
Cdd:PRK15134  447 IILDEPTSSLDKTVQAQILALLKSLQQKHqlAYLFISHDLH-VVRAlcHQVIVLRQGEVVEQGDCERVFAAPQQEY 521
cbiO PRK13649
energy-coupling factor transporter ATPase;
463-679 1.06e-21

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 95.97  E-value: 1.06e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 463 IRFEDVYFEYLEGQ----KVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVG----LES 534
Cdd:PRK13649    3 INLQNVSYTYQAGTpfegRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdIKQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 535 LRKAVGVVPQ--DAVLFHNTIFYNLMYG--NINATAEDVYRVAR----LAGIHDAIL-KMPhkydtqvgergLKLSGGEK 605
Cdd:PRK13649   83 IRKKVGLVFQfpESQLFEETVLKDVAFGpqNFGVSQEEAEALAReklaLVGISESLFeKNP-----------FELSGGQM 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2569209806 606 QRVAIARAILKNPPILLYDEATSSLDSVTEENILTSMKEMVKD-RTSVFIAHRLSTIVD-ADEIIVLNQGKVAERG 679
Cdd:PRK13649  152 RRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSgMTIVLVTHLMDDVANyADFVYVLEKGKLVLSG 227
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
 473-673 2.27e-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: 94.92  E-value: 2.27e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 473 LEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQnirdvgleslrkaVGVVPQDAVLFHNT 552
Cdd:cd03291    47 LVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQFSWIMPGT 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 553 IFYNLMYGninaTAEDVYR---VARLAGIHDAILKMPHKYDTQVGERGLKLSGGEKQRVAIARAILKNPPILLYDEATSS 629
Cdd:cd03291   114 IKENIIFG----VSYDEYRyksVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGY 189

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2569209806 630 LDSVTEENILTS-MKEMVKDRTSVFIAHRLSTIVDADEIIVLNQG 673
Cdd:cd03291   190 LDVFTEKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEG 234
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
483-692 3.01e-21

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


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 96.64  E-value: 3.01e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 483 SFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGLESL----RKAVGVVPQD-AVLFHNTIFYNL 557
Cdd:PRK10070   48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELrevrRKKIAMVFQSfALMPHMTVLDNT 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 558 MYG-NINATAEDVYRVARLAGIHDAILK-MPHKYDTQvgerglkLSGGEKQRVAIARAILKNPPILLYDEATSSLDSVte 635
Cdd:PRK10070  128 AFGmELAGINAEERREKALDALRQVGLEnYAHSYPDE-------LSGGMRQRVGLARALAINPDILLMDEAFSALDPL-- 198

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2569209806 636 enILTSMK-EMVK-----DRTSVFIAHRLSTIVD-ADEIIVLNQGKVAERGNHQTLLDTPGSLY 692
Cdd:PRK10070  199 --IRTEMQdELVKlqakhQRTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEILNNPANDY 260
cbiO PRK13646
energy-coupling factor transporter ATPase;
462-684 5.68e-21

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 93.69  E-value: 5.68e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 462 TIRFEDVYFEYLEG----QKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNI----RDVGLE 533
Cdd:PRK13646    2 TIRFDNVSYTYQKGtpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktKDKYIR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 534 SLRKAVGVVPQ--DAVLFHNTIFYNLMYG--NINATAEDVYRVArlagiHDAILKMPHKYDTqVGERGLKLSGGEKQRVA 609
Cdd:PRK13646   82 PVRKRIGMVFQfpESQLFEDTVEREIIFGpkNFKMNLDEVKNYA-----HRLLMDLGFSRDV-MSQSPFQMSGGQMRKIA 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2569209806 610 IARAILKNPPILLYDEATSSLDSVTEENILTSMKEMVKD--RTSVFIAHRLSTIVD-ADEIIVLNQGKVAERGNHQTL 684
Cdd:PRK13646  156 IVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDenKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKEL 233
SapF COG4167
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
482-688 5.92e-21

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


Pssm-ID: 443328 [Multi-domain]  Cd Length: 265  Bit Score: 93.36  E-value: 5.92e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 482 VSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAG------------QNIR----DVGlESL--RKAVGvvp 543
Cdd:COG4167    32 VSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGhkleygdykyrcKHIRmifqDPN-TSLnpRLNIG--- 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 544 Q--DAVLFHNTifyNLmygNINATAEDVYRVARLAGIH-DAILKMPHKydtqvgerglkLSGGEKQRVAIARAILKNPPI 620
Cdd:COG4167   108 QilEEPLRLNT---DL---TAEEREERIFATLRLVGLLpEHANFYPHM-----------LSSGQKQRVALARALILQPKI 170

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2569209806 621 LLYDEATSSLDSVTEENILTSMKEMVKDR--TSVFIAHRLStIVD--ADEIIVLNQGKVAERGNHQTLLDTP 688
Cdd:COG4167   171 IIADEALAALDMSVRSQIINLMLELQEKLgiSYIYVSQHLG-IVKhiSDKVLVMHQGEVVEYGKTAEVFANP 241
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
 479-675 6.65e-21

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 96.63  E-value: 6.65e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 479 LNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQ--NIRDVGlESLRKAVGVVPQDAVLFHN-TIFY 555
Cdd:COG3845    21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKpvRIRSPR-DAIALGIGMVHQHFMLVPNlTVAE 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 556 NLMYGninatAEDV-YRVARLAGIHDAILKMPHKY------DTQVGErglkLSGGEKQRVAIARAILKNPPILLYDEATS 628
Cdd:COG3845   100 NIVLG-----LEPTkGGRLDRKAARARIRELSERYgldvdpDAKVED----LSVGEQQRVEILKALYRGARILILDEPTA 170

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2569209806 629 SLdsvTE---ENILTSMKEMVKDRTSV-FIAHRLSTIVD-ADEIIVLNQGKV 675
Cdd:COG3845   171 VL---TPqeaDELFEILRRLAAEGKSIiFITHKLREVMAiADRVTVLRRGKV 219
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
 477-676 1.12e-20

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: 91.56  E-value: 1.12e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 477 KVLNGVSFEVPAGKKVAIVGGSGSGKST----IVRLLfRFYEPQQGNIYIAGQNIRDvglESLRKAVGVVPQ-DAVLFHN 551
Cdd:cd03234    21 RILNDVSLHVESGQVMAILGSSGSGKTTlldaISGRV-EGGGTTSGQILFNGQPRKP---DQFQKCVAYVRQdDILLPGL 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 552 TIFYNLMYGNINATAE---DVYRVARlagihDAILKMPHKYDTQVGERGLK-LSGGEKQRVAIARAILKNPPILLYDEAT 627
Cdd:cd03234    97 TVRETLTYTAILRLPRkssDAIRKKR-----VEDVLLRDLALTRIGGNLVKgISGGERRRVSIAVQLLWDPKVLILDEPT 171

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2569209806 628 SSLDSVTEENILTSMKEM-VKDRTSVFIAHR-LSTIVDA-DEIIVLNQGKVA 676
Cdd:cd03234   172 SGLDSFTALNLVSTLSQLaRRNRIVILTIHQpRSDLFRLfDRILLLSSGEIV 223
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
 472-658 1.12e-20

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 92.15  E-value: 1.12e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 472 YLEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYE--PQ---QGNIYIAGQNI--RDVGLESLRKAVGVVPQ 544
Cdd:PRK14239   14 YYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnPEvtiTGSIVYNGHNIysPRTDTVDLRKEIGMVFQ 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 545 DAVLFHNTIFYNLMYGninataedvyrvARLAGIHDAilkmpHKYDTQVgERGLK------------------LSGGEKQ 606
Cdd:PRK14239   94 QPNPFPMSIYENVVYG------------LRLKGIKDK-----QVLDEAV-EKSLKgasiwdevkdrlhdsalgLSGGQQQ 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2569209806 607 RVAIARAILKNPPILLYDEATSSLDSVTEENILTSMKEMVKDRTSVFIAHRL 658
Cdd:PRK14239  156 RVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSM 207
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
 475-693 1.26e-20

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 94.91  E-value: 1.26e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 475 GQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGLESLRKAVGVVPQDAVLfhntif 554
Cdd:PRK09536   15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSL------ 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 555 ynlmygNINATAEDVYRVARLAgiHDAILKMPHKYDTQVGERGLK--------------LSGGEKQRVAIARAILKNPPI 620
Cdd:PRK09536   89 ------SFEFDVRQVVEMGRTP--HRSRFDTWTETDRAAVERAMErtgvaqfadrpvtsLSGGERQRVLLARALAQATPV 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2569209806 621 LLYDEATSSLDSVTEENILTSMKEMVKD-RTSVFIAHRLSTIVD-ADEIIVLNQGKVAERGNHQTLLdTPGSLYA 693
Cdd:PRK09536  161 LLLDEPTASLDINHQVRTLELVRRLVDDgKTAVAAIHDLDLAARyCDELVLLADGRVRAAGPPADVL-TADTLRA 234
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
 479-691 2.10e-20

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: 90.51  E-value: 2.10e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 479 LNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNI-RDVGleSLRKAVGVVPQDAVL------FHN 551
Cdd:cd03265    16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVvREPR--EVRRRIGIVFQDLSVddeltgWEN 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 552 TIFYNLMYGNINATA-EDVYRVARLAGIHDAILKMPHKYdtqvgerglklSGGEKQRVAIARAILKNPPILLYDEATSSL 630
Cdd:cd03265    94 LYIHARLYGVPGAERrERIDELLDFVGLLEAADRLVKTY-----------SGGMRRRLEIARSLVHRPEVLFLDEPTIGL 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2569209806 631 DSVTEENILTSMKEMVKDR-TSVFI-------AHRLstivdADEIIVLNQGKVAERGnhqtlldTPGSL 691
Cdd:cd03265   163 DPQTRAHVWEYIEKLKEEFgMTILLtthymeeAEQL-----CDRVAIIDHGRIIAEG-------TPEEL 219
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
 460-688 3.55e-20

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 90.88  E-value: 3.55e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 460 EATIRFEDVY-----FEYLEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYE------PQQGNIYIAGQNIR 528
Cdd:PRK14246    2 EAGKSAEDVFnisrlYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 529 DVGLESLRKAVGVVPQDAVLF-HNTIFYNLMYGNINATAEDVYRVARLagIHDAILKM---PHKYDtQVGERGLKLSGGE 604
Cdd:PRK14246   82 QIDAIKLRKEVGMVFQQPNPFpHLSIYDNIAYPLKSHGIKEKREIKKI--VEECLRKVglwKEVYD-RLNSPASQLSGGQ 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 605 KQRVAIARAILKNPPILLYDEATSSLDSVTEENILTSMKEMVKDRTSVFIAHRLSTIVD-ADEIIVLNQGKVAERGNHQT 683
Cdd:PRK14246  159 QQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNE 238


                  ....*
gi 2569209806 684 LLDTP 688
Cdd:PRK14246  239 IFTSP 243
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
 477-675 3.79e-20

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


Pssm-ID: 213236 [Multi-domain]  Cd Length: 210  Bit Score: 89.26  E-value: 3.79e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 477 KVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGleslRKAVGVVPQDAVLFHN-TIFY 555
Cdd:cd03269    14 TALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIGYLPEERGLYPKmKVID 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 556 NLMYgninataedvyrVARLAG--IHDAI---------LKMPHKYDTQVGErglkLSGGEKQRVAIARAILKNPPILLYD 624
Cdd:cd03269    90 QLVY------------LAQLKGlkKEEARrridewlerLELSEYANKRVEE----LSKGNQQKVQFIAAVIHDPELLILD 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2569209806 625 EATSSLDSVTEENILTSMKEMV-KDRTSVFIAHRLSTIVD-ADEIIVLNQGKV 675
Cdd:cd03269   154 EPFSGLDPVNVELLKDVIRELArAGKTVILSTHQMELVEElCDRVLLLNKGRA 206
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
474-693 5.84e-20

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 92.59  E-value: 5.84e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 474 EGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVglESLRKAVGVVPQDAVLF-HNT 552
Cdd:PRK11607   30 DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHV--PPYQRPINMMFQSYALFpHMT 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 553 IFYNLMYG---NINATAEDVYRVAR-LAGIH--DAILKMPHkydtqvgerglKLSGGEKQRVAIARAILKNPPILLYDEA 626
Cdd:PRK11607  108 VEQNIAFGlkqDKLPKAEIASRVNEmLGLVHmqEFAKRKPH-----------QLSGGQRQRVALARSLAKRPKLLLLDEP 176

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2569209806 627 TSSLDSVTEENiltsMKEMVKD------RTSVFIAH-RLSTIVDADEIIVLNQGKVAERGNHQTLLDTPGSLYA 693
Cdd:PRK11607  177 MGALDKKLRDR----MQLEVVDilervgVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYS 246
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
459-683 6.14e-20

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 90.33  E-value: 6.14e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 459 QEATIRFEDVYFEYLEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRdvglESLRKA 538
Cdd:PRK15056    3 QQAGIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR----QALQKN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 539 -VGVVPQD-------AVLFHNTIFYNlMYGNIN----ATAEDVYRV-ARLAGIHdaILKMPHKydtQVGErglkLSGGEK 605
Cdd:PRK15056   79 lVAYVPQSeevdwsfPVLVEDVVMMG-RYGHMGwlrrAKKRDRQIVtAALARVD--MVEFRHR---QIGE----LSGGQK 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2569209806 606 QRVAIARAILKNPPILLYDEATSSLDSVTEENILTSMKEMVKD-RTSVFIAHRLSTIVDADEIIVLNQGKVAERGNHQT 683
Cdd:PRK15056  149 KRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEgKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTET 227
cbiO PRK13645
energy-coupling factor transporter ATPase;
470-703 7.83e-20

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 90.45  E-value: 7.83e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 470 FEYlegqKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNI----YIAGQNIRDVG-LESLRKAVGVVPQ 544
Cdd:PRK13645   22 FEF----KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTivgdYAIPANLKKIKeVKRLRKEIGLVFQ 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 545 --DAVLFHNTIFYNLMYGNIN--ATAEDVYRvaRLAGIHDaILKMPHKYdtqVGERGLKLSGGEKQRVAIARAILKNPPI 620
Cdd:PRK13645   98 fpEYQLFQETIEKDIAFGPVNlgENKQEAYK--KVPELLK-LVQLPEDY---VKRSPFELSGGQKRRVALAGIIAMDGNT 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 621 LLYDEATSSLDSVTEENILTSMKEMVKD--RTSVFIAHRLSTIVD-ADEIIVLNQGKVAERG------NHQTLLDT---- 687
Cdd:PRK13645  172 LVLDEPTGGLDPKGEEDFINLFERLNKEykKRIIMVTHNMDQVLRiADEVIVMHEGKVISIGspfeifSNQELLTKieid 251

                         250
                  ....*....|....*.
gi 2569209806 688 PGSLYANLWNTQNSRI 703
Cdd:PRK13645  252 PPKLYQLMYKLKNKGI 267
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
 476-714 8.91e-20

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 93.62  E-value: 8.91e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 476 QKVLNGVSFEVPAGKKVAIVGGSGSGKS----TIVRLLfrfyePQ------QGNIYIAGQNIRDVGLESLRKAVGvvPQD 545
Cdd:PRK15134   22 RTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLL-----PSppvvypSGDIRFHGESLLHASEQTLRGVRG--NKI 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 546 AVLFH---------NTIFYNL---------MYGNInATAEDVYRVARLaGIHDAILKM---PHKydtqvgerglkLSGGE 604
Cdd:PRK15134   95 AMIFQepmvslnplHTLEKQLyevlslhrgMRREA-ARGEILNCLDRV-GIRQAAKRLtdyPHQ-----------LSGGE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 605 KQRVAIARAILKNPPILLYDEATSSLDSVTEENILTSMKEMVK--DRTSVFIAHRLStIVD--ADEIIVLNQGKVAERGN 680
Cdd:PRK15134  162 RQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLS-IVRklADRVAVMQNGRCVEQNR 240

                         250       260       270
                  ....*....|....*....|....*....|....
gi 2569209806 681 HQTLLDTPGSLYanlwnTQnsRILSNGSKPEPVP 714
Cdd:PRK15134  241 AATLFSAPTHPY-----TQ--KLLNSEPSGDPVP 267
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
 479-679 1.06e-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: 88.68  E-value: 1.06e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 479 LNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGleslrkavgvvPQDAVLFHNtifYNLM 558
Cdd:TIGR01184   1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPG-----------PDRMVVFQN---YSLL 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 559 -----YGNI----NATAEDVYRVARLAGI--HDAILKMPHKYDTQVGErglkLSGGEKQRVAIARAILKNPPILLYDEAT 627
Cdd:TIGR01184  67 pwltvRENIalavDRVLPDLSKSERRAIVeeHIALVGLTEAADKRPGQ----LSGGMKQRVAIARALSIRPKVLLLDEPF 142

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2569209806 628 SSLDSVTEENILTSMKEMVKDR--TSVFIAHRL-STIVDADEIIVLNQGKVAERG 679
Cdd:TIGR01184 143 GALDALTRGNLQEELMQIWEEHrvTVLMVTHDVdEALLLSDRVVMLTNGPAANIG 197
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
 473-673 1.61e-19

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: 94.21  E-value: 1.61e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806  473 LEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQnirdvgleslrkaVGVVPQDAVLFHNT 552
Cdd:TIGR01271  436 LYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQTSWIMPGT 502

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806  553 IFYNLMYGninaTAEDVYR---VARLAGIHDAILKMPHKYDTQVGERGLKLSGGEKQRVAIARAILKNPPILLYDEATSS 629
Cdd:TIGR01271  503 IKDNIIFG----LSYDEYRytsVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTH 578

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 2569209806  630 LDSVTEENILTS-MKEMVKDRTSVFIAHRLSTIVDADEIIVLNQG 673
Cdd:TIGR01271  579 LDVVTEKEIFEScLCKLMSNKTRILVTSKLEHLKKADKILLLHEG 623
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
477-675 1.93e-19

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 92.86  E-value: 1.93e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 477 KVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGLESL----RKAVGVVPQD-AVLFHN 551
Cdd:PRK10535   22 EVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrREHFGFIFQRyHLLSHL 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 552 TIFYNLMYGNINATAEdvyRVARLAGIHDAILKMphKYDTQVGERGLKLSGGEKQRVAIARAILKNPPILLYDEATSSLD 631
Cdd:PRK10535  102 TAAQNVEVPAVYAGLE---RKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALD 176

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2569209806 632 SVTEENILTSMKEMvKDR--TSVFIAHRLSTIVDADEIIVLNQGKV 675
Cdd:PRK10535  177 SHSGEEVMAILHQL-RDRghTVIIVTHDPQVAAQAERVIEIRDGEI 221
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
 479-679 2.05e-19

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


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 92.80  E-value: 2.05e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 479 LNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLfRFYEPQ----QGNIYIAGqniRDVGLESLRKAVGVVPQDAVLF-HNTI 553
Cdd:TIGR00955  41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNAL-AFRSPKgvkgSGSVLLNG---MPIDAKEMRAISAYVQQDDLFIpTLTV 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 554 FYNLMYGNINATAEDVYRVARLAGIHDAILKMPHK--YDTQVGERGLK--LSGGEKQRVAIARAILKNPPILLYDEATSS 629
Cdd:TIGR00955 117 REHLMFQAHLRMPRRVTKKEKRERVDEVLQALGLRkcANTRIGVPGRVkgLSGGERKRLAFASELLTDPPLLFCDEPTSG 196

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2569209806 630 LDSVTEENILTSMKEMV-KDRTSVFIAHR-LSTIVDA-DEIIVLNQGKVAERG 679
Cdd:TIGR00955 197 LDSFMAYSVVQVLKGLAqKGKTIICTIHQpSSELFELfDKIILMAEGRVAYLG 249
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
 465-631 3.28e-19

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 91.66  E-value: 3.28e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 465 FEDVYFEYlEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGqNIRdvgleslrkaVGVVPQ 544
Cdd:COG0488     1 LENLSKSF-GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-GLR----------IGYLPQ 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 545 DAVLF-HNTIF----------------YNLMYGNINATAEDVYRVARLAGIHDAI---------------LKMPHK-YDT 591
Cdd:COG0488    69 EPPLDdDLTVLdtvldgdaelraleaeLEELEAKLAEPDEDLERLAELQEEFEALggweaearaeeilsgLGFPEEdLDR 148

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2569209806 592 QVGErglkLSGGEKQRVAIARAILKNPPILLYDEATSSLD 631
Cdd:COG0488   149 PVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLD 184
PRK10522 PRK10522
multidrug transporter membrane component/ATP-binding component; Provisional
 375-677 7.09e-19

multidrug transporter membrane component/ATP-binding component; Provisional


Pssm-ID: 236707 [Multi-domain]  Cd Length: 547  Bit Score: 90.80  E-value: 7.09e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 375 IFSVGLTAIMVLASKGIMsgtmtvgdLVMVNGLLFQ-------LSLPLNFLgtvyretRQALIDM-NTLFTLLSVDT--- 443
Cdd:PRK10522  233 LSAVNWSNIMMLGAIGLV--------FYMANSLGWAdtnvaatYSLTLLFL-------RTPLLSAvGALPTLLSAQVafn 297

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 444 KIKEKEMAP--PLIVTPQEA----TIRFEDVYFEYLEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQ 517
Cdd:PRK10522  298 KLNKLALAPykAEFPRPQAFpdwqTLELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQS 377

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 518 GNIYIAGQNIRDVGLESLRKAVGVVPQDAVLFHNTIfynlmyGNINATAEDvyrvaRLAGIHDAILKMPHKYDTQVGE-R 596
Cdd:PRK10522  378 GEILLDGKPVTAEQPEDYRKLFSAVFTDFHLFDQLL------GPEGKPANP-----ALVEKWLERLKMAHKLELEDGRiS 446

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 597 GLKLSGGEKQRVAIARAILKNPPILLYDEATSSLD----SVTEENILTSMKEMVKdrTSVFIAHRLSTIVDADEIIVLNQ 672
Cdd:PRK10522  447 NLKLSKGQKKRLALLLALAEERDILLLDEWAADQDphfrREFYQVLLPLLQEMGK--TIFAISHDDHYFIHADRLLEMRN 524


                  ....*
gi 2569209806 673 GKVAE 677
Cdd:PRK10522  525 GQLSE 529
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
 478-680 9.79e-19

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


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 86.29  E-value: 9.79e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 478 VLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGqniRDVGLESLrkAVGvvpqdavlFH------- 550
Cdd:COG1134    41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG---RVSALLEL--GAG--------FHpeltgre 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 551 NTIFYNLMYGNINATAEDVYR-VARLAGIHDAIlkmphkyDTQVGerglKLSGGEKQRVAIARAILKNPPILLYDEATSS 629
Cdd:COG1134   108 NIYLNGRLLGLSRKEIDEKFDeIVEFAELGDFI-------DQPVK----TYSSGMRARLAFAVATAVDPDILLVDEVLAV 176

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2569209806 630 LDSVTEENILTSMKEMVKD-RTSVFIAHRLSTIVD-ADEIIVLNQGKVAERGN 680
Cdd:COG1134   177 GDAAFQKKCLARIRELRESgRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGD 229
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
 475-675 1.02e-18

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 86.66  E-value: 1.02e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 475 GQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIyIAGQnirdVGLESLRKAVGVVPQDAVLFH-NTI 553
Cdd:PRK11247   24 ERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGT----APLAEAREDTRLMFQDARLLPwKKV 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 554 FYNL---MYGNINATAEDVYRVARLAgihdailkmphkydTQVGERGLKLSGGEKQRVAIARAILKNPPILLYDEATSSL 630
Cdd:PRK11247   99 IDNVglgLKGQWRDAALQALAAVGLA--------------DRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGAL 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2569209806 631 DSVTEenilTSMKEMVKDR------TSVFIAHRLSTIVD-ADEIIVLNQGKV 675
Cdd:PRK11247  165 DALTR----IEMQDLIESLwqqhgfTVLLVTHDVSEAVAmADRVLLIEEGKI 212
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
 463-674 1.28e-18

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: 82.88  E-value: 1.28e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 463 IRFEDVYFEYlEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGnIYIAGQNIRdvgleslrkaVGVV 542
Cdd:cd03221     1 IELENLSKTY-GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEG-IVTWGSTVK----------IGYF 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 543 PQdavlfhntifynlmygninataedvyrvarlagihdailkmphkydtqvgerglkLSGGEKQRVAIARAILKNPPILL 622
Cdd:cd03221    69 EQ-------------------------------------------------------LSGGEKMRLALAKLLLENPNLLL 93

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2569209806 623 YDEATSSLDSVTeeniLTSMKEMVKD--RTSVFIAH-R--LSTIvdADEIIVLNQGK 674
Cdd:cd03221    94 LDEPTNHLDLES----IEALEEALKEypGTVILVSHdRyfLDQV--ATKIIELEDGK 144
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
461-694 1.49e-18

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


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 87.98  E-value: 1.49e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 461 ATIRFEDVYFEYLEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDvgLESLRKAVG 540
Cdd:PRK11650    2 AGLKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNE--LEPADRDIA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 541 VVPQDAVLF-HNTIFYNLMYGNINA---TAEDVYRVARLAGIhdaiLKMPHKYDtqvgERGLKLSGGEKQRVAIARAILK 616
Cdd:PRK11650   80 MVFQNYALYpHMSVRENMAYGLKIRgmpKAEIEERVAEAARI----LELEPLLD----RKPRELSGGQRQRVAMGRAIVR 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 617 NPPILLYDEATSSLDSvteeniltsmKEMVKDR------------TSVFIAH-RLSTIVDADEIIVLNQGKVAERGnhqt 683
Cdd:PRK11650  152 EPAVFLFDEPLSNLDA----------KLRVQMRleiqrlhrrlktTSLYVTHdQVEAMTLADRVVVMNGGVAEQIG---- 217

                         250
                  ....*....|.
gi 2569209806 684 lldTPGSLYAN 694
Cdd:PRK11650  218 ---TPVEVYEK 225
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
 478-679 1.58e-18

ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.


Pssm-ID: 213187 [Multi-domain]  Cd Length: 224  Bit Score: 84.89  E-value: 1.58e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 478 VLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGqniRDVGLesLRKAVGVVPqDAVLFHNTIFYNL 557
Cdd:cd03220    37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG---RVSSL--LGLGGGFNP-ELTGRENIYLNGR 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 558 MYGNINATAEDVY-RVARLAGIHDAIlkmphkyDTQVGErglkLSGGEKQRVAIARAILKNPPILLYDEATSSLDSVTEE 636
Cdd:cd03220   111 LLGLSRKEIDEKIdEIIEFSELGDFI-------DLPVKT----YSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQE 179

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2569209806 637 NILTSMKEMVKDRTSVFIA-HRLSTIVD-ADEIIVLNQGKVAERG 679
Cdd:cd03220   180 KCQRRLRELLKQGKTVILVsHDPSSIKRlCDRALVLEKGKIRFDG 224
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
460-687 1.66e-18

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 86.78  E-value: 1.66e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 460 EATIRFEDVYFEYLEgQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGLESlRKAV 539
Cdd:PRK13537    5 VAPIDFRNVEKRYGD-KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA-RQRV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 540 GVVPQ------DAVLFHNTIFYNLMYGNINATAEdvyrvARLAGIHDaILKMPHKYDTQVGErglkLSGGEKQRVAIARA 613
Cdd:PRK13537   83 GVVPQfdnldpDFTVRENLLVFGRYFGLSAAAAR-----ALVPPLLE-FAKLENKADAKVGE----LSGGMKRRLTLARA 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 614 ILKNPPILLYDEATSSLDSVTEENILTSMKEMVKDRTSVFI-------AHRLstivdADEIIVLNQG-KVAErGNHQTLL 685
Cdd:PRK13537  153 LVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLtthfmeeAERL-----CDRLCVIEEGrKIAE-GAPHALI 226


                  ..
gi 2569209806 686 DT 687
Cdd:PRK13537  227 ES 228
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
476-679 2.15e-18

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 85.45  E-value: 2.15e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 476 QKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGLESLRKAVGVVPQ-----DAVLFH 550
Cdd:PRK11231   15 KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQhhltpEGITVR 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 551 NTIFY-----NLMYGNInaTAEDVYRVARlagihdailKMPHKYDTQVGERGL-KLSGGEKQRVAIARAILKNPPILLYD 624
Cdd:PRK11231   95 ELVAYgrspwLSLWGRL--SAEDNARVNQ---------AMEQTRINHLADRRLtDLSGGQRQRAFLAMVLAQDTPVVLLD 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2569209806 625 EATSSLDSVTEENILTSMKEM-VKDRTSVFIAHRLSTIVD-ADEIIVLNQGKVAERG 679
Cdd:PRK11231  164 EPTTYLDINHQVELMRLMRELnTQGKTVVTVLHDLNQASRyCDHLVVLANGHVMAQG 220
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
482-679 2.30e-18

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 87.39  E-value: 2.30e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 482 VSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVglESLRKAVGVVPQDAVLF-HNTIFYNLMYG 560
Cdd:PRK11000   22 INLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDV--PPAERGVGMVFQSYALYpHLSVAENMSFG 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 561 NINATA---EDVYRVARLAgihdAILKMPHKYDTQVGErglkLSGGEKQRVAIARAILKNPPILLYDEATSSLDSVTEEN 637
Cdd:PRK11000  100 LKLAGAkkeEINQRVNQVA----EVLQLAHLLDRKPKA----LSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQ 171

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2569209806 638 ILTSMKEMVK--DRTSVFIAH-RLSTIVDADEIIVLNQGKVAERG 679
Cdd:PRK11000  172 MRIEISRLHKrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVG 216
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
472-659 2.60e-18

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 84.87  E-value: 2.60e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 472 YLEGQ---KVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDvgLESLRKA------VGVV 542
Cdd:PRK11629   15 YQEGSvqtDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSK--LSSAAKAelrnqkLGFI 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 543 PQdavlFHN-----TIFYN----LMYGNINAtaedvyrvarlAGIHDAILKMPHK--YDTQVGERGLKLSGGEKQRVAIA 611
Cdd:PRK11629   93 YQ----FHHllpdfTALENvampLLIGKKKP-----------AEINSRALEMLAAvgLEHRANHRPSELSGGERQRVAIA 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2569209806 612 RAILKNPPILLYDEATSSLDSVTEENILTSMKEMVKDRTSVF--------IAHRLS 659
Cdd:PRK11629  158 RALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFlvvthdlqLAKRMS 213
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
 463-680 2.60e-18

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


Pssm-ID: 132313 [Multi-domain]  Cd Length: 520  Bit Score: 88.71  E-value: 2.60e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 463 IRFEDVYFEYlEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLL--FRFYEPQQGNI-----------YI-----AG 524
Cdd:TIGR03269   1 IEVKNLTKKF-DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIiyhvalcekcgYVerpskVG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 525 QNIR---------DVGLESLRKAV--GVVPQDAVLFHNTIfynLMYGN-------INATAEDVYRVARLAGIHDAILKMp 586
Cdd:TIGR03269  80 EPCPvcggtlepeEVDFWNLSDKLrrRIRKRIAIMLQRTF---ALYGDdtvldnvLEALEEIGYEGKEAVGRAVDLIEM- 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 587 hkydTQVGER----GLKLSGGEKQRVAIARAILKNPPILLYDEATSSLDSVTEENILTSMKEMVKDR--TSVFIAHRLST 660
Cdd:TIGR03269 156 ----VQLSHRithiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgiSMVLTSHWPEV 231

                         250       260
                  ....*....|....*....|.
gi 2569209806 661 IVD-ADEIIVLNQGKVAERGN 680
Cdd:TIGR03269 232 IEDlSDKAIWLENGEIKEEGT 252
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
 475-688 3.32e-18

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 85.53  E-value: 3.32e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 475 GQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEP-----QQGNIYIAGQNI---RDVgLEsLRKAVGVVPQDA 546
Cdd:PRK14271   33 GKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIfnyRDV-LE-FRRRVGMLFQRP 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 547 VLFHNTIFYNLMYGninATAEDVYRVARLAGIHDAILKMPHKYDT---QVGERGLKLSGGEKQRVAIARAILKNPPILLY 623
Cdd:PRK14271  111 NPFPMSIMDNVLAG---VRAHKLVPRKEFRGVAQARLTEVGLWDAvkdRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLL 187

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2569209806 624 DEATSSLDSVTEENILTSMKEMVKDRTSVFIAHRLSTIVD-ADEIIVLNQGKVAERGNHQTLLDTP 688
Cdd:PRK14271  188 DEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLFSSP 253
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
 473-675 3.56e-18

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


Pssm-ID: 213182 [Multi-domain]  Cd Length: 182  Bit Score: 82.87  E-value: 3.56e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 473 LEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNI-RDVGLESLRKAVGVVPQD---AVL 548
Cdd:cd03215    10 LSVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVtRRSPRDAIRAGIAYVPEDrkrEGL 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 549 FHN-TIFYNLMYGNInataedvyrvarlagihdailkmphkydtqvgerglkLSGGEKQRVAIARAILKNPPILLYDEAT 627
Cdd:cd03215    90 VLDlSVAENIALSSL-------------------------------------LSGGNQQKVVLARWLARDPRVLILDEPT 132

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2569209806 628 SSLDSVTEENILTSMKEMVKDRTSVFIahrLSTIVD-----ADEIIVLNQGKV 675
Cdd:cd03215   133 RGVDVGAKAEIYRLIRELADAGKAVLL---ISSELDellglCDRILVMYEGRI 182
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
466-678 4.12e-18

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 84.75  E-value: 4.12e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 466 EDVYFEYlEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGLESlrkavGVVPQ- 544
Cdd:PRK11248    5 SHLYADY-GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER-----GVVFQn 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 545 DAVLFHNTIFYNLMYGninataedvyrvARLAGI-----HDAILKMPHKYDTQ-VGERGL-KLSGGEKQRVAIARAILKN 617
Cdd:PRK11248   79 EGLLPWRNVQDNVAFG------------LQLAGVekmqrLEIAHQMLKKVGLEgAEKRYIwQLSGGQRQRVGIARALAAN 146

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2569209806 618 PPILLYDEATSSLDSVTEENILTSMKEMVKD-RTSVF-IAHRLSTIV-DADEIIVL--NQGKVAER 678
Cdd:PRK11248  147 PQLLLLDEPFGALDAFTREQMQTLLLKLWQEtGKQVLlITHDIEEAVfMATELVLLspGPGRVVER 212
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
 463-687 4.14e-18

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 85.91  E-value: 4.14e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 463 IRFEDVYFEYLEGQ----KVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRD--------V 530
Cdd:PRK13651    3 IKVKNIVKIFNKKLptelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNkkktkekeK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 531 GLES----------------LRKAVGVVPQDA--VLFHNTIFYNLMYGNIN--ATAEDVYRVARlagihdailkmphKYD 590
Cdd:PRK13651   83 VLEKlviqktrfkkikkikeIRRRVGVVFQFAeyQLFEQTIEKDIIFGPVSmgVSKEEAKKRAA-------------KYI 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 591 TQVG--ERGLK-----LSGGEKQRVAIARAILKNPPILLYDEATSSLDSVTEENILTSMKEMVKD-RTSVFIAHRLSTIV 662
Cdd:PRK13651  150 ELVGldESYLQrspfeLSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQgKTIILVTHDLDNVL 229

                         250       260
                  ....*....|....*....|....*..
gi 2569209806 663 D-ADEIIVLNQGKVAERGN-HQTLLDT 687
Cdd:PRK13651  230 EwTKRTIFFKDGKIIKDGDtYDILSDN 256
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
 472-688 4.18e-18

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 84.51  E-value: 4.18e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 472 YLEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQ-----GNIYIAGQNI--RDVGLESLRKAVGVVPQ 544
Cdd:PRK14267   13 YYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearveGEVRLFGRNIysPDVDPIEVRREVGMVFQ 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 545 DAVLF-HNTIFYN----LMYGNINATAEDVYRVARLAgihdaiLKMPHKYD---TQVGERGLKLSGGEKQRVAIARAILK 616
Cdd:PRK14267   93 YPNPFpHLTIYDNvaigVKLNGLVKSKKELDERVEWA------LKKAALWDevkDRLNDYPSNLSGGQRQRLVIARALAM 166

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2569209806 617 NPPILLYDEATSSLDSVTEENILTSMKEMVKDRTSVFIAHRLSTIVD-ADEIIVLNQGKVAERGNHQTLLDTP 688
Cdd:PRK14267  167 KPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARvSDYVAFLYLGKLIEVGPTRKVFENP 239
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
 436-692 4.97e-18

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 88.37  E-value: 4.97e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 436 FTLLSVDTKIKEKEMAPPLIVTPQEATIRFEDVYFEYLEGQKVLNGVSFEVPA----------GKKVAIVGGSGSGKSTI 505
Cdd:PRK10261  287 FPLISLEHPAKQEPPIEQDTVVDGEPILQVRNLVTRFPLRSGLLNRVTREVHAvekvsfdlwpGETLSLVGESGSGKSTT 366

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 506 VRLLFRFYEPQQGNIYIAGQNI---RDVGLESLRKAVGVVPQD--AVLF-HNTIFYNLM-----YGNINATAEdVYRVA- 573
Cdd:PRK10261  367 GRALLRLVESQGGEIIFNGQRIdtlSPGKLQALRRDIQFIFQDpyASLDpRQTVGDSIMeplrvHGLLPGKAA-AARVAw 445

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 574 ---RLAGIHDAILKMPHKYdtqvgerglklSGGEKQRVAIARAILKNPPILLYDEATSSLDSVTEENILTSMKEMVKDR- 649
Cdd:PRK10261  446 lleRVGLLPEHAWRYPHEF-----------SGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFg 514

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2569209806 650 -TSVFIAHRLSTIVD-ADEIIVLNQGKVAERGNHQTLLDTPGSLY 692
Cdd:PRK10261  515 iAYLFISHDMAVVERiSHRVAVMYLGQIVEIGPRRAVFENPQHPY 559
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
463-686 6.22e-18

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 85.65  E-value: 6.22e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 463 IRFEDVYFEYlEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGlESLRKAVGVV 542
Cdd:PRK13536   42 IDLAGVSKSY-GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARA-RLARARIGVV 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 543 PQ-DAVLFHNTIFYNLM-YG--------NINATAEDVYRVARLAgihdailkmpHKYDTQVGErglkLSGGEKQRVAIAR 612
Cdd:PRK13536  120 PQfDNLDLEFTVRENLLvFGryfgmstrEIEAVIPSLLEFARLE----------SKADARVSD----LSGGMKRRLTLAR 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 613 AILKNPPILLYDEATSSLDSVTEENILTSMKEMV-KDRTSVFIAH------RLstivdADEIIVLNQG-KVAErGNHQTL 684
Cdd:PRK13536  186 ALINDPQLLILDEPTTGLDPHARHLIWERLRSLLaRGKTILLTTHfmeeaeRL-----CDRLCVLEAGrKIAE-GRPHAL 259


                  ..
gi 2569209806 685 LD 686
Cdd:PRK13536  260 ID 261
PvdE COG4615
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...
 176-684 1.55e-17

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: 86.39  E-value: 1.55e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 176 VVTMATAVLIGYGVSRTGSALFNELRNAVFGKVAQSSIRRIAKnvflhlhnldLGFHlsRQTGALSKAIDrgtrgisfVL 255
Cdd:COG4615    59 VLLLLSRLASQLLLTRLGQHAVARLRLRLSRRILAAPLERLER----------IGAA--RLLAALTEDVR--------TI 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 256 SALVFNLGPTLFEMMLVSGILYYkcgghfalvtLGTLS--------AYTAFTVAVTQWRTQfRIE--MNKA-DNEAG-NA 323
Cdd:COG4615   119 SQAFVRLPELLQSVALVLGCLAY----------LAWLSpplflltlVLLGLGVAGYRLLVR-RARrhLRRArEAEDRlFK 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 324 AIDSL--------LNYETVKYFNNEKYE--AERYdgflkvyESSSLKTTSTLAML-NFGQSAIFSV-GLTAIMVL----A 387
Cdd:COG4615   188 HFRALlegfkelkLNRRRRRAFFDEDLQptAERY-------RDLRIRADTIFALAnNWGNLLFFALiGLILFLLPalgwA 260

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 388 SKGIMSGTMTVgdlvmvngLLFqLSLPL-NFLGTV--YRETRQALIDMNTLFTLLSVDTKIKEKEMAPPLIVTPQeaTIR 464
Cdd:COG4615   261 DPAVLSGFVLV--------LLF-LRGPLsQLVGALptLSRANVALRKIEELELALAAAEPAAADAAAPPAPADFQ--TLE 329

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 465 FEDVYFEYLEGQK----VLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGLESLRKAVG 540
Cdd:COG4615   330 LRGVTYRYPGEDGdegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFS 409

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 541 VVPQDAVLFHNtiFYNLmygninATAEDVYRVARLagIHDaiLKMPHKydTQVgERG----LKLSGGEKQRVAIARAILK 616
Cdd:COG4615   410 AVFSDFHLFDR--LLGL------DGEADPARAREL--LER--LELDHK--VSV-EDGrfstTDLSQGQRKRLALLVALLE 474

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 617 NPPILLYDEATSSLDSV------TEenILTSMKEMVKdrTSVFIAHrlstivD------ADEIIVLNQGKVAERGNHQTL 684
Cdd:COG4615   475 DRPILVFDEWAADQDPEfrrvfyTE--LLPELKARGK--TVIAISH------DdryfdlADRVLKMDYGKLVELTGPAAL 544
TauB COG4525
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
461-678 1.57e-17

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


Pssm-ID: 443596 [Multi-domain]  Cd Length: 262  Bit Score: 82.99  E-value: 1.57e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 461 ATIRFEDVYFEY---LEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGLEslRk 537
Cdd:COG4525     2 SMLTVRHVSVRYpggGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGAD--R- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 538 avGVVPQ-DAVLFHNTIFYNLMYGninataedvyrvARLAGI-HDAILKMPHKYDTQVGERGL------KLSGGEKQRVA 609
Cdd:COG4525    79 --GVVFQkDALLPWLNVLDNVAFG------------LRLRGVpKAERRARAEELLALVGLADFarrriwQLSGGMRQRVG 144

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2569209806 610 IARAILKNPPILLYDEATSSLDSVTEEniltSMKEM---VKDRTSV---FIAHRL-STIVDADEIIVL--NQGKVAER 678
Cdd:COG4525   145 IARALAADPRFLLMDEPFGALDALTRE----QMQELlldVWQRTGKgvfLITHSVeEALFLATRLVVMspGPGRIVER 218
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
 463-677 1.72e-17

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 86.27  E-value: 1.72e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 463 IRFEDVYFEYlEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIaGQNIRdvgleslrkaVGVV 542
Cdd:COG0488   316 LELEGLSKSY-GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK----------IGYF 383

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 543 PQDAVLFH--NTIFYNLMYGNINATaeDVYRVARLAgihdAILKMPHKYDTQVGerglKLSGGEKQRVAIARAILKNPPI 620
Cdd:COG0488   384 DQHQEELDpdKTVLDELRDGAPGGT--EQEVRGYLG----RFLFSGDDAFKPVG----VLSGGEKARLALAKLLLSPPNV 453

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2569209806 621 LLYDEATSSLDSVTeeniLTSMKEMVKD--RTSVFIAH-R--LSTIvdADEIIVLNQGKVAE 677
Cdd:COG0488   454 LLLDEPTNHLDIET----LEALEEALDDfpGTVLLVSHdRyfLDRV--ATRILEFEDGGVRE 509
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 475-680 3.07e-17

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


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 82.85  E-value: 3.07e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 475 GQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDvgleSLRKAVGVVPQDAVLfhntif 554
Cdd:COG4152    13 DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDP----EDRRRIGYLPEERGL------ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 555 ynlmYGNInaTAED--VYrVARLAGI--HDAI---------LKMPHKYDTQVGErglkLSGGEKQRVAIARAILKNPPIL 621
Cdd:COG4152    83 ----YPKM--KVGEqlVY-LARLKGLskAEAKrradewlerLGLGDRANKKVEE----LSKGNQQKVQLIAALLHDPELL 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2569209806 622 LYDEATSSLDSVTEENILTSMKEMV-KDRTSVFIAHRLSTiVD--ADEIIVLNQGKVAERGN 680
Cdd:COG4152   152 ILDEPFSGLDPVNVELLKDVIRELAaKGTTVIFSSHQMEL-VEelCDRIVIINKGRKVLSGS 212
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
 477-680 6.93e-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: 80.66  E-value: 6.93e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 477 KVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGL-ESLRKAVGVVPQDAvlfhnTIFY 555
Cdd:cd03218    14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMhKRARLGIGYLPQEA-----SIFR 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 556 NLmygninATAEDVYRVARLAGIHDAILKmpHKYDTQVGE---------RGLKLSGGEKQRVAIARAILKNPPILLYDEA 626
Cdd:cd03218    89 KL------TVEENILAVLEIRGLSKKERE--EKLEELLEEfhithlrksKASSLSGGERRRVEIARALATNPKFLLLDEP 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2569209806 627 TSSLDSVTEENILTSMKEMVKDRTSVFIA-HRLSTIVD-ADEIIVLNQGKVAERGN 680
Cdd:cd03218   161 FAGVDPIAVQDIQKIIKILKDRGIGVLITdHNVRETLSiTDRAYIIYEGKVLAEGT 216
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
 451-699 8.87e-17

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 83.95  E-value: 8.87e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 451 APPLIvtpqEATirfeDVYFEYlEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIrdV 530
Cdd:PRK15439    8 APPLL----CAR----SISKQY-SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPC--A 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 531 GLE-SLRKAVGV--VPQDAVLFHN-TIFYNLMYGnINATAEDVYRVARLAgihdAILKMPHKYDTQVGerglKLSGGEKQ 606
Cdd:PRK15439   77 RLTpAKAHQLGIylVPQEPLLFPNlSVKENILFG-LPKRQASMQKMKQLL----AALGCQLDLDSSAG----SLEVADRQ 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 607 RVAIARAILKNPPILLYDEATSSLDSVTEENILTSMKEM-VKDRTSVFIAHRLSTIVD-ADEIIVLNQGKVAERG----- 679
Cdd:PRK15439  148 IVEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELlAQGVGIVFISHKLPEIRQlADRISVMRDGTIALSGktadl 227

                         250       260
                  ....*....|....*....|..
gi 2569209806 680 NHQTLLD--TPGSLYANLWNTQ 699
Cdd:PRK15439  228 STDDIIQaiTPAAREKSLSASQ 249
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
 478-675 1.07e-16

ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.


Pssm-ID: 213234 [Multi-domain]  Cd Length: 236  Bit Score: 80.07  E-value: 1.07e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 478 VLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAgqnirdvGLESLRKAVGVVPQDAVLF--HNTIFY 555
Cdd:cd03267    36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVA-------GLVPWKRRKKFLRRIGVVFgqKTQLWW 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 556 NLMYGNINATAEDVYRV------ARLAGIHDaILKMPHKYDTQVgeRglKLSGGEKQRVAIARAILKNPPILLYDEATSS 629
Cdd:cd03267   109 DLPVIDSFYLLAAIYDLpparfkKRLDELSE-LLDLEELLDTPV--R--QLSLGQRMRAEIAAALLHEPEILFLDEPTIG 183

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2569209806 630 LDSVTEENILTSMKEMVKDR--TSVFIAHRLSTIVD-ADEIIVLNQGKV 675
Cdd:cd03267   184 LDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEAlARRVLVIDKGRL 232
cbiO PRK13643
energy-coupling factor transporter ATPase;
463-679 1.44e-16

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 80.93  E-value: 1.44e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 463 IRFEDVYFEYLE----GQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVG----LES 534
Cdd:PRK13643    2 IKFEKVNYTYQPnspfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeIKP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 535 LRKAVGVVPQ--DAVLFHNTIFYNLMYG--NINATAEDVYRVA----RLAGIHDAILKmphkydtqvgERGLKLSGGEKQ 606
Cdd:PRK13643   82 VRKKVGVVFQfpESQLFEETVLKDVAFGpqNFGIPKEKAEKIAaeklEMVGLADEFWE----------KSPFELSGGQMR 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2569209806 607 RVAIARAILKNPPILLYDEATSSLDSVTEENILTSMKEMVKD-RTSVFIAHRLSTIVD-ADEIIVLNQGKVAERG 679
Cdd:PRK13643  152 RVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSgQTVVLVTHLMDDVADyADYVYLLEKGHIISCG 226
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
467-693 1.51e-16

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 80.44  E-value: 1.51e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 467 DVYFEYlEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQ--NIRDVGLESLRKAVGVVPQ 544
Cdd:PRK13638    6 DLWFRY-QDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQVATVFQ 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 545 DAvlfHNTIFYNLMYGNInataedVYRVARLAGIHDAILKMPHKYDTQVGERGLK------LSGGEKQRVAIARAILKNP 618
Cdd:PRK13638   85 DP---EQQIFYTDIDSDI------AFSLRNLGVPEAEITRRVDEALTLVDAQHFRhqpiqcLSHGQKKRVAIAGALVLQA 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2569209806 619 PILLYDEATSSLDSVTEENILTSMKEMVKDRTSVFI-AHRLSTIVD-ADEIIVLNQGKVAERGNhqtlldtPGSLYA 693
Cdd:PRK13638  156 RYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIIsSHDIDLIYEiSDAVYVLRQGQILTHGA-------PGEVFA 225
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
475-677 3.90e-16

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 81.88  E-value: 3.90e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 475 GQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQ-----NIRDvgleSLRKAVGVVPQDAVLF 549
Cdd:PRK11288   16 GVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQemrfaSTTA----ALAAGVAIIYQELHLV 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 550 HN-TIFYNLMYGNINATA-----EDVYRVAR--LAGIHDAIlkmphKYDTQVGErglkLSGGEKQRVAIARAILKNPPIL 621
Cdd:PRK11288   92 PEmTVAENLYLGQLPHKGgivnrRLLNYEAReqLEHLGVDI-----DPDTPLKY----LSIGQRQMVEIAKALARNARVI 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2569209806 622 LYDEATSSLdSVTEENILTSMKEMVKD--RTSVFIAHRLSTIVD-ADEIIVLNQGKVAE 677
Cdd:PRK11288  163 AFDEPTSSL-SAREIEQLFRVIRELRAegRVILYVSHRMEEIFAlCDAITVFKDGRYVA 220
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
 475-674 4.32e-16

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 81.90  E-value: 4.32e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 475 GQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYePQ---QGNIYIAGQ-----NIRDvgleSLRKAVGVVPQDA 546
Cdd:PRK13549   17 GVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEelqasNIRD----TERAGIAIIHQEL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 547 VLFHN-TIFYNLMYGN-------INATAedVY-RVARLAgihdAILKMPHKYDTQVGErglkLSGGEKQRVAIARAILKN 617
Cdd:PRK13549   92 ALVKElSVLENIFLGNeitpggiMDYDA--MYlRAQKLL----AQLKLDINPATPVGN----LGLGQQQLVEIAKALNKQ 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2569209806 618 PPILLYDEATSSL-DSVTEE--NILTSMKEmvKDRTSVFIAHRLSTIVD-ADEIIVLNQGK 674
Cdd:PRK13549  162 ARLLILDEPTASLtESETAVllDIIRDLKA--HGIACIYISHKLNEVKAiSDTICVIRDGR 220
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
459-694 5.99e-16

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


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 78.00  E-value: 5.99e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 459 QEATIRFEDVYFEYLEGQkVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGLES-LRK 537
Cdd:PRK11614    2 EKVMLSFDKVSAHYGKIQ-ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKiMRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 538 AVGVVPQDAVLFHN-TIFYNLMYGNINATAEDVY-RVARLAGIhdailkMPHKYDTQVgERGLKLSGGEKQRVAIARAIL 615
Cdd:PRK11614   81 AVAIVPEGRRVFSRmTVEENLAMGGFFAERDQFQeRIKWVYEL------FPRLHERRI-QRAGTMSGGEQQMLAIGRALM 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 616 KNPPILLYDEATSSLDSVTEENILTSMKEMVKDRTSVFIAHRlstivDADEIIVL-NQGKVAERGnHQTLLDTPGSLYAN 694
Cdd:PRK11614  154 SQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQ-----NANQALKLaDRGYVLENG-HVVLEDTGDALLAN 227
ABC_6TM_exporter_like cd18563
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
 131-429 6.32e-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: 79.09  E-value: 6.32e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 131 VVISLSLLAGAKITNVMVPFMFKYAVDSLNQMSGHMLNLSDAPNTVVTMAtavligygVSRTGSALFNELRNAVFGKVAQ 210
Cdd:cd18563     1 LILGFLLMLLGTALGLVPPYLTKILIDDVLIQLGPGGNTSLLLLLVLGLA--------GAYVLSALLGILRGRLLARLGE 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 211 SSIRRIAKNVFLHLHNLDLGFHLSRQTGALskaIDRGTRGISFVLSALVFNLGPTLFEMMLVSGIlyykcGG-------H 283
Cdd:cd18563    73 RITADLRRDLYEHLQRLSLSFFDKRQTGSL---MSRVTSDTDRLQDFLSDGLPDFLTNILMIIGI-----GVvlfslnwK 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 284 FALVTLGTLSAYTAFTVAV-----TQWRTQFRIemnkadneagNAAIDSLLNyET------VKYFNNEKYEAERYDGFLK 352
Cdd:cd18563   145 LALLVLIPVPLVVWGSYFFwkkirRLFHRQWRR----------WSRLNSVLN-DTlpgirvVKAFGQEKREIKRFDEANQ 213

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2569209806 353 VYESSSLKTTSTLAMLNFGQSAIFSVGLTAIMVLASKGIMSGTMTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQAL 429
Cdd:cd18563   214 ELLDANIRAEKLWATFFPLLTFLTSLGTLIVWYFGGRQVLSGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRAL 290
ABC_6TM_YknU_like cd18542
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ...
 131-419 9.58e-16

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


Pssm-ID: 349986 [Multi-domain]  Cd Length: 292  Bit Score: 78.24  E-value: 9.58e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 131 VVISLSLLAGAKITNVMVPFMFKYAVDSLnqmsghmlnLSDAPNTVVTMATAVLIGYGVSRtgsALFNELRNAVFGKVAQ 210
Cdd:cd18542     1 YLLAILALLLATALNLLIPLLIRRIIDSV---------IGGGLRELLWLLALLILGVALLR---GVFRYLQGYLAEKASQ 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 211 SSIRRIAKNVFLHLHNLDLGFHLSRQTGALskaIDRGT-------RGISFVLSALVFNLgptlfemMLVSGILYY----- 278
Cdd:cd18542    69 KVAYDLRNDLYDHLQRLSFSFHDKARTGDL---MSRCTsdvdtirRFLAFGLVELVRAV-------LLFIGALIImfsin 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 279 -KcgghFALVTLGT--LSAYTAFTVAVTQWRTQFRI-----EMNKA--DNEAGNaaidsllnyETVKYFNNEKYEAERYD 348
Cdd:cd18542   139 wK----LTLISLAIipFIALFSYVFFKKVRPAFEEIreqegELNTVlqENLTGV---------RVVKAFAREDYEIEKFD 205

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2569209806 349 GFLKVYESSSLKTTSTLA----MLNFgqsaIFSVGLTAIMVLASKGIMSGTMTVGDLVMVNGLLFQLSLPLNFLG 419
Cdd:cd18542   206 KENEEYRDLNIKLAKLLAkywpLMDF----LSGLQIVLVLWVGGYLVINGEITLGELVAFISYLWMLIWPVRQLG 276
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
 477-688 1.36e-15

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 78.59  E-value: 1.36e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 477 KVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGLESL---RKAVGVVPQDAVLFHN-- 551
Cdd:PRK15079   35 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWravRSDIQMIFQDPLASLNpr 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 552 -TIfynlmyGNINA----------TAEDVY-RV----ARLAGIHDAILKMPHKYdtqvgerglklSGGEKQRVAIARAIL 615
Cdd:PRK15079  115 mTI------GEIIAeplrtyhpklSRQEVKdRVkammLKVGLLPNLINRYPHEF-----------SGGQCQRIGIARALI 177

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2569209806 616 KNPPILLYDEATSSLD-SVTEE--NILTSM-KEMvkDRTSVFIAHRLSTIVD-ADEIIVLNQGKVAERGNHQTLLDTP 688
Cdd:PRK15079  178 LEPKLIICDEPVSALDvSIQAQvvNLLQQLqREM--GLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEVYHNP 253
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
474-670 1.82e-15

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 75.35  E-value: 1.82e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 474 EGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGqnirdvgleslRKAVGVVPQ----DAVLf 549
Cdd:NF040873    3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQrsevPDSL- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 550 hntifynlmygniNATAEDVYRVARLAgiHDAILKMPHKYDTQVGERGLK--------------LSGGEKQRVAIARAIL 615
Cdd:NF040873   71 -------------PLTVRDLVAMGRWA--RRGLWRRLTRDDRAAVDDALErvgladlagrqlgeLSGGQRQRALLAQGLA 135

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2569209806 616 KNPPILLYDEATSSLDSVTEENILTSMKEMVKD-RTSVFIAHRLSTIVDADEIIVL 670
Cdd:NF040873  136 QEADLLLLDEPTTGLDAESRERIIALLAEEHARgATVVVVTHDLELVRRADPCVLL 191
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
482-688 2.32e-15

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 76.75  E-value: 2.32e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 482 VSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIR--DVGLESLRkaVGVVPQDAVLFHN------TI 553
Cdd:PRK15112   32 LSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDYSYRSQR--IRMIFQDPSTSLNprqrisQI 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 554 FYNLMYGNINATAED----VYRVARLAGI-HDAILKMPHKydtqvgerglkLSGGEKQRVAIARAILKNPPILLYDEATS 628
Cdd:PRK15112  110 LDFPLRLNTDLEPEQrekqIIETLRQVGLlPDHASYYPHM-----------LAPGQKQRLGLARALILRPKVIIADEALA 178

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2569209806 629 SLDSVTEENILTSMKEMVKDR--TSVFIAHRLSTIVD-ADEIIVLNQGKVAERGNHQTLLDTP 688
Cdd:PRK15112  179 SLDMSMRSQLINLMLELQEKQgiSYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVLASP 241
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
 478-636 2.77e-15

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 75.30  E-value: 2.77e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 478 VLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGLESLRKAVGvvPQDAVLFHNTIFYNL 557
Cdd:PRK13539   17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLG--HRNAMKPALTVAENL 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 558 -MYGNINATAE-DVYRVARLAGIHDaILKMPHKYdtqvgerglkLSGGEKQRVAIARAILKNPPILLYDEATSSLDSVTE 635
Cdd:PRK13539   95 eFWAAFLGGEElDIAAALEAVGLAP-LAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAV 163


                  .
gi 2569209806 636 E 636
Cdd:PRK13539  164 A 164
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
 460-685 3.23e-15

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


Pssm-ID: 132313 [Multi-domain]  Cd Length: 520  Bit Score: 79.08  E-value: 3.23e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 460 EATIRFEDVYFEYLEGQ----KVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYI-AGQNIRDV---- 530
Cdd:TIGR03269 277 EPIIKVRNVSKRYISVDrgvvKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrVGDEWVDMtkpg 356

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 531 --GLESLRKAVGVVPQDAVLF-HNTIFYNLMYGnIN-------ATAEDVYrVARLAGIHD----AIL-KMPHKydtqvge 595
Cdd:TIGR03269 357 pdGRGRAKRYIGILHQEYDLYpHRTVLDNLTEA-IGlelpdelARMKAVI-TLKMVGFDEekaeEILdKYPDE------- 427

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 596 rglkLSGGEKQRVAIARAILKNPPILLYDEATSSLDSVTE----ENILTSMKEMvkDRTSVFIAHRLSTIVD-ADEIIVL 670
Cdd:TIGR03269 428 ----LSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKvdvtHSILKAREEM--EQTFIIVSHDMDFVLDvCDRAALM 501

                         250
                  ....*....|....*
gi 2569209806 671 NQGKVAERGNHQTLL 685
Cdd:TIGR03269 502 RDGKIVKIGDPEEIV 516
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
 461-685 3.39e-15

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 75.70  E-value: 3.39e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 461 ATIRFEDVYFEYlEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGL-ESLRKAV 539
Cdd:PRK10895    2 ATLTAKNLAKAY-KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhARARRGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 540 GVVPQDAVLFHN-TIFYNLMygNINATAEDVYRVARLAGIHDAI--LKMPHKYDTQvgerGLKLSGGEKQRVAIARAILK 616
Cdd:PRK10895   81 GYLPQEASIFRRlSVYDNLM--AVLQIRDDLSAEQREDRANELMeeFHIEHLRDSM----GQSLSGGERRRVEIARALAA 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2569209806 617 NPPILLYDEATSSLDSVTEENILTSMKEMVKDRTSVFIA-HRLSTIVDADE-IIVLNQGKVAERGNHQTLL 685
Cdd:PRK10895  155 NPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITdHNVRETLAVCErAYIVSQGHLIAHGTPTEIL 225
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
 475-695 6.83e-15

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 75.35  E-value: 6.83e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 475 GQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGLESL---------RKAVGVVPQD 545
Cdd:PRK11701   18 PRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseaerrrllRTEWGFVHQH 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 546 A-------VLFHNTIFYNLM------YGNINATAED-VYRV----ARlagIHDAilkmPHKYdtqvgerglklSGGEKQR 607
Cdd:PRK11701   98 PrdglrmqVSAGGNIGERLMavgarhYGDIRATAGDwLERVeidaAR---IDDL----PTTF-----------SGGMQQR 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 608 VAIARAILKNPPILLYDEATSSLDSVTEENILTSMKEMVKD-RTSVFI-AHRLSTI-VDADEIIVLNQGKVAERGNHQTL 684
Cdd:PRK11701  160 LQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIvTHDLAVArLLAHRLLVMKQGRVVESGLTDQV 239

                         250
                  ....*....|.
gi 2569209806 685 LDTPGSLYANL 695
Cdd:PRK11701  240 LDDPQHPYTQL 250
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
456-679 8.06e-15

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 75.41  E-value: 8.06e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 456 VTPQEATIRFEDVYFEYleGQK-VLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGLES 534
Cdd:PRK10253    1 MTESVARLRGEQLTLGY--GKYtVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 535 LRKAVGVVPQDAVLFHNTIFYNL----------MYGNINATAED-VYRVARLAGIHDAILKmphKYDTqvgerglkLSGG 603
Cdd:PRK10253   79 VARRIGLLAQNATTPGDITVQELvargryphqpLFTRWRKEDEEaVTKAMQATGITHLADQ---SVDT--------LSGG 147

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2569209806 604 EKQRVAIARAILKNPPILLYDEATSSLDSVTEENILTSMKEMVKDR--TSVFIAHRLSTIVD-ADEIIVLNQGKVAERG 679
Cdd:PRK10253  148 QRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKgyTLAAVLHDLNQACRyASHLIALREGKIVAQG 226
BtuD COG4138
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ...
 479-691 3.31e-14

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


Pssm-ID: 443313 [Multi-domain]  Cd Length: 248  Bit Score: 72.95  E-value: 3.31e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 479 LNGVSFEVPAGKKVAIVGGSGSGKSTivrLLFRF--YEPQQGNIYIAGQNIRDVGLESLRKAVGVVPQDAVL------FH 550
Cdd:COG4138    12 LGPISAQVNAGELIHLIGPNGAGKST---LLARMagLLPGQGEILLNGRPLSDWSAAELARHRAYLSQQQSPpfampvFQ 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 551 ntiFYNLMYGNINATAEDVYRVARLAGIhdaiLKMPHKYDTQVGerglKLSGGEKQRVAIARAILK-----NPP--ILLY 623
Cdd:COG4138    89 ---YLALHQPAGASSEAVEQLLAQLAEA----LGLEDKLSRPLT----QLSGGEWQRVRLAAVLLQvwptiNPEgqLLLL 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2569209806 624 DEATSSLDsVTEENIL-TSMKEMV-KDRTSVFIAHRLS-TIVDADEIIVLNQGKVAERGNHQTLLdTPGSL 691
Cdd:COG4138   158 DEPMNSLD-VAQQAALdRLLRELCqQGITVVMSSHDLNhTLRHADRVWLLKQGKLVASGETAEVM-TPENL 226
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
 463-657 4.41e-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: 70.65  E-value: 4.41e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 463 IRFEDVYFEYLEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNirdvgleslrkavgvv 542
Cdd:cd03223     1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGE---------------- 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 543 pqdAVLFhntifynlmygninataedvyrvarlagihdailkMPHK-YDTQVGER-------GLKLSGGEKQRVAIARAI 614
Cdd:cd03223    65 ---DLLF-----------------------------------LPQRpYLPLGTLReqliypwDDVLSGGEQQRLAFARLL 106

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2569209806 615 LKNPPILLYDEATSSLDSVTEENILtsmkEMVKDR--TSVFIAHR 657
Cdd:cd03223   107 LHKPKFVFLDEATSALDEESEDRLY----QLLKELgiTVISVGHR 147
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
459-688 5.17e-14

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 72.90  E-value: 5.17e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 459 QEATIRFEDVYFEyLEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGLESLRKA 538
Cdd:PRK10575    8 SDTTFALRNVSFR-VPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARK 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 539 VGVVPQdavlfhntifynlmygniNATAEDVYRVARLAGI-----HDAILKMPHKYDTQVGER----GLK---------L 600
Cdd:PRK10575   87 VAYLPQ------------------QLPAAEGMTVRELVAIgrypwHGALGRFGAADREKVEEAislvGLKplahrlvdsL 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 601 SGGEKQRVAIARAILKNPPILLYDEATSSLDSVTEENILTSMKEMVKDRTSVFIA--HRLSTIVD-ADEIIVLNQGKVAE 677
Cdd:PRK10575  149 SGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAvlHDINMAARyCDYLVALRGGEMIA 228

                         250
                  ....*....|.
gi 2569209806 678 RGNHQTLLDTP 688
Cdd:PRK10575  229 QGTPAELMRGE 239
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
 475-678 1.05e-13

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 74.27  E-value: 1.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 475 GQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGLESLRKA-VGVVPQDAVLFHN-T 552
Cdd:PRK10762   16 GVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAgIGIIHQELNLIPQlT 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 553 IFYNLMYGNINATA------EDVYRVArlagihDAILK---MPHKYDTQVGErglkLSGGEKQRVAIARAILKNPPILLY 623
Cdd:PRK10762   96 IAENIFLGREFVNRfgridwKKMYAEA------DKLLArlnLRFSSDKLVGE----LSIGEQQMVEIAKVLSFESKVIIM 165

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 624 DEATSSL-DSVTEE--NILTSMKEmvKDRTSVFIAHRLSTIVD-ADEIIVLNQGK-VAER 678
Cdd:PRK10762  166 DEPTDALtDTETESlfRVIRELKS--QGRGIVYISHRLKEIFEiCDDVTVFRDGQfIAER 223
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
 473-690 1.07e-13

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 71.65  E-value: 1.07e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 473 LEGQKVL-NGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEP----QQGNIYIAGQ---------------------- 525
Cdd:PRK10418   12 LQAAQPLvHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKpvapcalrgrkiatimqnprsa 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 526 -----NIRDVGLESLRkAVGVVPQDAVLFHNTIFYNLmygninataEDVYRVARLagihdailkmpHKYDtqvgerglkL 600
Cdd:PRK10418   92 fnplhTMHTHARETCL-ALGKPADDATLTAALEAVGL---------ENAARVLKL-----------YPFE---------M 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 601 SGGEKQRVAIARAILKNPPILLYDEATSSLDSVTEENILTSMKEMVKDRTS--VFIAHRLSTIVD-ADEIIVLNQGKVAE 677
Cdd:PRK10418  142 SGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALgmLLVTHDMGVVARlADDVAVMSHGRIVE 221

                         250
                  ....*....|...
gi 2569209806 678 RGNHQTLLDTPGS 690
Cdd:PRK10418  222 QGDVETLFNAPKH 234
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 477-680 1.10e-13

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


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 72.81  E-value: 1.10e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 477 KVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNI---RdvglESLRKAVGVV----------- 542
Cdd:COG4586    36 EAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPfkrR----KEFARRIGVVfgqrsqlwwdl 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 543 -PQDAVLFHNTIfYNLmygninatAEDVY--RVARLAGihdaILKMPHKYDTQVgeRglKLSGGEKQRVAIARAILKNPP 619
Cdd:COG4586   112 pAIDSFRLLKAI-YRI--------PDAEYkkRLDELVE----LLDLGELLDTPV--R--QLSLGQRMRCELAAALLHRPK 174

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2569209806 620 ILLYDEATSSLDSVTEENILTSMKEMVKDR-TSVFIA-HRLSTIVD-ADEIIVLNQGKVAERGN 680
Cdd:COG4586   175 ILFLDEPTIGLDVVSKEAIREFLKEYNRERgTTILLTsHDMDDIEAlCDRVIVIDHGRIIYDGS 238
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
 462-692 1.42e-13

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 74.12  E-value: 1.42e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 462 TIRFEDvyfeylEGQKV--LNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIR----------- 528
Cdd:PRK10261   19 NIAFMQ------EQQKIaaVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRrrsrqvielse 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 529 --DVGLESLRKA-VGVVPQDAVLFHNTIF-------------YNLMYGNINATAEDVYRVARLAGIHDAILKMPHKydtq 592
Cdd:PRK10261   93 qsAAQMRHVRGAdMAMIFQEPMTSLNPVFtvgeqiaesirlhQGASREEAMVEAKRMLDQVRIPEAQTILSRYPHQ---- 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 593 vgerglkLSGGEKQRVAIARAILKNPPILLYDEATSSLDSVTEENILTSMKEMVKDRTS--VFIAHRLSTIVD-ADEIIV 669
Cdd:PRK10261  169 -------LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMgvIFITHDMGVVAEiADRVLV 241

                         250       260
                  ....*....|....*....|...
gi 2569209806 670 LNQGKVAERGNHQTLLDTPGSLY 692
Cdd:PRK10261  242 MYQGEAVETGSVEQIFHAPQHPY 264
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
 493-675 2.42e-13

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: 74.28  E-value: 2.42e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806  493 AIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIrDVGLESLRKAVGVVPQDAVLFHNTIF--YNLMYGNINATAEDVY 570
Cdd:TIGR01257  960 AFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHLTVaeHILFYAQLKGRSWEEA 1038

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806  571 RVARLAGIHDAILKmpHKYDtqvgERGLKLSGGEKQRVAIARAILKNPPILLYDEATSSLDSVTEENILTSMKEMVKDRT 650
Cdd:TIGR01257 1039 QLEMEAMLEDTGLH--HKRN----EEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRT 1112

                          170       180
                   ....*....|....*....|....*.
gi 2569209806  651 SVFIAHRLSTI-VDADEIIVLNQGKV 675
Cdd:TIGR01257 1113 IIMSTHHMDEAdLLGDRIAIISQGRL 1138
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
 470-654 2.52e-13

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127 [Multi-domain]  Cd Length: 200  Bit Score: 69.21  E-value: 2.52e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 470 FEYlEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIrDVGLESLRKAVGVVPQDAVLF 549
Cdd:PRK13540    9 FDY-HDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI-KKDLCTYQKQLCFVGHRSGIN 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 550 HN-TIFYNLMYG-NINATAEDVYRVARlagihdaILKMPHKYDTQVGerglKLSGGEKQRVAIARAILKNPPILLYDEAT 627
Cdd:PRK13540   87 PYlTLRENCLYDiHFSPGAVGITELCR-------LFSLEHLIDYPCG----LLSSGQKRQVALLRLWMSKAKLWLLDEPL 155

                         170       180
                  ....*....|....*....|....*..
gi 2569209806 628 SSLDSVTEENILTSMKEMVKDRTSVFI 654
Cdd:PRK13540  156 VALDELSLLTIITKIQEHRAKGGAVLL 182
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
 475-625 2.61e-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: 2.61e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 475 GQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIvrllfrFY------EPQQGNIYIAGQNIRDvglesL------RKAVGVV 542
Cdd:COG1137    15 KRTVVKDVSLEVNQGEIVGLLGPNGAGKTTT------FYmivglvKPDSGRIFLDGEDITH-----LpmhkraRLGIGYL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 543 PQDAvlfhnTIFYNL-MYGNINATAEDVY-----RVARLagihDAILK---MPHKYDTqvgeRGLKLSGGEKQRVAIARA 613
Cdd:COG1137    84 PQEA-----SIFRKLtVEDNILAVLELRKlskkeREERL----EELLEefgITHLRKS----KAYSLSGGERRRVEIARA 150

                         170
                  ....*....|..
gi 2569209806 614 ILKNPPILLYDE 625
Cdd:COG1137   151 LATNPKFILLDE 162
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
 478-654 2.82e-13

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 69.81  E-value: 2.82e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 478 VLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGLE---SLR-KAVGVVPQDAVL----- 548
Cdd:PRK10584   25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEaraKLRaKHVGFVFQSFMLiptln 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 549 -FHNTIFYNLMYG-NINATAEDVYRVARLAGIHDAILKMPhkydtqvgergLKLSGGEKQRVAIARAILKNPPILLYDEA 626
Cdd:PRK10584  105 aLENVELPALLRGeSSRQSRNGAKALLEQLGLGKRLDHLP-----------AQLSGGEQQRVALARAFNGRPDVLFADEP 173

                         170       180
                  ....*....|....*....|....*...
gi 2569209806 627 TSSLDSVTEENILTSMKEMVKDRTSVFI 654
Cdd:PRK10584  174 TGNLDRQTGDKIADLLFSLNREHGTTLI 201
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
 475-642 2.85e-13

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: 69.06  E-value: 2.85e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 475 GQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGLESLRKAVGVVPQDAVLFHNTIF 554
Cdd:cd03231    12 GRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 555 YNL-MYGNINATA--EDVYRVARLAGIHDAILKmphkydtqvgerglKLSGGEKQRVAIARAILKNPPILLYDEATSSLD 631
Cdd:cd03231    92 ENLrFWHADHSDEqvEEALARVGLNGFEDRPVA--------------QLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157

                         170
                  ....*....|.
gi 2569209806 632 SVTEENILTSM 642
Cdd:cd03231   158 KAGVARFAEAM 168
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
 474-679 3.09e-13

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: 69.09  E-value: 3.09e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 474 EGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRF--YEPQQGNIYIAGQNIRDVGL-ESLRKAVGVVPQDAVLFH 550
Cdd:cd03217    11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPeERARLGIFLAFQYPPEIP 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 551 NTifynlmygninaTAEDVYRvarlagihdailkmphkydtQVGErglKLSGGEKQRVAIARAILKNPPILLYDEATSSL 630
Cdd:cd03217    91 GV------------KNADFLR--------------------YVNE---GFSGGEKKRNEILQLLLLEPDLAILDEPDSGL 135

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2569209806 631 DSVTEENILTSMKEMVKDRTSVF-IAH--RLSTIVDADEIIVLNQGKVAERG 679
Cdd:cd03217   136 DIDALRLVAEVINKLREEGKSVLiITHyqRLLDYIKPDRVHVLYDGRIVKSG 187
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
 482-675 3.70e-13

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 69.96  E-value: 3.70e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 482 VSFEVPAGKKVAIVGGSGSGKSTivrLLFRF--YEPQQGNIYIAGQNIRDVGLESL--RKAVgVVPQDAVLFHNTIFYNL 557
Cdd:PRK03695   15 LSAEVRAGEILHLVGPNGAGKST---LLARMagLLPGSGSIQFAGQPLEAWSAAELarHRAY-LSQQQTPPFAMPVFQYL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 558 MY-----GNINATAEDVYRVARLAGIHDailkmphKYDTQVGErglkLSGGEKQRVAIARAILK-----NP--PILLYDE 625
Cdd:PRK03695   91 TLhqpdkTRTEAVASALNEVAEALGLDD-------KLGRSVNQ----LSGGEWQRVRLAAVVLQvwpdiNPagQLLLLDE 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2569209806 626 ATSSLDsVTEENILTSM-KEMVKDRTSVFIA-HRLS-TIVDADEIIVLNQGKV 675
Cdd:PRK03695  160 PMNSLD-VAQQAALDRLlSELCQQGIAVVMSsHDLNhTLRHADRVWLLKQGKL 211
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
 475-674 3.99e-13

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


Pssm-ID: 131681 [Multi-domain]  Cd Length: 500  Bit Score: 72.55  E-value: 3.99e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 475 GQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYePQ---QGNIYIAGQNIRDVGL-ESLRKAVGVVPQDAVLFH 550
Cdd:TIGR02633  13 GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHgtwDGEIYWSGSPLKASNIrDTERAGIVIIHQELTLVP 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 551 N-TIFYNLMYGN-------INATAEDVYRVARLAgihdAILKMPHKYDTQ-VGERGlklsGGEKQRVAIARAILKNPPIL 621
Cdd:TIGR02633  92 ElSVAENIFLGNeitlpggRMAYNAMYLRAKNLL----RELQLDADNVTRpVGDYG----GGQQQLVEIAKALNKQARLL 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2569209806 622 LYDEATSSLDSVTEENILTSMKEM-VKDRTSVFIAHRLSTI-VDADEIIVLNQGK 674
Cdd:TIGR02633 164 ILDEPSSSLTEKETEILLDIIRDLkAHGVACVYISHKLNEVkAVCDTICVIRDGQ 218
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
 477-688 5.54e-13

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 70.54  E-value: 5.54e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 477 KVLNGVSFEVPAGKKVAIVGGSGSGKS----TIVRLLFRFYEPQQGNIYIAGQNIRDVGLESLRKAVG----VVPQDAVL 548
Cdd:PRK11022   21 RAVDRISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISEKERRNLVGaevaMIFQDPMT 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 549 FHN---TIFYNLMY-------GNINATAEDVYRVARLAGIHDAILKM---PHKydtqvgerglkLSGGEKQRVAIARAIL 615
Cdd:PRK11022  101 SLNpcyTVGFQIMEaikvhqgGNKKTRRQRAIDLLNQVGIPDPASRLdvyPHQ-----------LSGGMSQRVMIAMAIA 169

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2569209806 616 KNPPILLYDEATSSLDSVTEENILTSMKEMVK--DRTSVFIAHRLSTIVD-ADEIIVLNQGKVAERGNHQTLLDTP 688
Cdd:PRK11022  170 CRPKLLIADEPTTALDVTIQAQIIELLLELQQkeNMALVLITHDLALVAEaAHKIIVMYAGQVVETGKAHDIFRAP 245
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
448-676 5.75e-13

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 71.97  E-value: 5.75e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 448 KEMAPPLIVTPQEATIRFEDvyfeyLEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQ-- 525
Cdd:COG1129   242 EDLFPKRAAAPGEVVLEVEG-----LSVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpv 316

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 526 NIRDVGlESLRKAVGVVPQD----AVLFHNTIFYNLMYGNI--------------NATAEDVyrVARLAgihdaiLKMPH 587
Cdd:COG1129   317 RIRSPR-DAIRAGIAYVPEDrkgeGLVLDLSIRENITLASLdrlsrgglldrrreRALAEEY--IKRLR------IKTPS 387

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 588 KyDTQVGErglkLSGGEKQRVAIARAILKNPPILLYDEATSSLDSVTEENILTSMKEMVKDRTSV-FIAHRLSTIVD-AD 665
Cdd:COG1129   388 P-EQPVGN----LSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAViVISSELPELLGlSD 462

                         250
                  ....*....|.
gi 2569209806 666 EIIVLNQGKVA 676
Cdd:COG1129   463 RILVMREGRIV 473
ABC_6TM_PCAT1_LagD_like cd18570
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ...
 130-418 6.73e-13

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: 69.78  E-value: 6.73e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 130 RVVISLSLLAGAKIT--NVMVPFMFKYAVDSL--NQMSghmlnlsdapNTVVTMATAVLIGYGVSrtgsALFNELRNAVF 205
Cdd:cd18570     1 KKLLILILLLSLLITllGIAGSFFFQILIDDIipSGDI----------NLLNIISIGLILLYLFQ----SLLSYIRSYLL 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 206 GKVAQSSIRRIAKNVFLHLHNLDLGFHLSRQTGA-LSKAIDrgTRGISFVLSALVFNLGPTLFeMMLVSGILYYKCGGHF 284
Cdd:cd18570    67 LKLSQKLDIRLILGYFKHLLKLPLSFFETRKTGEiISRFND--ANKIREAISSTTISLFLDLL-MVIISGIILFFYNWKL 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 285 ALVTLGTLSAYTAFTVAvtqwrtqFRIEMNKADNEA--GNAA-----IDSLLNYETVKYFNNEKYEAERYDGFLKVYESS 357
Cdd:cd18570   144 FLITLLIIPLYILIILL-------FNKPFKKKNREVmeSNAElnsylIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKK 216

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2569209806 358 SLKTTSTLAMLNFGQSAIFSVGLTAIMVLASKGIMSGTMTVGDLVMVNGLLFQLSLPLNFL 418
Cdd:cd18570   217 SFKLGKLSNLQSSIKGLISLIGSLLILWIGSYLVIKGQLSLGQLIAFNALLGYFLGPIENL 277
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
477-682 1.52e-12

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 68.50  E-value: 1.52e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 477 KVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFY---EPQQGNIYIAGQNIRDVG-----LESLRKAVGVVPQDAVL 548
Cdd:PRK09984   18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVQREGrlardIRKSRANTGYIFQQFNL 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 549 FHN-TIFYNLMYGNINATAedVYRVArLAGIHDAILKMPHKYDTQVG------ERGLKLSGGEKQRVAIARAILKNPPIL 621
Cdd:PRK09984   98 VNRlSVLENVLIGALGSTP--FWRTC-FSWFTREQKQRALQALTRVGmvhfahQRVSTLSGGQQQRVAIARALMQQAKVI 174

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2569209806 622 LYDEATSSLDSVTEENILTSMKEMVKDR--TSVFIAHRLSTIVD-ADEIIVLNQGKVAERGNHQ 682
Cdd:PRK09984  175 LADEPIASLDPESARIVMDTLRDINQNDgiTVVVTLHQVDYALRyCERIVALRQGHVFYDGSSQ 238
ABC_6TM_exporter_like cd18564
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
 132-427 1.70e-12

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


Pssm-ID: 350008 [Multi-domain]  Cd Length: 307  Bit Score: 69.08  E-value: 1.70e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 132 VISLSLLAGAKITNVMVPFMFKYAVDS------LNQMSGHMLNLSDAPNTVVTMATAVLIGYGVSRtgsALFNELRNAVF 205
Cdd:cd18564     2 ALALLALLLETALRLLEPWPLKVVIDDvlgdkpLPGLLGLAPLLGPDPLALLLLAAAALVGIALLR---GLASYAGTYLT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 206 GKVAQSSIRRIAKNVFLHLHNLDLGFHLSRQTGALskaIDRGTRGI----SFVLSALVfNLGPTLFEMMLVSGILYY--- 278
Cdd:cd18564    79 ALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDL---LSRLTGDVgaiqDLLVSGVL-PLLTNLLTLVGMLGVMFWldw 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 279 KcgghFALVTLGTLSaytAFTVAVTQWRTQFRIEMNKADNEAGN-AAI--DSLLNYETVKYFNNEKYEAERYDGFLKVYE 355
Cdd:cd18564   155 Q----LALIALAVAP---LLLLAARRFSRRIKEASREQRRREGAlASVaqESLSAIRVVQAFGREEHEERRFARENRKSL 227

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2569209806 356 SSSLKTTSTLAMLNFGQSAIFSVGLTAIMVLASKGIMSGTMTVGDLvmvngLLFqlslpLNFLGTVYRETRQ 427
Cdd:cd18564   228 RAGLRAARLQALLSPVVDVLVAVGTALVLWFGAWLVLAGRLTPGDL-----LVF-----LAYLKNLYKPVRD 289
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
 476-677 2.91e-12

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


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 66.91  E-value: 2.91e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 476 QKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYE--PQQGNIYIAGQNIrdvgleslrkavgvvPQDAVLFHNti 553
Cdd:COG2401    43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQF---------------GREASLIDA-- 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 554 fynlmYGNINATAEDVYRVARlAGIHDAILkMPHKYDTqvgerglkLSGGEKQRVAIARAILKNPPILLYDEATSSLDSV 633
Cdd:COG2401   106 -----IGRKGDFKDAVELLNA-VGLSDAVL-WLRRFKE--------LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQ 170

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2569209806 634 TEENILTSMKEMVKDR--TSVFIAHRlSTIVDA---DEIIVLNQGKVAE 677
Cdd:COG2401   171 TAKRVARNLQKLARRAgiTLVVATHH-YDVIDDlqpDLLIFVGYGGVPE 218
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
 441-683 4.02e-12

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 69.29  E-value: 4.02e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 441 VDTKIKEKEMAPPliVTPQEATIRFEDVYFEYLEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNI 520
Cdd:COG3845   238 VGREVLLRVEKAP--AEPGEVVLEVENLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSI 315

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 521 YIAGQNIRDVGLESLRKA-VGVVPQD-----AV----LFHNTIFYN-----------LMYGNINATAEDV---YRVaRLA 576
Cdd:COG3845   316 RLDGEDITGLSPRERRRLgVAYIPEDrlgrgLVpdmsVAENLILGRyrrppfsrggfLDRKAIRAFAEELieeFDV-RTP 394

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 577 GIhdailkmphkyDTQVGerglKLSGGEKQRVAIARAILKNPPILLYDEATSSLDSVTEENILTSMKEMVKDRTSV-FIA 655
Cdd:COG3845   395 GP-----------DTPAR----SLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVlLIS 459

                         250       260       270
                  ....*....|....*....|....*....|
gi 2569209806 656 HRLSTIVD-ADEIIVLNQGK-VAERGNHQT 683
Cdd:COG3845   460 EDLDEILAlSDRIAVMYEGRiVGEVPAAEA 489
ABC_6TM_MsbA_like cd18552
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ...
 131-429 5.41e-12

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: 67.06  E-value: 5.41e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 131 VVISLSLLAGAKITNVMVPFMFKYAVDSLNQmsghmlnlSDAPNTVVTMATAVLIGYGVSrtgsALFNELRNAVFGKVAQ 210
Cdd:cd18552     1 LALAILGMILVAATTAALAWLLKPLLDDIFV--------EKDLEALLLVPLAIIGLFLLR----GLASYLQTYLMAYVGQ 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 211 SSIRRIAKNVFLHLHNLDLGFHLSRQTGALskaIDRGTRGISFVLSALVFNLGPTLFEMMLVSGILYY------KcgghF 284
Cdd:cd18552    69 RVVRDLRNDLFDKLLRLPLSFFDRNSSGDL---ISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVlfyldwK----L 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 285 ALVTLGTLSAyTAFTVAVTQWRtqFRIEMNKADNEAGN---AAIDSLLNYETVKYFNNEKYEAERYDGFLKVYESSSLKT 361
Cdd:cd18552   142 TLIALVVLPL-AALPIRRIGKR--LRKISRRSQESMGDltsVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKI 218

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2569209806 362 TSTLAMLNFGQSAIFSVGLTAIMVLASKGIMSGTMTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQAL 429
Cdd:cd18552   219 ARARALSSPLMELLGAIAIALVLWYGGYQVISGELTPGEFISFITALLLLYQPIKRLSNVNANLQRGL 286
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
476-716 6.14e-12

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 66.71  E-value: 6.14e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 476 QKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDV---GLESLRKAVGVVPQDAVLFHN- 551
Cdd:PRK11831   20 RCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMsrsRLYTVRKRMSMLFQSGALFTDm 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 552 TIFYNLMYGNINATA--EDVYRVARL-----AGIHDAILKMPHkydtqvgerglKLSGGEKQRVAIARAILKNPPILLYD 624
Cdd:PRK11831  100 NVFDNVAYPLREHTQlpAPLLHSTVMmkleaVGLRGAAKLMPS-----------ELSGGMARRAALARAIALEPDLIMFD 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 625 EATSSLDSVTEENILTSMKEMVKDR--TSVFIAHRLSTIVD-ADEIIVLNQGKVAERGnhqtlldTPGSLYANlwNTQNS 701
Cdd:PRK11831  169 EPFVGQDPITMGVLVKLISELNSALgvTCVVVSHDVPEVLSiADHAYIVADKKIVAHG-------SAQALQAN--PDPRV 239

                         250
                  ....*....|....*
gi 2569209806 702 RILSNGSKPEPVPER 716
Cdd:PRK11831  240 RQFLDGIADGPVPFR 254
PLN03211 PLN03211
ABC transporter G-25; Provisional
 471-674 7.06e-12

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 68.75  E-value: 7.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 471 EYLEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTivrLLFRFYEPQQGNIYIAG--QNIRDVGLESLRKaVGVVPQDAVL 548
Cdd:PLN03211   76 RQIQERTILNGVTGMASPGEILAVLGPSGSGKST---LLNALAGRIQGNNFTGTilANNRKPTKQILKR-TGFVTQDDIL 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 549 F-HNTIFYNLMYGNINATAEDVYRVARLAGIHDAI--LKMPHKYDTQVGERGLK-LSGGEKQRVAIARAILKNPPILLYD 624
Cdd:PLN03211  152 YpHLTVRETLVFCSLLRLPKSLTKQEKILVAESVIseLGLTKCENTIIGNSFIRgISGGERKRVSIAHEMLINPSLLILD 231

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2569209806 625 EATSSLDSVTEENILTSMKEMV-KDRTSVFIAHRLSTIVDA--DEIIVLNQGK 674
Cdd:PLN03211  232 EPTSGLDATAAYRLVLTLGSLAqKGKTIVTSMHQPSSRVYQmfDSVLVLSEGR 284
ABC_6TM_bac_exporter_ABCB8_10_like cd18576
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ...
 134-429 7.10e-12

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: 66.74  E-value: 7.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 134 SLSLLAGAKITNVMVPFMFKYAVDSLNQmSGHMLNLsdapNTVVTMATAVLIGygvsrtgSALFNELRNAVFGKVAQSSI 213
Cdd:cd18576     1 GLILLLLSSAIGLVFPLLAGQLIDAALG-GGDTASL----NQIALLLLGLFLL-------QAVFSFFRIYLFARVGERVV 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 214 RRIAKNVFLHLHNLDLGFHLSRQTGALSKaidRGTRGISFVLSALVFNLGPTLFEMMLVSG---ILYYKcGGHFALVTLG 290
Cdd:cd18576    69 ADLRKDLYRHLQRLPLSFFHERRVGELTS---RLSNDVTQIQDTLTTTLAEFLRQILTLIGgvvLLFFI-SWKLTLLMLA 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 291 TLSAYTAftVAVTQWRTQFRIEMNKADN--EAGNAAIDSLLNYETVKYFNNEKYEAERYDGFLKVYESSSLKTTSTLAML 368
Cdd:cd18576   145 TVPVVVL--VAVLFGRRIRKLSKKVQDElaEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALF 222

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2569209806 369 NFGQSAIFSVGLTAIMVLASKGIMSGTMTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQAL 429
Cdd:cd18576   223 SSFIIFLLFGAIVAVLWYGGRLVLAGELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKAL 283
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
 476-631 7.45e-12

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 66.29  E-value: 7.45e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 476 QKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIyiagqnIRDVGLEslrkaVGVVPQ----DAVL-FH 550
Cdd:PRK09544   17 RRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI------KRNGKLR-----IGYVPQklylDTTLpLT 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 551 NTIFYNLMYGNINATAEDVYRVARLAGIHDAILKmphkydtqvgerglKLSGGEKQRVAIARAILKNPPILLYDEATSSL 630
Cdd:PRK09544   86 VNRFLRLRPGTKKEDILPALKRVQAGHLIDAPMQ--------------KLSGGETQRVLLARALLNRPQLLVLDEPTQGV 151


                  .
gi 2569209806 631 D 631
Cdd:PRK09544  152 D 152
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
 472-653 9.62e-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: 65.89  E-value: 9.62e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 472 YLEGQKVLNGVSFEVPAG-----KKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIyiagqnirdvglESLRKAVGVVPQDA 546
Cdd:cd03237     3 YPTMKKTLGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI------------EIELDTVSYKPQYI 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 547 VLFHNTIFYNLMYGNINATAEDVYRVARLAGIhdaiLKMPHKYDTQVGErglkLSGGEKQRVAIARAILKNPPILLYDEA 626
Cdd:cd03237    71 KADYEGTVRDLLSSITKDFYTHPYFKTEIAKP----LQIEQILDREVPE----LSGGELQRVAIAACLSKDADIYLLDEP 142

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2569209806 627 TSSLDS----------------------VTEENILtsMKEMVKDRTSVF 653
Cdd:cd03237   143 SAYLDVeqrlmaskvirrfaennektafVVEHDII--MIDYLADRLIVF 189
3a01203 TIGR00954
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...
 455-659 1.01e-11

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


Pssm-ID: 273360 [Multi-domain]  Cd Length: 659  Bit Score: 68.24  E-value: 1.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 455 IVTPQEATIRFEDVYFEYLEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLF--------RFYEPQQGNIYIAGQN 526
Cdd:TIGR00954 444 IVEYQDNGIKFENIPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGelwpvyggRLTKPAKGKLFYVPQR 523

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 527 IRdVGLESLRkavgvvpqDAVLFHNTIFYNLMYGNINATAEDVYRVARLagihDAILKMPHKYDTqVGERGLKLSGGEKQ 606
Cdd:TIGR00954 524 PY-MTLGTLR--------DQIIYPDSSEDMKRRGLSDKDLEQILDNVQL----THILEREGGWSA-VQDWMDVLSGGEKQ 589

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2569209806 607 RVAIARAILKNPPILLYDEATSSLDSVTEENILTSMKEMvkdRTSVF-IAHRLS 659
Cdd:TIGR00954 590 RIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREF---GITLFsVSHRKS 640
ABC_6TM_TAP cd18572
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ...
 134-429 1.05e-11

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


Pssm-ID: 350016 [Multi-domain]  Cd Length: 289  Bit Score: 66.41  E-value: 1.05e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 134 SLSLLAGAKITNVMVPFMFKYAVDSLNQMSGHMlnlsdapntVVTMATAVLIGYGVsrtGSALFNELRNAVFGKVAQSSI 213
Cdd:cd18572     1 AFVFLVVAALSELAIPHYTGAVIDAVVADGSRE---------AFYRAVLLLLLLSV---LSGLFSGLRGGCFSYAGTRLV 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 214 RRIAKNVFLHLHNLDLGFHLSRQTGAL--------SKAIDRGTRGISFVLSALVFNLGPTLFeMMLVSGILyykcgghfA 285
Cdd:cd18572    69 RRLRRDLFRSLLRQDIAFFDATKTGELtsrltsdcQKVSDPLSTNLNVFLRNLVQLVGGLAF-MFSLSWRL--------T 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 286 LVTLGTLSAYTAFTVAVTQWRTQFRIEMNKADNEAGNAAIDSLLNYETVKYFNNEKYEAERYDGFLKVYESSSLKTtstl 365
Cdd:cd18572   140 LLAFITVPVIALITKVYGRYYRKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQ---- 215

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 366 AMLNFGQSAIFSVGLTAIMVLA----SKGIMSGTMTVGDLVMVngLLFQLSL--PLNFLGTVYRETRQAL 429
Cdd:cd18572   216 ALAYAGYVAVNTLLQNGTQVLVlfygGHLVLSGRMSAGQLVTF--MLYQQQLgeAFQSLGDVFSSLMQAV 283
ABC_6TM_TmrA_like cd18544
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ...
 131-403 1.43e-11

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: 65.87  E-value: 1.43e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 131 VVISLSLLAGAKITNVMVPFMFKYAVDslnqmsGHMLNLSDAPNTVVTMAtavlIGYGVSRTGSALFNELRNAVFGKVAQ 210
Cdd:cd18544     1 FILALLLLLLATALELLGPLLIKRAID------DYIVPGQGDLQGLLLLA----LLYLGLLLLSFLLQYLQTYLLQKLGQ 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 211 SSIRRIAKNVFLHLHNLDLGFHLSRQTGALSkaidrgTR--------------GISFVLSALVFNLGpTLFEMMLVSGIL 276
Cdd:cd18544    71 RIIYDLRRDLFSHIQRLPLSFFDRTPVGRLV------TRvtndtealnelftsGLVTLIGDLLLLIG-ILIAMFLLNWRL 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 277 yykcgghfALVTLGTLsaytAFTVAVTQWrtqFRIEMNKADNE--AGNAAIDSLLNyE------TVKYFNNEKYEAERYD 348
Cdd:cd18544   144 --------ALISLLVL----PLLLLATYL---FRKKSRKAYREvrEKLSRLNAFLQ-EsisgmsVIQLFNREKREFEEFD 207

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2569209806 349 GFLKVYESSSLKTTSTLAMLNFGQSAIFSVGLTAIMVLASKGIMSGTMTVGDLVM 403
Cdd:cd18544   208 EINQEYRKANLKSIKLFALFRPLVELLSSLALALVLWYGGGQVLSGAVTLGVLYA 262
ABC_6TM_exporter_like cd18565
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
 131-421 2.56e-11

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


Pssm-ID: 350009 [Multi-domain]  Cd Length: 313  Bit Score: 65.28  E-value: 2.56e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 131 VVISLSLLAGAKITNVMVPFMFKYAVDS--LNQMSGHMLNLSDAPNT-----VVTMATAVLIGYGVSrtgsALFNELRNA 203
Cdd:cd18565     1 LVLGLLASILNRLFDLAPPLLIGVAIDAvfNGEASFLPLVPASLGPAdprgqLWLLGGLTVAAFLLE----SLFQYLSGV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 204 VFGKVAQSSIRRIAKNVFLHLHNLDLGFHLSRQTG----ALSKAIDRGTRGISFVLSALVfnlgpTLFEMMLVSGILYYK 279
Cdd:cd18565    77 LWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGdlmsVLNNDVNQLERFLDDGANSII-----RVVVTVLGIGAILFY 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 280 CGGHFALVTLGTLSAYTAFTvavtqWRTQFRIEMNKAD--NEAG--NAAI-DSLLNYETVKYFNNEKYEAER-------- 346
Cdd:cd18565   152 LNWQLALVALLPVPLIIAGT-----YWFQRRIEPRYRAvrEAVGdlNARLeNNLSGIAVIKAFTAEDFERERvadaseey 226

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2569209806 347 YDGFLKVYESSSLKTTSTLAMLNFGQSAIFSVGltAIMVLASKGIMSGTMTVGDLVMVNGLLFQLSLPLNFLGTV 421
Cdd:cd18565   227 RDANWRAIRLRAAFFPVIRLVAGAGFVATFVVG--GYWVLDGPPLFTGTLTVGTLVTFLFYTQRLLWPLTRLGDL 299
ABC_6TM_TAP_ABCB8_10_like cd18557
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ...
 135-429 2.70e-11

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: 64.89  E-value: 2.70e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 135 LSLLAGAKITNVMVPFMFKYAVDSLNQMSghmlNLSDAPNTVVTMATAVLIgygvsrtgSALFNELRNAVFGKVAQSSIR 214
Cdd:cd18557     2 LLFLLISSAAQLLLPYLIGRLIDTIIKGG----DLDVLNELALILLAIYLL--------QSVFTFVRYYLFNIAGERIVA 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 215 RIAKNVFLHLHNLDLGFHLSRQTGALskaIDRGTRGISFVLSALVFNLGPTLFEMMLVSG------ILYYKcgghFALVT 288
Cdd:cd18557    70 RLRRDLFSSLLRQEIAFFDKHKTGEL---TSRLSSDTSVLQSAVTDNLSQLLRNILQVIGgliilfILSWK----LTLVL 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 289 LGTLSAYTAFTVAVTQWRTQFRIEMNKADNEAGNAAIDSLLNYETVKYFNNEKYEAERYDGFLKVYESSSLKTTSTLAML 368
Cdd:cd18557   143 LLVIPLLLIASKIYGRYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALF 222

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2569209806 369 NFGQSAIFSVGLTAIMVLASKGIMSGTMTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQAL 429
Cdd:cd18557   223 QGITSLLIYLSLLLVLWYGGYLVLSGQLTVGELTSFILYTIMVASSVGGLSSLLADIMKAL 283
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 489-668 4.63e-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: 61.62  E-value: 4.63e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806  489 GKKVAIVGGSGSGKSTIVRLLFRFYEPQQGN-IYIAGQNIRDVGLESLRKavgvvpqdavlfhntifynlmygninatae 567
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPGGGvIYIDGEDILEEVLDQLLL------------------------------ 51

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806  568 dvyrvarlagihdailkmphkydTQVGERGLKLSGGEKQRVAIARAILKNPPILLYDEATSSLDSVTEENIL------TS 641
Cdd:smart00382  52 -----------------------IIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleelrLL 108

                          170       180
                   ....*....|....*....|....*..
gi 2569209806  642 MKEMVKDRTSVFIAHRLSTIVDADEII 668
Cdd:smart00382 109 LLLKSEKNLTVILTTNDEKDLGPALLR 135
ABC_6TM_Pgp_ABCB1_D1_like cd18577
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ...
 135-404 4.71e-11

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: 64.42  E-value: 4.71e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 135 LSLLAGAkitnvMVPFM---FKYAVDSLNQMSGHMLNLSDAPNTVvTMATAVLIGYGVsrtGSALFNELRNAVFGKVAQS 211
Cdd:cd18577     7 AAIAAGA-----ALPLMtivFGDLFDAFTDFGSGESSPDEFLDDV-NKYALYFVYLGI---GSFVLSYIQTACWTITGER 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 212 SIRRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTR----GISFVLSALVFNLGptlfemMLVSGI---LYYkcGGHF 284
Cdd:cd18577    78 QARRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNliqdGIGEKLGLLIQSLS------TFIAGFiiaFIY--SWKL 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 285 ALVTLGTLSAYTAFTVAVTQWRTQFRIEMNKADNEAGNAAIDSLLNYETVKYFNNEKYEAERYDGFLKVYESSSLKTTST 364
Cdd:cd18577   150 TLVLLATLPLIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLV 229

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 2569209806 365 LAmlnFGQSAIFSVgLTAIMVLA----SKGIMSGTMTVGDLVMV 404
Cdd:cd18577   230 SG---LGLGLLFFI-IFAMYALAfwygSRLVRDGEISPGDVLTV 269
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
 477-675 4.72e-11

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


Pssm-ID: 131681 [Multi-domain]  Cd Length: 500  Bit Score: 66.00  E-value: 4.72e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 477 KVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQ-QGNIYIAGQ--NIRDVgLESLRKAVGVVPQD-------- 545
Cdd:TIGR02633 274 KRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKpvDIRNP-AQAIRAGIAMVPEDrkrhgivp 352

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 546 -AVLFHNTIFYNL----MYGNINATAEdvyRVARLAGIHDAILKMPHKyDTQVGerglKLSGGEKQRVAIARAILKNPPI 620
Cdd:TIGR02633 353 iLGVGKNITLSVLksfcFKMRIDAAAE---LQIIGSAIQRLKVKTASP-FLPIG----RLSGGNQQKAVLAKMLLTNPRV 424

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2569209806 621 LLYDEATSSLDSVTEENILTSMKEMVKDRTS-VFIAHRLSTIVD-ADEIIVLNQGKV 675
Cdd:TIGR02633 425 LILDEPTRGVDVGAKYEIYKLINQLAQEGVAiIVVSSELAEVLGlSDRVLVIGEGKL 481
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
 477-675 7.56e-11

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: 62.28  E-value: 7.56e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 477 KVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEpqqGNIYIAGqNIRDVGLESLrkavgvvpQDAVLFHNTIFYN 556
Cdd:cd03233    21 PILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTE---GNVSVEG-DIHYNGIPYK--------EFAEKYPGEIIYV 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 557 lmygninaTAEDVyrvarlagiHDAILKMPHKYDTQVGERG----LKLSGGEKQRVAIARAILKNPPILLYDEATSSLDS 632
Cdd:cd03233    89 --------SEEDV---------HFPTLTVRETLDFALRCKGnefvRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDS 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2569209806 633 VTEENILTSMKEMVKD-RTSVFIAhrLS----TIVDA-DEIIVLNQGKV 675
Cdd:cd03233   152 STALEILKCIRTMADVlKTTTFVS--LYqasdEIYDLfDKVLVLYEGRQ 198
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
 475-674 1.99e-10

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 63.98  E-value: 1.99e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 475 GQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIR-DVGLESLRKAVGVVPQDAVLF-HNT 552
Cdd:PRK10982   10 GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQELNLVlQRS 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 553 IFYNLMYGN-----INATAEDVYRVARlaGIHDAIlkmphKYDTQVGERGLKLSGGEKQRVAIARAILKNPPILLYDEAT 627
Cdd:PRK10982   90 VMDNMWLGRyptkgMFVDQDKMYRDTK--AIFDEL-----DIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPT 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2569209806 628 SSLdSVTEENILTSMKEMVKDRTS--VFIAHRLSTIVD-ADEIIVLNQGK 674
Cdd:PRK10982  163 SSL-TEKEVNHLFTIIRKLKERGCgiVYISHKMEEIFQlCDEITILRDGQ 211
ABC_6TM_Rv0194_D1_like cd18543
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ...
 131-428 2.18e-10

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: 62.50  E-value: 2.18e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 131 VVISLSLLAGAKITNVMVPFMFKYAVDSLnqmsghmlnLSDAPNTVVTMATAVLIGYGVSRtgsALFNELRNAVFGKVA- 209
Cdd:cd18543     1 LILALLAALLATLAGLAIPLLTRRAIDGP---------IAHGDRSALWPLVLLLLALGVAE---AVLSFLRRYLAGRLSl 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 210 --QSSIRRiakNVFLHLHNLDLGFHLSRQTGAL-SKAI-DRGTrgISFVLSALVFNLGPTLfeMMLVSGILYykcgghFA 285
Cdd:cd18543    69 gvEHDLRT---DLFAHLQRLDGAFHDRWQSGQLlSRATsDLSL--VQRFLAFGPFLLGNLL--TLVVGLVVM------LV 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 286 L---VTLGTLSAYTAFTVAVTQWRTQFRIEMNKADNEAGNAA--ID-SLLNYETVKYFNNEKYEAERYDGFLKVYESSSL 359
Cdd:cd18543   136 LsppLALVALASLPPLVLVARRFRRRYFPASRRAQDQAGDLAtvVEeSVTGIRVVKAFGRERRELDRFEAAARRLRATRL 215

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2569209806 360 KTTSTLAMLNFGQSAIFSVGLTAIMVLASKGIMSGTMTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQA 428
Cdd:cd18543   216 RAARLRARFWPLLEALPELGLAAVLALGGWLVANGSLTLGTLVAFSAYLTMLVWPVRMLGWLLAMAQRA 284
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
 567-674 2.95e-10

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


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 63.97  E-value: 2.95e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806  567 EDVYRvARLAGIHDAILKMPHKYDTQVGE---RGLklSGGEKQRVAIARAILKNPPILLYDEATSSLDSVTEENILTSMK 643
Cdd:TIGR00956  177 REEYA-KHIADVYMATYGLSHTRNTKVGNdfvRGV--SGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALK 253

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 2569209806  644 EMVK--DRTSVFIAHRLSTivDA----DEIIVLNQGK 674
Cdd:TIGR00956  254 TSANilDTTPLVAIYQCSQ--DAyelfDKVIVLYEGY 288
GguA NF040905
sugar ABC transporter ATP-binding protein;
475-677 3.53e-10

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 62.88  E-value: 3.53e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 475 GQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYePQ---QGNIYIAGQ-----NIRDvgleSLRKAVGVVPQD- 545
Cdd:NF040905   13 GVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGEvcrfkDIRD----SEALGIVIIHQEl 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 546 AVLFHNTIFYNLMYGNINATA-----EDVYRVAR--LA--GIHDAilkmPhkyDTQVGERGLklsgGEKQRVAIARAILK 616
Cdd:NF040905   88 ALIPYLSIAENIFLGNERAKRgvidwNETNRRARelLAkvGLDES----P---DTLVTDIGV----GKQQLVEIAKALSK 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2569209806 617 NPPILLYDEATSSL---DSvteENILTSMKEMvKDR--TSVFIAHRLSTIVD-ADEIIVLNQGKVAE 677
Cdd:NF040905  157 DVKLLILDEPTAALneeDS---AALLDLLLEL-KAQgiTSIIISHKLNEIRRvADSITVLRDGRTIE 219
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
471-673 5.65e-10

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 62.49  E-value: 5.65e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 471 EYLEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQ--NIRDVGLeSLRKAVGVVPQD-AV 547
Cdd:PRK09700   13 KSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNInyNKLDHKL-AAQLGIGIIYQElSV 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 548 LFHNTIFYNLMYGN--------INATaeDVYRVARLAGIHDAILKMPHKYDTQVGErglkLSGGEKQRVAIARAILKNPP 619
Cdd:PRK09700   92 IDELTVLENLYIGRhltkkvcgVNII--DWREMRVRAAMMLLRVGLKVDLDEKVAN----LSISHKQMLEIAKTLMLDAK 165

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2569209806 620 ILLYDEATSSLDSVTEENILTSMKEMVKDRTS-VFIAHRLSTIVD-ADEIIVLNQG 673
Cdd:PRK09700  166 VIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAiVYISHKLAEIRRiCDRYTVMKDG 221
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
 480-674 7.52e-10

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


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 60.39  E-value: 7.52e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 480 NGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRdvGLESLRKA-VGVVP--QDAVLFHN-TIFY 555
Cdd:PRK11300   22 NNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIE--GLPGHQIArMGVVRtfQHVRLFREmTVIE 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 556 NLMygninataedvyrVAR----LAGIHDAILKMP--HKYDTQVGER--------GLK---------LSGGEKQRVAIAR 612
Cdd:PRK11300  100 NLL-------------VAQhqqlKTGLFSGLLKTPafRRAESEALDRaatwlervGLLehanrqagnLAYGQQRRLEIAR 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2569209806 613 AILKNPPILLYDEATSSLD-SVTEEniLTSMKEMVKDRTSV---FIAHRLSTIVD-ADEIIVLNQGK 674
Cdd:PRK11300  167 CMVTQPEILMLDEPAAGLNpKETKE--LDELIAELRNEHNVtvlLIEHDMKLVMGiSDRIYVVNQGT 231
tagH PRK13545
teichoic acids export protein ATP-binding subunit; Provisional
 464-733 7.72e-10

teichoic acids export protein ATP-binding subunit; Provisional


Pssm-ID: 184130 [Multi-domain]  Cd Length: 549  Bit Score: 62.22  E-value: 7.72e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 464 RFEDVYFEYLEGQ--KVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYI----------AGQNIRDVG 531
Cdd:PRK13545   23 KLKDLFFRSKDGEyhYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIkgsaaliaisSGLNGQLTG 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 532 LEslrkavgvvpqdavlfhNTIFYNLMYGNINATAEDVY-RVARLAGIHDAILKMPHKYdtqvgerglklSGGEKQRVAI 610
Cdd:PRK13545  103 IE-----------------NIELKGLMMGLTKEKIKEIIpEIIEFADIGKFIYQPVKTY-----------SSGMKSRLGF 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 611 ARAILKNPPILLYDEATSSLDSVTEENILTSMKEMV-KDRTSVFIAHRLSTIVD-ADEIIVLNQGKVAERGNHQTLLDTP 688
Cdd:PRK13545  155 AISVHINPDILVIDEALSVGDQTFTKKCLDKMNEFKeQGKTIFFISHSLSQVKSfCTKALWLHYGQVKEYGDIKEVVDHY 234

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2569209806 689 GSLyanlwntqnsrilsngskpepVPERVSQKEEERKKLQEEIMN 733
Cdd:PRK13545  235 DEF---------------------LKKYNQMSVEERKDFREEQIS 258
ABC_6TM_ABCB10_like cd18573
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ...
 134-412 7.94e-10

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


Pssm-ID: 350017 [Multi-domain]  Cd Length: 294  Bit Score: 60.61  E-value: 7.94e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 134 SLSLLAGAKITNVMVPFMFKYAVDSLNQMSGHMLNLSDAPNTVVT-MATAVLIGygvsrtgsALFNELRNAVFGKVAQSS 212
Cdd:cd18573     1 ALALLLVSSAVTMSVPFAIGKLIDVASKESGDIEIFGLSLKTFALaLLGVFVVG--------AAANFGRVYLLRIAGERI 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 213 IRRIAKNVFLHLHNLDLGFHLSRQTGAL-----------SKAIdrgTRGISFVLSALVFNLGPTLFeMMLVSGILyykcg 281
Cdd:cd18573    73 VARLRKRLFKSILRQDAAFFDKNKTGELvsrlssdtsvvGKSL---TQNLSDGLRSLVSGVGGIGM-MLYISPKL----- 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 282 ghfALVTLGTLSAYTAFTVA------VTQWRTQfriemnKADNEAGNAAIDSLLNYETVKYFNNEKYEAERYDGflKVYE 355
Cdd:cd18573   144 ---TLVMLLVVPPIAVGAVFygryvrKLSKQVQ------DALADATKVAEERLSNIRTVRAFAAERKEVERYAK--KVDE 212

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2569209806 356 SSSLKTTSTLAMLNFGQSAIFSVGLTAIMVLASKGIM--SGTMTVGDL-------VMVNGLLFQLS 412
Cdd:cd18573   213 VFDLAKKEALASGLFFGSTGFSGNLSLLSVLYYGGSLvaSGELTVGDLtsflmyaVYVGSSVSGLS 278
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
 475-675 8.22e-10

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 61.87  E-value: 8.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 475 GQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQ-QGNIYIAGQ--NIR------DVGLESL---RKAVGVV 542
Cdd:PRK13549  274 HIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRwEGEIFIDGKpvKIRnpqqaiAQGIAMVpedRKRDGIV 353

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 543 PQDAVLfHNTIFYNL----MYGNINATAEdvyrvarLAGIHDAILKMPHKYDT---QVGerglKLSGGEKQRVAIARAIL 615
Cdd:PRK13549  354 PVMGVG-KNITLAALdrftGGSRIDDAAE-------LKTILESIQRLKVKTASpelAIA----RLSGGNQQKAVLAKCLL 421

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2569209806 616 KNPPILLYDEATSSLDSVTEENILTSMKEMVKDRTSV-FIAHRLSTIVD-ADEIIVLNQGKV 675
Cdd:PRK13549  422 LNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIiVISSELPEVLGlSDRVLVMHEGKL 483
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
 480-693 8.54e-10

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 60.89  E-value: 8.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 480 NGVSFEVPAGKKVAIVGGSGSGKS----TIVRLLFRfyepqqgNIYIAGQ---------NIRDVGLESLR-KAVGVVPQD 545
Cdd:PRK09473   33 NDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAA-------NGRIGGSatfngreilNLPEKELNKLRaEQISMIFQD 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 546 AVLFHN---TIFYNLM--------YGNINATAEDVyRVARLAGIHDAILKM---PHKYdtqvgerglklSGGEKQRVAIA 611
Cdd:PRK09473  106 PMTSLNpymRVGEQLMevlmlhkgMSKAEAFEESV-RMLDAVKMPEARKRMkmyPHEF-----------SGGMRQRVMIA 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 612 RAILKNPPILLYDEATSSLDSVTEENILTSMKEMVKD-RTS-VFIAHRLSTIVD-ADEIIVLNQGKVAERGNHQTLLDTP 688
Cdd:PRK09473  174 MALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAiIMITHDLGVVAGiCDKVLVMYAGRTMEYGNARDVFYQP 253


                  ....*
gi 2569209806 689 GSLYA 693
Cdd:PRK09473  254 SHPYS 258
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 463-679 1.39e-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: 1.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 463 IRFE----------DVYFEYLEGQKVLNGVSFEVPAGK-----KVAIVGGSGSGKSTIVRLLFRFYEPQQGNI------- 520
Cdd:COG1245   325 IEFEvhaprrekeeETLVEYPDLTKSYGGFSLEVEGGEiregeVLGIVGPNGIGKTTFAKILAGVLKPDEGEVdedlkis 404

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 521 ----YIAGQNIRDVGlESLRKAVGVVpqdavlFHNTIFYNlmygninataedvyRVARLAGIHdailKMphkYDTQVGEr 596
Cdd:COG1245   405 ykpqYISPDYDGTVE-EFLRSANTDD------FGSSYYKT--------------EIIKPLGLE----KL---LDKNVKD- 455

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 597 glkLSGGEKQRVAIARAILKNPPILLYDEATSSLDSvtEENILTS--MKEMV--KDRTSVFIAHRLsTIVD--ADEIIVL 670
Cdd:COG1245   456 ---LSGGELQRVAIAACLSRDADLYLLDEPSAHLDV--EQRLAVAkaIRRFAenRGKTAMVVDHDI-YLIDyiSDRLMVF 529


                  ....*....
gi 2569209806 671 NqGKVAERG 679
Cdd:COG1245   530 E-GEPGVHG 537
ABC_6TM_AtABCB27_like cd18780
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ...
 134-429 1.42e-09

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


Pssm-ID: 350053 [Multi-domain]  Cd Length: 295  Bit Score: 59.96  E-value: 1.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 134 SLSLLAGAkITNVMVPFMFKYAVDSLNQMSGhmlNLSDAPNTVVTMATAVLIGYGVsrtGSALFNELRNAVFGKVAQSSI 213
Cdd:cd18780     2 TIALLVSS-GTNLALPYFFGQVIDAVTNHSG---SGGEEALRALNQAVLILLGVVL---IGSIATFLRSWLFTLAGERVV 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 214 RRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGISfvlSALVFNLGPTLFEMMLVSG---ILYYKCgghfALVTLG 290
Cdd:cd18780    75 ARLRKRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQ---NAVTVNLSMLLRYLVQIIGglvFMFTTS----WKLTLV 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 291 TLSAYTAFTVAVTQW-------RTQFRIEMNKAdneaGNAAIDSLLNYETVKYFNNEKYEAERYDGflKVYESSSL--KT 361
Cdd:cd18780   148 MLSVVPPLSIGAVIYgkyvrklSKKFQDALAAA----STVAEESISNIRTVRSFAKETKEVSRYSE--KINESYLLgkKL 221

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2569209806 362 TSTLAMLNFGQSAIFSVGLTAIMVLASKGIMSGTMTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQAL 429
Cdd:cd18780   222 ARASGGFNGFMGAAAQLAIVLVLWYGGRLVIDGELTTGLLTSFLLYTLTVAMSFAFLSSLYGDFMQAV 289
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
 482-676 1.42e-09

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 61.22  E-value: 1.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 482 VSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGLESlRKAVGVV--PQD---------AVLFH 550
Cdd:PRK15439  282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ-RLARGLVylPEDrqssglyldAPLAW 360

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 551 NTifYNLMYGNINATAEDVYRVARLAGIHDAI-LKMPHKyDTQVGerglKLSGGEKQRVAIARAILKNPPILLYDEATSS 629
Cdd:PRK15439  361 NV--CALTHNRRGFWIKPARENAVLERYRRALnIKFNHA-EQAAR----TLSGGNQQKVLIAKCLEASPQLLIVDEPTRG 433

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2569209806 630 LDSVTEENILTSMKEMVKDRTSV-FIAHRLSTIVD-ADEIIVLNQGKVA 676
Cdd:PRK15439  434 VDVSARNDIYQLIRSIAAQNVAVlFISSDLEEIEQmADRVLVMHQGEIS 482
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
489-670 6.44e-09

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 59.05  E-value: 6.44e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 489 GKKVAIVGGSGSGKSTIVRLLfrfyepqqgniyiAGQNIRDVGleslrKAVGVVPQDAVLFH------NTIFYNLMYGNI 562
Cdd:PRK13409   99 GKVTGILGPNGIGKTTAVKIL-------------SGELIPNLG-----DYEEEPSWDEVLKRfrgtelQNYFKKLYNGEI 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 563 NA----------------TAEDVYRVARLAGIHDAI---LKMPHKYDTQVGErglkLSGGEKQRVAIARAILKNPPILLY 623
Cdd:PRK13409  161 KVvhkpqyvdlipkvfkgKVRELLKKVDERGKLDEVverLGLENILDRDISE----LSGGELQRVAIAAALLRDADFYFF 236

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2569209806 624 DEATSSLDSVTEENILTSMKEMVKDRTSVFIAHRLsTIVD--ADEIIVL 670
Cdd:PRK13409  237 DEPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDL-AVLDylADNVHIA 284
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
 479-668 1.02e-08

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


Pssm-ID: 213205 [Multi-domain]  Cd Length: 176  Bit Score: 55.41  E-value: 1.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 479 LNGVSFEVPAGKKVAIVGGSGSGKSTIVrllfrfyepQQGnIYIAGQNIrdvgLESLRKAVGvvpqdavlFHNTIFynlm 558
Cdd:cd03238    11 LQNLDVSIPLNVLVVVTGVSGSGKSTLV---------NEG-LYASGKAR----LISFLPKFS--------RNKLIF---- 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 559 ygninataedvyrVARLAgihdAILKMPHKYDTqVGERGLKLSGGEKQRVAIARAILKNPP--ILLYDEATSSLDSVTEE 636
Cdd:cd03238    65 -------------IDQLQ----FLIDVGLGYLT-LGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDIN 126

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2569209806 637 NILTSMKEMV-KDRTSVFIAHRLSTIVDADEII 668
Cdd:cd03238   127 QLLEVIKGLIdLGNTVILIEHNLDVLSSADWII 159
ABC_6TM_exporter_like cd18550
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
 131-429 1.67e-08

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


Pssm-ID: 349994 [Multi-domain]  Cd Length: 294  Bit Score: 56.72  E-value: 1.67e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 131 VVISLSLLAGAKITNVMVPFMFKYAVDS---------LNQMSGHMLNLsdapnTVVTMATAVLIGYGVSRTGSALFNELR 201
Cdd:cd18550     1 LALVLLLILLSALLGLLPPLLLREIIDDalpqgdlglLVLLALGMVAV-----AVASALLGVVQTYLSARIGQGVMYDLR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 202 NAVFGkvaqssirriaknvflHLHNLDLGFHLSRQTGAL-SK------AIDRG-TRGISFVLSALVfNLGPTLFEMMLVS 273
Cdd:cd18550    76 VQLYA----------------HLQRMSLAFFTRTRTGEIqSRlnndvgGAQSVvTGTLTSVVSNVV-TLVATLVAMLALD 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 274 GILyykcgghfALVTLGTLSAYTAFT--VAVTQWRTQfRIEMNKadneagNAAIDSLLNyET--------VKYFNNEKYE 343
Cdd:cd18550   139 WRL--------ALLSLVLLPLFVLPTrrVGRRRRKLT-REQQEK------LAELNSIMQ-ETlsvsgallVKLFGREDDE 202

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 344 AERYDGflKVYESSSLKTTSTLAMLNFGQ--SAIFSVGLTAIMVLASKGIMSGTMTVGDLVMVNGLLFQLSLPLNFLGTV 421
Cdd:cd18550   203 AARFAR--RSRELRDLGVRQALAGRWFFAalGLFTAIGPALVYWVGGLLVIGGGLTIGTLVAFTALLGRLYGPLTQLLNI 280


                  ....*...
gi 2569209806 422 YRETRQAL 429
Cdd:cd18550   281 QVDLMTSL 288
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
466-679 2.37e-08

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 57.51  E-value: 2.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 466 EDVYFEYLEGQKVLNGVSFEVPAGKK-----VAIVGGSGSGKSTIVRLLFRFYEPQQGNIyiagqnirdvgLESLRkaVG 540
Cdd:PRK13409  337 RETLVEYPDLTKKLGDFSLEVEGGEIyegevIGIVGPNGIGKTTFAKLLAGVLKPDEGEV-----------DPELK--IS 403

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 541 VVPQdavlfhntifynlmY--GNINATAEDVyrvarLAGIHDAI------------LKMPHKYDTQVGErglkLSGGEKQ 606
Cdd:PRK13409  404 YKPQ--------------YikPDYDGTVEDL-----LRSITDDLgssyykseiikpLQLERLLDKNVKD----LSGGELQ 460

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2569209806 607 RVAIARAILKNPPILLYDEATSSLDSvtEENILTS--MKEMV--KDRTSVFIAHRLSTIvD--ADEIIVLNqGKVAERG 679
Cdd:PRK13409  461 RVAIAACLSRDADLYLLDEPSAHLDV--EQRLAVAkaIRRIAeeREATALVVDHDIYMI-DyiSDRLMVFE-GEPGKHG 535
sufC PRK09580
cysteine desulfurase ATPase component; Reviewed
 473-681 2.47e-08

cysteine desulfurase ATPase component; Reviewed


Pssm-ID: 181965 [Multi-domain]  Cd Length: 248  Bit Score: 55.57  E-value: 2.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 473 LEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLF--RFYEPQQGNIYIAGQNIRDVGLESlRKAVGVV-----PQD 545
Cdd:PRK09580   11 VEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDLLELSPED-RAGEGIFmafqyPVE 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 546 AVLFHNTIFYNLmygNINATAE-------DVYRVARLAGIHDAILKMPHKYDTQVGERGlkLSGGEKQRVAIARAILKNP 618
Cdd:PRK09580   90 IPGVSNQFFLQT---ALNAVRSyrgqeplDRFDFQDLMEEKIALLKMPEDLLTRSVNVG--FSGGEKKRNDILQMAVLEP 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2569209806 619 PILLYDEATSSLDsVTEENILTSMKEMVKDRTSVFIA----HRLSTIVDADEIIVLNQGKVAERGNH 681
Cdd:PRK09580  165 ELCILDESDSGLD-IDALKIVADGVNSLRDGKRSFIIvthyQRILDYIKPDYVHVLYQGRIVKSGDF 230
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
 475-631 3.16e-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: 56.87  E-value: 3.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 475 GQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAgQNIRdvgleslrkaVGVVPQDAVLFHN-TI 553
Cdd:TIGR03719  17 KKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQ-PGIK----------VGYLPQEPQLDPTkTV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 554 FYNLMYG-----NINATAEDVY---------------RVARLAGIHDAI---------------LKMPhKYDTQVGergl 598
Cdd:TIGR03719  86 RENVEEGvaeikDALDRFNEISakyaepdadfdklaaEQAELQEIIDAAdawdldsqleiamdaLRCP-PWDADVT---- 160

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2569209806 599 KLSGGEKQRVAIARAILKNPPILLYDEATSSLD 631
Cdd:TIGR03719 161 KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD 193
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
461-656 3.91e-08

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 54.04  E-value: 3.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 461 ATIRFEDVYFEylegqkvlnGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGLEslrkavg 540
Cdd:PRK13538    8 ACERDERILFS---------GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDE------- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 541 vvpqdavlFHntifYNLMY-GNINA-----TAEDVYRV-ARLAG------IHDAIlkmphkydTQVGERGLK------LS 601
Cdd:PRK13538   72 --------YH----QDLLYlGHQPGiktelTALENLRFyQRLHGpgddeaLWEAL--------AQVGLAGFEdvpvrqLS 131

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2569209806 602 GGEKQRVAIARAILKNPPILLYDEATSSLDsvteeniltsmKEMVKDRTSVFIAH 656
Cdd:PRK13538  132 AGQQRRVALARLWLTRAPLWILDEPFTAID-----------KQGVARLEALLAQH 175
ABC_6TM_HetC_like cd18568
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ...
 285-435 6.42e-08

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


Pssm-ID: 350012 [Multi-domain]  Cd Length: 294  Bit Score: 54.87  E-value: 6.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 285 ALVTLGTLSAYTAFTVAVTQWRTQFRIEMNKADNEAGNAAIDSLLNYETVKYFNNE-----KYEaERYDGFLKVYesssL 359
Cdd:cd18568   144 TLIVLAFIPLYVLLTLLSSPKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAErpirwRWE-NKFAKALNTR----F 218

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2569209806 360 KTTSTLAMLNFGQSAIFSVGLTAIMVLASKGIMSGTMTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDMNTL 435
Cdd:cd18568   219 RGQKLSIVLQLISSLINHLGTIAVLWYGAYLVISGQLTIGQLVAFNMLFGSVINPLLALVGLWDELQETRISVERL 294
ABC_6TM_Tm287_like cd18548
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ...
 131-421 6.59e-08

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


Pssm-ID: 349992 [Multi-domain]  Cd Length: 292  Bit Score: 54.71  E-value: 6.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 131 VVISLSLLAGAKITNVMVPFMFKYAVDS---------LNQMSGHMLNLsdapnTVVTMATAVLIGYGVSRTGSALFNELR 201
Cdd:cd18548     1 AILAPLFKLLEVLLELLLPTLMADIIDEgiangdlsyILRTGLLMLLL-----ALLGLIAGILAGYFAAKASQGFGRDLR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 202 NAVFGKVAQSSirriaknvflhLHNLDlgfHLSrqTGALskaIDRGTRGISFVLSALVFNL-----GPtlfeMMLVSGIL 276
Cdd:cd18548    76 KDLFEKIQSFS-----------FAEID---KFG--TSSL---ITRLTNDVTQVQNFVMMLLrmlvrAP----IMLIGAII 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 277 yykcgghFALVTLGTLSAYTAFTVAV---------TQWRTQFRI------EMNKADNEagnaaidSLLNYETVKYFNNEK 341
Cdd:cd18548   133 -------MAFRINPKLALILLVAIPIlalvvflimKKAIPLFKKvqkkldRLNRVVRE-------NLTGIRVIRAFNRED 198

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 342 YEAERYDGFLKVYESSSLKTTSTLAMLNFGQSAIFSVGLTAIMVLASKGIMSGTMTVGDLVMVNGLLFQLSLPLNFLGTV 421
Cdd:cd18548   199 YEEERFDKANDDLTDTSLKAGRLMALLNPLMMLIMNLAIVAILWFGGHLINAGSLQVGDLVAFINYLMQILMSLMMLSMV 278
ABC_6TM_PrtD_LapB_HlyB_like cd18566
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ...
 173-416 6.98e-08

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


Pssm-ID: 350010 [Multi-domain]  Cd Length: 294  Bit Score: 54.90  E-value: 6.98e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 173 PNTVVTMATAVLIGYGVSRTGSALFNELRNAVFGKVAQSSIRRIAKNVFLHLHNLDLGFHLSRQTGALskaIDRgtrgis 252
Cdd:cd18566    34 PNESIPTLQVLVIGVVIAILLESLLRLLRSYILAWIGARFDHRLSNAAFEHLLSLPLSFFEREPSGAH---LER------ 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 253 fvLSALV----FNLGPTLFEMM-----LVSGILYYKCGGHFALVTLGTLSAYTAFTVAV-TQWRTQFRiEMNKADNEAGN 322
Cdd:cd18566   105 --LNSLEqireFLTGQALLALLdlpfvLIFLGLIWYLGGKLVLVPLVLLGLFVLVAILLgPILRRALK-ERSRADERRQN 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 323 AAIDSLLNYETVKYFNNEKYEAERYDGFLKVYESSSLKTTSTLAMLNfGQSAIFSVgLTAIMVLA--SKGIMSGTMTVGD 400
Cdd:cd18566   182 FLIETLTGIHTIKAMAMEPQMLRRYERLQANAAYAGFKVAKINAVAQ-TLGQLFSQ-VSMVAVVAfgALLVINGDLTVGA 259

                         250
                  ....*....|....*.
gi 2569209806 401 LVMVNGLLFQLSLPLN 416
Cdd:cd18566   260 LIACTMLSGRVLQPLQ 275
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
 452-676 1.36e-07

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 54.74  E-value: 1.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 452 PPLIVTPQEATIRFEDVYfeyLEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRD-V 530
Cdd:PRK10982  240 PDKENKPGEVILEVRNLT---SLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNhN 316

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 531 GLESL----------RKAVGVVPQDAVLFhNTIFYNL-MYGNINATAEDVYRVARLAGIHDAI-LKMPhKYDTQVGErgl 598
Cdd:PRK10982  317 ANEAInhgfalvteeRRSTGIYAYLDIGF-NSLISNIrNYKNKVGLLDNSRMKSDTQWVIDSMrVKTP-GHRTQIGS--- 391

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 599 kLSGGEKQRVAIARAILKNPPILLYDEATSSLDSVTEENILTSMKEMV-KDRTSVFIAHRLSTIVD-ADEIIVLNQGKVA 676
Cdd:PRK10982  392 -LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAkKDKGIIIISSEMPELLGiTDRILVMSNGLVA 470
ABC_6TM_TmrB_like cd18541
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ...
 132-419 1.39e-07

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


Pssm-ID: 349985 [Multi-domain]  Cd Length: 293  Bit Score: 53.95  E-value: 1.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 132 VISLSLLAGAKITNVMVPFMFKYAVDSLNQMSghmLNLSDAPNTVVTMATAVLIGYgVSRTGSalfnelRNAVFGkvaqs 211
Cdd:cd18541     2 LLGILFLILVDLLQLLIPRIIGRAIDALTAGT---LTASQLLRYALLILLLALLIG-IFRFLW------RYLIFG----- 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 212 SIRRIAK----NVFLHLHNLDLGFHLSRQTGAL-SKAI-DrgtrgisfvLSALVFNLGPTLfeMMLVSGILYykcgGHFA 285
Cdd:cd18541    67 ASRRIEYdlrnDLFAHLLTLSPSFYQKNRTGDLmARATnD---------LNAVRMALGPGI--LYLVDALFL----GVLV 131

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 286 LVTLGTLSAY-TAFTVA-------VTQW-----RTQFRI------EMNkadneagNAAIDSLLNYETVKYFNNEKYEAER 346
Cdd:cd18541   132 LVMMFTISPKlTLIALLplpllalLVYRlgkkiHKRFRKvqeafsDLS-------DRVQESFSGIRVIKAFVQEEAEIER 204

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2569209806 347 YDGFLKVYESSSLKTTSTLAMlnFGQSAIFSVGLTAIMVLA--SKGIMSGTMTVGDLVMVNGLLFQLSLPLNFLG 419
Cdd:cd18541   205 FDKLNEEYVEKNLRLARVDAL--FFPLIGLLIGLSFLIVLWygGRLVIRGTITLGDLVAFNSYLGMLIWPMMALG 277
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 489-670 1.48e-07

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


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 54.79  E-value: 1.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 489 GKKVAIVGGSGSGKSTIVRLLfrfyepqqgniyiAGQ---NIRDVGLEslrkavgvVPQDAVL--FHNTI----FYNLMY 559
Cdd:COG1245    99 GKVTGILGPNGIGKSTALKIL-------------SGElkpNLGDYDEE--------PSWDEVLkrFRGTElqdyFKKLAN 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 560 GNINAT--AEDVYRVAR-LAGIHDAILKmphKYDtqvgERGL-------------------KLSGGEKQRVAIARAILKN 617
Cdd:COG1245   158 GEIKVAhkPQYVDLIPKvFKGTVRELLE---KVD----ERGKldelaeklglenildrdisELSGGELQRVAIAAALLRD 230

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2569209806 618 PPILLYDEATSSLDsVTEE-NILTSMKEMVKDRTSVFIA-HRLsTIVD--ADEIIVL 670
Cdd:COG1245   231 ADFYFFDEPSSYLD-IYQRlNVARLIRELAEEGKYVLVVeHDL-AILDylADYVHIL 285
PLN03073 PLN03073
ABC transporter F family; Provisional
 458-676 1.62e-07

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 54.87  E-value: 1.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 458 PQEATIRFEDVYFEYLEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYiagqnirdvglESLRK 537
Cdd:PLN03073  504 PGPPIISFSDASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF-----------RSAKV 572

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 538 AVGVVPQDAV----LFHNTIFYnlMYGNINATAEDVYRvARLA--GIHDAILKMPHkydtqvgergLKLSGGEKQRVAIA 611
Cdd:PLN03073  573 RMAVFSQHHVdgldLSSNPLLY--MMRCFPGVPEQKLR-AHLGsfGVTGNLALQPM----------YTLSGGQKSRVAFA 639

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2569209806 612 RAILKNPPILLYDEATSSLDSVTEENILTSMkeMVKDRTSVFIAHRLSTIVDA-DEIIVLNQGKVA 676
Cdd:PLN03073  640 KITFKKPHILLLDEPSNHLDLDAVEALIQGL--VLFQGGVLMVSHDEHLISGSvDELWVVSEGKVT 703
ABC_6TM_CyaB_HlyB_like cd18588
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ...
 220-435 2.00e-07

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: 53.27  E-value: 2.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 220 VFLHLHNLDLGFHLSRQTG-------------------ALSKAIDrgtrgisfVLSALVFnlgptLFEMMLVSGILyykc 280
Cdd:cd18588    81 LFRHLLRLPLSYFESRQVGdtvarvrelesirqfltgsALTLVLD--------LVFSVVF-----LAVMFYYSPTL---- 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 281 gghfALVTLGTLSAYTAFTVAVT---QWRTQFRIEMNkADNEAGNaaIDSLLNYETVKYFNNEKYEAERYDGFLKVYESS 357
Cdd:cd18588   144 ----TLIVLASLPLYALLSLLVTpilRRRLEEKFQRG-AENQSFL--VETVTGIETVKSLAVEPQFQRRWEELLARYVKA 216

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2569209806 358 SLKTTSTLAMLNFGQSAIFSVGLTAIMVLASKGIMSGTMTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDMNTL 435
Cdd:cd18588   217 SFKTANLSNLASQIVQLIQKLTTLAILWFGAYLVMDGELTIGQLIAFNMLAGQVSQPVLRLVQLWQDFQQAKVSVERL 294
ABC_6TM_LmrA_like cd18551
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ...
 131-429 2.02e-07

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


Pssm-ID: 349995 [Multi-domain]  Cd Length: 289  Bit Score: 53.21  E-value: 2.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 131 VVISLSLLAGAkiTNVMVPFMFKYAVDSLNQMSGHMlnlsdapNTVVTMATAVLigygvsrtGSALFNELRNAVFGKVAQ 210
Cdd:cd18551     3 LALLLSLLGTA--ASLAQPLLVKNLIDALSAGGSSG-------GLLALLVALFL--------LQAVLSALSSYLLGRTGE 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 211 SSIRRIAKNVFLHLHNLDLGFHLSRQTG-----------ALSKAIDRGTrgISFVLSALVFnLGpTLFEMMLVSGILyyk 279
Cdd:cd18551    66 RVVLDLRRRLWRRLLRLPVSFFDRRRSGdlvsrvtndttLLRELITSGL--PQLVTGVLTV-VG-AVVLMFLLDWVL--- 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 280 cgghfALVTLGTLSAYTAFTVAVTQWRTQFRIEMNKADNEAGNAAIDSLLNYETVKYFNNEKYEAERYDGFLKVYESSSL 359
Cdd:cd18551   139 -----TLVTLAVVPLAFLIILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGL 213

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2569209806 360 KTTSTLAMLnfgqSAIFSVGLTAIM--VLASKGIM--SGTMTVGDLV---MvngLLFQLSLPLNFLGTVYRETRQAL 429
Cdd:cd18551   214 KAAKIEALI----GPLMGLAVQLALlvVLGVGGARvaSGALTVGTLVaflL---YLFQLITPLSQLSSFFTQLQKAL 283
ABC_6TM_Tm288_like cd18547
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ...
 131-416 2.35e-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: 53.18  E-value: 2.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 131 VVISLSLLAGAKITNVMVPFMFKYAVDSLNQmsGHMLNLSDAPNTVVTMATAVLIGYGVSrtgsALFNELRNAVFGKVAQ 210
Cdd:cd18547     1 LILVIILAIISTLLSVLGPYLLGKAIDLIIE--GLGGGGGVDFSGLLRILLLLLGLYLLS----ALFSYLQNRLMARVSQ 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 211 SSIRRIAKNVFLHLHNLDLGFHLSRQTGA-LSKA---IDRGTRGISFVLSAL---VFNLGPTLFEMMLVSGILyykcggh 283
Cdd:cd18547    75 RTVYDLRKDLFEKLQRLPLSYFDTHSHGDiMSRVtndVDNISQALSQSLTQLissILTIVGTLIMMLYISPLL------- 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 284 fALVTLGT--LSAYTAFTVA-------VTQWRTQFRIemnkadneagNAAID-SLLNYETVKYFNNEKYEAERYDGF-LK 352
Cdd:cd18547   148 -TLIVLVTvpLSLLVTKFIAkrsqkyfRKQQKALGEL----------NGYIEeMISGQKVVKAFNREEEAIEEFDEInEE 216

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2569209806 353 VYES-------SSLKTTSTLAMLNFGQSAIFSVGltAIMVLaskgimSGTMTVGDLV----MVNgllfQLSLPLN 416
Cdd:cd18547   217 LYKAsfkaqfySGLLMPIMNFINNLGYVLVAVVG--GLLVI------NGALTVGVIQaflqYSR----QFSQPIN 279
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
 444-631 2.79e-07

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 53.74  E-value: 2.79e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 444 KIKEKEMAPPLIVTPqeaTIRFED--------VYFEYL----EGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFR 511
Cdd:PRK15064  291 KIKLEEVKPSSRQNP---FIRFEQdkklhrnaLEVENLtkgfDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVG 367

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 512 FYEPQQGNIYIAgQNIRdvgleslrkaVGVVPQD-AVLFHNTIfyNLM--YGNINATAED--VYR--VARLAGIHDAILK 584
Cdd:PRK15064  368 ELEPDSGTVKWS-ENAN----------IGYYAQDhAYDFENDL--TLFdwMSQWRQEGDDeqAVRgtLGRLLFSQDDIKK 434

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2569209806 585 mphkyDTQVgerglkLSGGEKQRVAIARAILKNPPILLYDEATSSLD 631
Cdd:PRK15064  435 -----SVKV------LSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMD 470
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
 475-633 3.05e-07

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 53.58  E-value: 3.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 475 GQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIA-GQNI------------RDVgLESLRKAVGV 541
Cdd:PRK11819   19 KKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPApGIKVgylpqepqldpeKTV-RENVEEGVAE 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 542 VpQDAVLFHNTIfyNLMYGN----INATAEdvyRVARLAGIHDAI---------------LKMPHKyDTQVGerglKLSG 602
Cdd:PRK11819   98 V-KAALDRFNEI--YAAYAEpdadFDALAA---EQGELQEIIDAAdawdldsqleiamdaLRCPPW-DAKVT----KLSG 166

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2569209806 603 GEKQRVAIARAILKNPPILLYDEATSSLD--SV 633
Cdd:PRK11819  167 GERRRVALCRLLLEKPDMLLLDEPTNHLDaeSV 199
ABC_6TM_YknV_like cd18545
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ...
 130-422 4.09e-07

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: 52.47  E-value: 4.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 130 RVVISLSLLAGAKITNVMVPFMFKYAVDSlnqmsghmlnlsDAPNTVVTMATAVLIGYGVSRTGSALFNELRNAVFGKVA 209
Cdd:cd18545     1 KLLLALLLMLLSTAASLAGPYLIKIAIDE------------YIPNGDLSGLLIIALLFLALNLVNWVASRLRIYLMAKVG 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 210 QSSIRRIAKNVFLHLHNLDLGFHLSRQTGA-LSKAI-DRGTrgISFVLSALVFNLGPTLFEMMLVSGILYYKcggHF--A 285
Cdd:cd18545    69 QRILYDLRQDLFSHLQKLSFSFFDSRPVGKiLSRVInDVNS--LSDLLSNGLINLIPDLLTLVGIVIIMFSL---NVrlA 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 286 LVTLGTL--SAYTAFTVAVTQwRTQFRIEMNKADNEagNAAI-DSLLNYETVKYFNNEKYEAERYDGFLKVYESSSLKTT 362
Cdd:cd18545   144 LVTLAVLplLVLVVFLLRRRA-RKAWQRVRKKISNL--NAYLhESISGIRVIQSFAREDENEEIFDELNRENRKANMRAV 220

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2569209806 363 STLAMLNFGQSAIFSVGLTAIMVLASKGIMSGTMTVGDLV-MVN--GLLFQlslPLNFLGTVY 422
Cdd:cd18545   221 RLNALFWPLVELISALGTALVYWYGGKLVLGGAITVGVLVaFIGyvGRFWQ---PIRNLSNFY 280
ABC_6TM_Pgp_ABCB1_D2_like cd18578
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ...
 193-409 7.99e-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: 51.68  E-value: 7.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 193 GSALFNELRNAVFGKVAQSSIRRIAKNVFLHLHNLDLGFH--LSRQTGALSKAIDR---------GTRgISFVLSALVfn 261
Cdd:cd18578    64 VAGIAYFLQGYLFGIAGERLTRRLRKLAFRAILRQDIAWFddPENSTGALTSRLSTdasdvrglvGDR-LGLILQAIV-- 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 262 lgptlfemMLVSGI---LYYkcGGHFALVTLGTLSAYTAFTVAVTQWRTQFRIEMNKADNEAGNAAIDSLLNYETVKYFN 338
Cdd:cd18578   141 --------TLVAGLiiaFVY--GWKLALVGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLT 210

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2569209806 339 NEKYEAERYDGFLKVYESSSLKtTSTLAMLNFG--QSAIFsvgltAIMVLA----SKGIMSGTMTVGDLVMV-NGLLF 409
Cdd:cd18578   211 LEDYFLEKYEEALEEPLKKGLR-RALISGLGFGlsQSLTF-----FAYALAfwygGRLVANGEYTFEQFFIVfMALIF 282
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
477-677 8.64e-07

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 52.09  E-value: 8.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 477 KVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVG-LESLRKAVGVVPQ---DAVLFHN- 551
Cdd:PRK09700  277 KKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSpLDAVKKGMAYITEsrrDNGFFPNf 356

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 552 TIFYNL-------------MYGNINATAEdvyrvARLAGIHDAILKMP-HKYDTQVGErglkLSGGEKQRVAIARAILKN 617
Cdd:PRK09700  357 SIAQNMaisrslkdggykgAMGLFHEVDE-----QRTAENQRELLALKcHSVNQNITE----LSGGNQQKVLISKWLCCC 427

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2569209806 618 PPILLYDEATSSLDSVTEENILTSMKEMVKD-RTSVFIAHRLSTIVDA-DEIIVLNQGKVAE 677
Cdd:PRK09700  428 PEVIIFDEPTRGIDVGAKAEIYKVMRQLADDgKVILMVSSELPEIITVcDRIAVFCEGRLTQ 489
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
 463-639 9.06e-07

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


Pssm-ID: 274744 [Multi-domain]  Cd Length: 552  Bit Score: 52.24  E-value: 9.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 463 IRFEDVYFEYleGQKVL-NGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIaGQNIRdvgleslrkaVGV 541
Cdd:TIGR03719 323 IEAENLTKAF--GDKLLiDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVK----------LAY 389

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 542 VPQ--DAVLFHNTIFYNLMYGNinataeDVYRVARlagihdaiLKMPHK-Y---------DTQ--VGErglkLSGGEKQR 607
Cdd:TIGR03719 390 VDQsrDALDPNKTVWEEISGGL------DIIKLGK--------REIPSRaYvgrfnfkgsDQQkkVGQ----LSGGERNR 451

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2569209806 608 VAIARAILKNPPILLYDEATSSLDSVT----EENIL 639
Cdd:TIGR03719 452 VHLAKTLKSGGNVLLLDEPTNDLDVETlralEEALL 487
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
 484-687 1.02e-06

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 52.26  E-value: 1.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 484 FEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAgqniRDVGLESLRK--------------AVGVVPQDAVL- 548
Cdd:PRK11147   24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYE----QDLIVARLQQdpprnvegtvydfvAEGIEEQAEYLk 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 549 -FHNT---IFYNLMYGNINATAE-----DVYRVARL-AGIHDAILKMPHKYDTQVGErglkLSGGEKQRVAIARAILKNP 618
Cdd:PRK11147  100 rYHDIshlVETDPSEKNLNELAKlqeqlDHHNLWQLeNRINEVLAQLGLDPDAALSS----LSGGWLRKAALGRALVSNP 175

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2569209806 619 PILLYDEATSSLDSVT---EENILTSMKEMVkdrtsVFIAHRLSTIVD-ADEIIVLNQGKVAE-RGNHQTLLDT 687
Cdd:PRK11147  176 DVLLLDEPTNHLDIETiewLEGFLKTFQGSI-----IFISHDRSFIRNmATRIVDLDRGKLVSyPGNYDQYLLE 244
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
 486-670 1.46e-06

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: 50.44  E-value: 1.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 486 VPA-GKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNiYIAGQNIRDVgLESLRkavGVVPQDavlfhntIFYNLMYGNINA 564
Cdd:cd03236    22 VPReGQVLGLVGPNGIGKSTALKILAGKLKPNLGK-FDDPPDWDEI-LDEFR---GSELQN-------YFTKLLEGDVKV 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 565 TAEDVYrVARLA----GIHDAILKMPHKYDT-----------QVGERGL-KLSGGEKQRVAIARAILKNPPILLYDEATS 628
Cdd:cd03236    90 IVKPQY-VDLIPkavkGKVGELLKKKDERGKldelvdqlelrHVLDRNIdQLSGGELQRVAIAAALARDADFYFFDEPSS 168

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2569209806 629 SLDSVTEENILTSMKEMVKDRTSVFIA-HRLStIVD--ADEIIVL 670
Cdd:cd03236   169 YLDIKQRLNAARLIRELAEDDNYVLVVeHDLA-VLDylSDYIHCL 212
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
 466-636 2.34e-06

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 51.10  E-value: 2.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 466 EDVYFEyLEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIaGQNIRDVGLESLRKAVGvvPQd 545
Cdd:PRK11147  323 ENVNYQ-IDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTKLEVAYFDQHRAELD--PE- 397

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 546 avlfhNTIFYNLMYGNINATAEDVYRVArLAGIHDaILKMPHKYDTQVGerglKLSGGEKQRVAIARAILKNPPILLYDE 625
Cdd:PRK11147  398 -----KTVMDNLAEGKQEVMVNGRPRHV-LGYLQD-FLFHPKRAMTPVK----ALSGGERNRLLLARLFLKPSNLLILDE 466

                         170
                  ....*....|.
gi 2569209806 626 ATSSLDSVTEE 636
Cdd:PRK11147  467 PTNDLDVETLE 477
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
 480-668 3.08e-06

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: 47.74  E-value: 3.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 480 NGVSFevPAGKKVAIVGGSGSGKSTIVRLLfrfyepqqgnIYIAGQNIRDVGLESLRKAVGVVPQDAVLFHNTIfynlmy 559
Cdd:cd03227    14 NDVTF--GEGSLTIITGPNGSGKSTILDAI----------GLALGGAQSATRRRSGVKAGCIVAAVSAELIFTR------ 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 560 gninataedvyrvarlagihdailkmphkydtqvgergLKLSGGEKQRVAIARAI----LKNPPILLYDEATSSLDSVTE 635
Cdd:cd03227    76 --------------------------------------LQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDG 117

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2569209806 636 ENILTSMKEM-VKDRTSVFIAHRLSTIVDADEII 668
Cdd:cd03227   118 QALAEAILEHlVKGAQVIVITHLPELAELADKLI 151
ABC_6TM_McjD_like cd18556
Six-transmembrane helical domain of the antibacterial peptide ATP-binding cassette transporter ...
 131-429 3.19e-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: 49.56  E-value: 3.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 131 VVISLSLLAGAKITnvMVPFMFKYAVDSLNQmsghmlNLSDAPNTVVTMATAVLIGYGVSRTGSALFNELrnavfgkvaQ 210
Cdd:cd18556     6 SILFISLLSSILIS--ISPVILAKITDLLTS------SSSDSYNYIVVLAALYVITISATKLLGFLSLYL---------Q 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 211 SSIR-----RIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGISFVLSALVFNLGPTL----FEMMLVSGILYYKCG 281
Cdd:cd18556    69 SSLRveliiSISSSYFRYLYEQPKTFFVKENSGDITQRLNQASNDLYTLVRNLSTNILPPLlqliIAIVVILSSGDYFVA 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 282 GHFALVTLgtlsAYTAFTVAVTQWRTQFRIEMNKADNEAGNAAIDSLLNYETVKYFNNEKYEAERYDGFLKVYESSS--- 358
Cdd:cd18556   149 ALFLLYAV----LFVINNTIFTKKIVSLRNDLMDAGRKSYSLLTDSVKNIVAAKQNNAFDFLFKRYEATLTNDRNSQkry 224

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2569209806 359 LKTTSTLAMLNFGQSAIFsVGLTAIMVLAskGIMSGTMTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQAL 429
Cdd:cd18556   225 WKLTFKMLILNSLLNVIL-FGLSFFYSLY--GVVNGQVSIGHFVLITSYILLLSTPIESLGNMLSELRQSV 292
ABC_6TM_exporter_like cd18778
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
 131-402 3.21e-06

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


Pssm-ID: 350051 [Multi-domain]  Cd Length: 293  Bit Score: 49.46  E-value: 3.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 131 VVISLSLLAGAKITNVMVPFMFKYAVDSLNQMSGhmlNLSDAPNTVVTMATAVLigygvsrtGSALFNELRNAVFGKVAQ 210
Cdd:cd18778     1 LILTLLCALLSTLLGLVPPWLIRELVDLVTIGSK---SLGLLLGLALLLLGAYL--------LRALLNFLRIYLNHVAEQ 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 211 SSIRRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGISFVLSALVFNLGPTLFEMMLVSGILYYKcGGHFALVTLG 290
Cdd:cd18778    70 KVVADLRSDLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSI-NPKLALLTLI 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 291 TLSAYTAFTVAVT-----QWRTQFRI--EMNKA--DNEAGNAAIdsllnyetvKYFNNEKYEAERYDGFLKVYESSSLKT 361
Cdd:cd18778   149 PIPFLALGAWLYSkkvrpRYRKVREAlgELNALlqDNLSGIREI---------QAFGREEEEAKRFEALSRRYRKAQLRA 219

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 2569209806 362 TSTLAMlnFGQSAIFSVGLTAIMVLASKG--IMSGTMTVGDLV 402
Cdd:cd18778   220 MKLWAI--FHPLMEFLTSLGTVLVLGFGGrlVLAGELTIGDLV 260
ycf16 CHL00131
sulfate ABC transporter protein; Validated
 477-680 4.35e-06

sulfate ABC transporter protein; Validated


Pssm-ID: 214372 [Multi-domain]  Cd Length: 252  Bit Score: 48.87  E-value: 4.35e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 477 KVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRF--YEPQQGNIYIAGQNIRDVGLEsLRKAVGVV-----PQDAVLF 549
Cdd:CHL00131   21 EILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEPE-ERAHLGIFlafqyPIEIPGV 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 550 HNTIFYNLMYgNINATAEDVYRVARLA--GIHDAILKM----PHKYDTQVGErglKLSGGEKQRVAIARAILKNPPILLY 623
Cdd:CHL00131  100 SNADFLRLAY-NSKRKFQGLPELDPLEflEIINEKLKLvgmdPSFLSRNVNE---GFSGGEKKRNEILQMALLDSELAIL 175

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2569209806 624 DEATSSLD-----SVTEE-NILtsmkeMVKDRTSVFIAH--RLSTIVDADEIIVLNQGKVAERGN 680
Cdd:CHL00131  176 DETDSGLDidalkIIAEGiNKL-----MTSENSIILITHyqRLLDYIKPDYVHVMQNGKIIKTGD 235
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
 486-658 5.09e-06

retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]


Pssm-ID: 130324 [Multi-domain]  Cd Length: 2272  Bit Score: 50.40  E-value: 5.09e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806  486 VPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRdVGLESLRKAVGVVPQ-DAVlfhntifYNLMYGNina 564
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIL-TNISDVHQNMGYCPQfDAI-------DDLLTGR--- 2030

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806  565 taEDVYRVARLAGIHDAILKMPHKYDTQvgERGLKL---------SGGEKQRVAIARAILKNPPILLYDEATSSLDSVTE 635
Cdd:TIGR01257 2031 --EHLYLYARLRGVPAEEIEKVANWSIQ--SLGLSLyadrlagtySGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQAR 2106

                          170       180
                   ....*....|....*....|....
gi 2569209806  636 ENILTSMKEMVKD-RTSVFIAHRL 658
Cdd:TIGR01257 2107 RMLWNTIVSIIREgRAVVLTSHSM 2130
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
594-679 1.06e-05

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 48.19  E-value: 1.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 594 GERGLKLSGGEKQRVAIARAILKNPPILLYDEATSSLDSVTEENILTSMKEMVKDRTSVFIAHRLSTIVD--ADEIIVLN 671
Cdd:NF000106  139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEqlAHELTVID 218


                  ....*...
gi 2569209806 672 QGKVAERG 679
Cdd:NF000106  219 RGRVIADG 226
PRK13541 PRK13541
cytochrome c biogenesis protein CcmA; Provisional
 494-637 1.14e-05

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184128 [Multi-domain]  Cd Length: 195  Bit Score: 46.79  E-value: 1.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 494 IVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDVGleslrkavgvVPQDAVLFHN-------TIFYNL-MYGNINAT 565
Cdd:PRK13541   31 IKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIA----------KPYCTYIGHNlglklemTVFENLkFWSEIYNS 100

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2569209806 566 AEDVYrvarlAGIHdailkmPHKYDTQVGERGLKLSGGEKQRVAIARAILKNPPILLYDEATSSLDsvtEEN 637
Cdd:PRK13541  101 AETLY-----AAIH------YFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLS---KEN 158
ABC_6TM_YwjA_like cd18549
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ...
 218-402 1.34e-05

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: 47.83  E-value: 1.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 218 KNVFLHLHNLDLGFHLSRQTGALSkaidrgTRGIS--FVLSALVFNlGPtlfEMMLVSGIlyyKCGGHF----------A 285
Cdd:cd18549    79 RDLFEHLQKLSFSFFDNNKTGQLM------SRITNdlFDISELAHH-GP---EDLFISII---TIIGSFiilltinvplT 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 286 LVTLGTLSAYTAFTVAVT-QWRTQFRieMNKADNEAGNAAI-DSLLNYETVKYFNNEKYEAERYDGFLKVYESSslKTTS 363
Cdd:cd18549   146 LIVFALLPLMIIFTIYFNkKMKKAFR--RVREKIGEINAQLeDSLSGIRVVKAFANEEYEIEKFDEGNDRFLES--KKKA 221

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2569209806 364 TLAMLNFGQSAIFSVGLTAIMVLASKG--IMSGTMTVGDLV 402
Cdd:cd18549   222 YKAMAYFFSGMNFFTNLLNLVVLVAGGyfIIKGEITLGDLV 262
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
473-676 1.58e-05

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 47.98  E-value: 1.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 473 LEGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQ--NIRDVGlESL----------RKAVG 540
Cdd:PRK11288  263 LKGPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKpiDIRSPR-DAIragimlcpedRKAEG 341

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 541 VVPQDAVlfhntifynlmYGNINATAE----------DVYRVARLAGIHDAIL--KMPHKyDTQVGerglKLSGGEKQRV 608
Cdd:PRK11288  342 IIPVHSV-----------ADNINISARrhhlragcliNNRWEAENADRFIRSLniKTPSR-EQLIM----NLSGGNQQKA 405

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 609 AIARAILKNPPILLYDEATSSLDSVTEENILTSMKEMVKD-RTSVFIAHRLSTIVD-ADEIIVLNQGKVA 676
Cdd:PRK11288  406 ILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQgVAVLFVSSDLPEVLGvADRIVVMREGRIA 475
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
 598-670 1.77e-05

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


Pssm-ID: 213189 [Multi-domain]  Cd Length: 177  Bit Score: 46.03  E-value: 1.77e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2569209806 598 LKLSGGEKQRVAIARAILKNPPILLYDEATSSLDSVTEENILTSMKEMV-KDRTSVFIAHRLSTIVD--ADEIIVL 670
Cdd:cd03222    70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSeEGKKTALVVEHDLAVLDylSDRIHVF 145
PRK15093 PRK15093
peptide ABC transporter ATP-binding protein SapD;
599-688 1.94e-05

peptide ABC transporter ATP-binding protein SapD;


Pssm-ID: 185049 [Multi-domain]  Cd Length: 330  Bit Score: 47.49  E-value: 1.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 599 KLSGGEKQRVAIARAILKNPPILLYDEATSSLDSVTEENILTSMKEMVKDR--TSVFIAHRLSTIVD-ADEIIVLNQGKV 675
Cdd:PRK15093  158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNntTILLISHDLQMLSQwADKINVLYCGQT 237

                          90
                  ....*....|...
gi 2569209806 676 AERGNHQTLLDTP 688
Cdd:PRK15093  238 VETAPSKELVTTP 250
ABC_6TM_bac_exporter_ABCB8_10_like cd18575
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ...
 131-402 3.61e-05

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: 46.32  E-value: 3.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 131 VVISLSLLAGAkitNVMVPFMFKYAVDS-LNQMSGHMLNLSdapnTVVTMATAVLIG-------YGVSRTGSALFNELRN 202
Cdd:cd18575     1 ALIALLIAAAA---TLALGQGLRLLIDQgFAAGNTALLNRA----FLLLLAVALVLAlasalrfYLVSWLGERVVADLRK 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 203 AVFGkvaqssirriaknvflHLHNLDLGFHLSRQTG-----------ALSKAIdrGTrGISFVLSALVFNLGPTLfeMML 271
Cdd:cd18575    74 AVFA----------------HLLRLSPSFFETTRTGevlsrlttdttLIQTVV--GS-SLSIALRNLLLLIGGLV--MLF 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 272 VSGIlyykcggHFALVTLGTLSAYTAFTVAVTQW------RTQFRIemnkADneAGNAAIDSLLNYETVKYFNNEKYEAE 345
Cdd:cd18575   133 ITSP-------KLTLLVLLVIPLVVLPIILFGRRvrrlsrASQDRL----AD--LSAFAEETLSAIKTVQAFTREDAERQ 199

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2569209806 346 RYDGFLKVYESSSLKTTSTLAMLNFgqSAIFSV--GLTAIMVLASKGIMSGTMTVGDLV 402
Cdd:cd18575   200 RFATAVEAAFAAALRRIRARALLTA--LVIFLVfgAIVFVLWLGAHDVLAGRMSAGELS 256
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
 479-631 3.63e-05

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 46.92  E-value: 3.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 479 LNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIrdvgleslrkaVGVVPQDAVlfHNTIFY--- 555
Cdd:PRK10762  268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEV-----------VTRSPQDGL--ANGIVYise 334

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 556 -----NLMYG-----NINATAEDVYrvARLAG----------IHDAI----LKMPHKyDTQVGerglKLSGGEKQRVAIA 611
Cdd:PRK10762  335 drkrdGLVLGmsvkeNMSLTALRYF--SRAGGslkhadeqqaVSDFIrlfnIKTPSM-EQAIG----LLSGGNQQKVAIA 407

                         170       180
                  ....*....|....*....|
gi 2569209806 612 RAILKNPPILLYDEATSSLD 631
Cdd:PRK10762  408 RGLMTRPKVLILDEPTRGVD 427
ABC_6TM_TAP1 cd18589
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ...
 214-429 5.64e-05

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: 45.54  E-value: 5.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 214 RRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGISFVLSAlvfNLGPTLFEMMLVSGILYYKCGG--HFALVTLGT 291
Cdd:cd18589    69 SRLQGLVFAAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSE---NLSLLMWYLARGLFLFIFMLWLspKLALLTALG 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 292 LSAYTAFTVAVTQWRTQFRIEMNKADNEAGNAAIDSLLNYETVKYFNNEKYEAERYDGFLKvyESSSL-KTTSTLAMLNF 370
Cdd:cd18589   146 LPLLLLVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEEGEAQRYRQRLQ--KTYRLnKKEAAAYAVSM 223

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2569209806 371 GQSAIFSVGL-TAIMVLASKGIMSGTMTVGDLVMVngLLFQL--SLPLNFLGTVYRETRQAL 429
Cdd:cd18589   224 WTSSFSGLALkVGILYYGGQLVTAGTVSSGDLVTF--VLYELqfTSAVEVLLSYYPSVMKAV 283
ABC_SMC_barmotin cd03278
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ...
 492-668 7.83e-05

ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).


Pssm-ID: 213245 [Multi-domain]  Cd Length: 197  Bit Score: 44.38  E-value: 7.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 492 VAIVGGSGSGKSTIVRLLfRFYEPQQGNIYIAGQNIRDV---GLESlRKAVGVVpQDAVLFHNTI-FYNLMY-GNInata 566
Cdd:cd03278    25 TAIVGPNGSGKSNIIDAI-RWVLGEQSAKSLRGEKMSDVifaGSET-RKPANFA-EVTLTFDNSDgRYSIISqGDV---- 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 567 edvyrvarlagihDAILKMPHKYDTQVGerglKLSGGEKQRVAIAR--AILK-NP-PILLYDEATSSLDSVTEENILTSM 642
Cdd:cd03278    98 -------------SEIIEAPGKKVQRLS----LLSGGEKALTALALlfAIFRvRPsPFCVLDEVDAALDDANVERFARLL 160

                         170       180
                  ....*....|....*....|....*.
gi 2569209806 643 KEMVKDRTSVFIAHRLSTIVDADEII 668
Cdd:cd03278   161 KEFSKETQFIVITHRKGTMEAADRLY 186
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
 474-686 1.00e-04

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


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 45.87  E-value: 1.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806  474 EGQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLfrfyePQQGNIYIAGQNIRDVGL----ESLRKAVGVVPQ-DAVL 548
Cdd:TIGR00956  774 EKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVL-----AERVTTGVITGGDRLVNGrpldSSFQRSIGYVQQqDLHL 848

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806  549 FHNTIFYNLMYG---------NINATAEDVYRVARLagihdaiLKMPHKYDTQVGERGLKLSGGEKQRVAIARAILKNPP 619
Cdd:TIGR00956  849 PTSTVRESLRFSaylrqpksvSKSEKMEYVEEVIKL-------LEMESYADAVVGVPGEGLNVEQRKRLTIGVELVAKPK 921

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2569209806  620 ILLY-DEATSSLDSVTEENILTSMKEMVKD-RTSVFIAHRLSTIVDA--DEIIVLNQG-KVAERG----NHQTLLD 686
Cdd:TIGR00956  922 LLLFlDEPTSGLDSQTAWSICKLMRKLADHgQAILCTIHQPSAILFEefDRLLLLQKGgQTVYFGdlgeNSHTIIN 997
ABC_6TM_ABCB9_like cd18784
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ...
 181-422 1.50e-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: 44.22  E-value: 1.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 181 TAVLIgYGVSRTGSALFNELRNAVFGKVAQSSIRRIAKNVFLHLHNLDLGFHLSRQTGALskaIDRGTRGISFVLSALVF 260
Cdd:cd18784    37 RAIII-MGLLAIASSVAAGIRGGLFTLAMARLNIRIRNLLFRSIVSQEIGFFDTVKTGDI---TSRLTSDTTTMSDTVSL 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 261 NLGPTLFEMMLVSG--ILYYKCGGHFALVTLGTLSAYTAFTVAVTQWRTQFRIEMNKADNEAGNAAIDSLLNYETVKYFN 338
Cdd:cd18784   113 NLNIFLRSLVKAIGviVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYYKKLSKAVQDSLAKANEVAEETISSIRTVRSFA 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 339 NEKYEAERYDGFLKVYESSSLKTTSTLAMLNFGqSAIFSVGLTAIMvLASKG--IMSGTMTVGDLVMVngLLFQLSL--P 414
Cdd:cd18784   193 NEDGEANRYSEKLKDTYKLKIKEALAYGGYVWS-NELTELALTVST-LYYGGhlVITGQISGGNLISF--ILYQLELgsC 268


                  ....*...
gi 2569209806 415 LNFLGTVY 422
Cdd:cd18784   269 LESVGSVY 276
ABC_6TM_Rv0194_D2_like cd18546
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ...
 131-428 1.64e-04

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


Pssm-ID: 349990 [Multi-domain]  Cd Length: 292  Bit Score: 44.40  E-value: 1.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 131 VVISLSLLAGAKITNVMVPFMFKYAVDS-LNQMSGHMLNLsdapnTVVTMATAVLIGYGVSRtgsalfneLRNAVFGKVA 209
Cdd:cd18546     1 LALALLLVVVDTAASLAGPLLVRYGIDSgVRAGDLGVLLL-----AAAAYLAVVLAGWVAQR--------AQTRLTGRTG 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 210 QSSIRRIAKNVFLHLHNLDLGFH--------LSRQTG---ALSKAIDRG-----TRGISFV-LSALVFNLGPTLfemmlv 272
Cdd:cd18546    68 ERLLYDLRLRVFAHLQRLSLDFHeretsgriMTRMTSdidALSELLQTGlvqlvVSLLTLVgIAVVLLVLDPRL------ 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 273 sgilyykcgghfALVTLGTLsaytAFTVAVTQWrtqFRIEMNKADNEAGNAAIDSLLNY-ET------VKYFNNEKYEAE 345
Cdd:cd18546   142 ------------ALVALAAL----PPLALATRW---FRRRSSRAYRRARERIAAVNADLqETlagirvVQAFRRERRNAE 202

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 346 RYDGFLKVYESSSLKTTSTLAMLNFGQSAIFSVGLTAIMVLASKGIMSGTMTVGDLV---MVNGLLFQlslPLNFLGTVY 422
Cdd:cd18546   203 RFAELSDDYRDARLRAQRLVAIYFPGVELLGNLATAAVLLVGAWRVAAGTLTVGVLVaflLYLRRFFA---PIQQLSQVF 279


                  ....*.
gi 2569209806 423 RETRQA 428
Cdd:cd18546   280 DSYQQA 285
ABC_6TM_Sav1866_like cd18554
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ...
 147-433 1.78e-04

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: 44.33  E-value: 1.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 147 MVPFMFKYAVDSLNQmsGHMLNLSDAPNTVVTMATAVLIGYGVSRTGSALFnelRNAVFGKVAQSSIRRIAKNVFLHLHN 226
Cdd:cd18554    17 LLPLILKYIVDDVIQ--GSSLTLDEKVYKLFTIIGIMFFIFLILRPPVEYY---RQYFAQWIANKILYDIRKDLFDHLQK 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 227 LDLGFHLSRQTGAL-SKAIDRGTRGISFVLSALVfNLGPTLFEMMLVSGILyykCGGHFALvTLGTLSAYTAFTVAVTQW 305
Cdd:cd18554    92 LSLRYYANNRSGEIiSRVINDVEQTKDFITTGLM-NIWLDMITIIIAICIM---LVLNPKL-TFVSLVIFPFYILAVKYF 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 306 RTQFRI---EMNKADNEAGNAAIDSLLNYETVKYFNNEKYEAERYDGFLKVYESSSLKTTS----TLAMLNfgqsAIFSV 378
Cdd:cd18554   167 FGRLRKltkERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRALKHTRwnakTFSAVN----TITDL 242

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2569209806 379 GLTAIMVLASKGIMSGTMTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDMN 433
Cdd:cd18554   243 APLLVIGFAAYLVIEGNLTVGTLVAFVGYMERMYSPLRRLVNSFTTLTQSFASMD 297
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
463-631 3.00e-04

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 44.35  E-value: 3.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 463 IRFEDVYFEYleGQKV-LNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIAGQNIRDvglESLRKAVG- 540
Cdd:NF033858    2 ARLEGVSHRY--GKTVaLDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAD---ARHRRAVCp 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 541 ---VVPQDavLFHN-----TIFYNLMYgninataedvyrVARLAGiHDAilkmphkydtqvGER-----------GL--- 598
Cdd:NF033858   77 riaYMPQG--LGKNlyptlSVFENLDF------------FGRLFG-QDA------------AERrrridellratGLapf 129

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2569209806 599 ------KLSGGEKQRVAIARAILKNPPILLYDEATSSLD 631
Cdd:NF033858  130 adrpagKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVD 168
ABC_6TM_TAP2 cd18590
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ...
 193-422 5.00e-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: 42.71  E-value: 5.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 193 GSALFNELRNAVFGKVAQSSIRRIAKNVFLHLHNLDLGFHLSRQTGA----LSKAIDRGTRGISFVLSALVFNLGPTLfe 268
Cdd:cd18590    48 GSSLSAGLRGGLFMCTLSRLNLRLRHQLFSSLVQQDIGFFEKTKTGDltsrLSTDTTLMSRSVALNANVLLRSLVKTL-- 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 269 mmlvsGILYYKCGGHFALVTLGTLSA-YTAFTVAVTQWRTQ-FRIEMNKADNEAGNAAIDSLLNYETVKYFNNEKYEAER 346
Cdd:cd18590   126 -----GMLGFMLSLSWQLTLLTLIEMpLTAIAQKVYNTYHQkLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACR 200

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2569209806 347 YDGFLKvyESSSLKTT-STLAMLNFGQSAIFSVGLTAIMV-LASKGIMSGTMTVGDLVMVngLLFQLSLPLNFLGTVY 422
Cdd:cd18590   201 YSEALE--RTYNLKDRrDTVRAVYLLVRRVLQLGVQVLMLyCGRQLIQSGHLTTGSLVSF--ILYQKNLGSYVRTLVY 274
GguA NF040905
sugar ABC transporter ATP-binding protein;
475-675 6.86e-04

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 42.85  E-value: 6.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 475 GQKVLNGVSFEVPAGKKVAIVGGSGSGKSTIVRLLF-RFYEPQ-QGNIYIAGQNIR--------DVGL----ESlRKAVG 540
Cdd:NF040905  272 ERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFgRSYGRNiSGTVFKDGKEVDvstvsdaiDAGLayvtED-RKGYG 350

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 541 VVPQDAVLfHNTIFYNL----MYGNINATAEdvYRVARlaGIHDAI-LKMPhkydtQVGERGLKLSGGEKQRVAIARAIL 615
Cdd:NF040905  351 LNLIDDIK-RNITLANLgkvsRRGVIDENEE--IKVAE--EYRKKMnIKTP-----SVFQKVGNLSGGNQQKVVLSKWLF 420

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2569209806 616 KNPPILLYDEATSSLDSVTEENILTSMKEMVKD-RTSVFIAHRLSTIVD-ADEIIVLNQGKV 675
Cdd:NF040905  421 TDPDVLILDEPTRGIDVGAKYEIYTIINELAAEgKGVIVISSELPELLGmCDRIYVMNEGRI 482
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
 479-670 8.75e-04

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


Pssm-ID: 213238 [Multi-domain]  Cd Length: 261  Bit Score: 41.83  E-value: 8.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 479 LNGVSFEVPAGKKVAIVGGSGSGKSTIV---------RLLFRFYEPqqgniyiAGQNIRDVGLESLRKAVgVVPQDAV-- 547
Cdd:cd03271    11 LKNIDVDIPLGVLTCVTGVSGSGKSSLIndtlypalaRRLHLKKEQ-------PGNHDRIEGLEHIDKVI-VIDQSPIgr 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 548 -LFHNTIFYNLMYGNINATAEDVYRVARL-----------AGIHDaILKMP---------------HKYDT--------- 591
Cdd:cd03271    83 tPRSNPATYTGVFDEIRELFCEVCKGKRYnretlevrykgKSIAD-VLDMTveealeffenipkiaRKLQTlcdvglgyi 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 592 QVGERGLKLSGGEKQRVAIARAILK---NPPILLYDEATSSLDSVTEENILTSMKEMV-KDRTSVFIAHRLSTIVDADEI 667
Cdd:cd03271   162 KLGQPATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRLVdKGNTVVVIEHNLDVIKCADWI 241


                  ...
gi 2569209806 668 IVL 670
Cdd:cd03271   242 IDL 244
ABC_6TM_CvaB_RaxB_like cd18567
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ...
 219-402 9.20e-04

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


Pssm-ID: 350011 [Multi-domain]  Cd Length: 294  Bit Score: 42.06  E-value: 9.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 219 NVFLHLHNLDLGFHLSRQTG----------ALSKAIdrgTRG-ISFVLSALVFNLgpTLFEMMLVSGILyykcgghfALV 287
Cdd:cd18567    80 NLFRHLLRLPLSYFEKRHLGdivsrfgsldEIQQTL---TTGfVEALLDGLMAIL--TLVMMFLYSPKL--------ALI 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 288 TLGTLSAYTAFTVAVtqwrtqFRIEMNKADNEAGNAA------IDSLLNYETVKYFNNEKYEAERYDGFLKVYESSSLKT 361
Cdd:cd18567   147 VLAAVALYALLRLAL------YPPLRRATEEQIVASAkeqshfLETIRGIQTIKLFGREAEREARWLNLLVDAINADIRL 220

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2569209806 362 TSTLAMLNFGQSAIFSVGLTAIMVLASKGIMSGTMTVGDLV 402
Cdd:cd18567   221 QRLQILFSAANGLLFGLENILVIYLGALLVLDGEFTVGMLF 261
PLN03140 PLN03140
ABC transporter G family member; Provisional
 590-686 9.73e-04

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 42.91  E-value: 9.73e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806  590 DTQVGERGLK-LSGGEKQRVAIARAILKNPPILLYDEATSSLDSVTEENILTSMKEMVKDRTSVFIAHRLS----TIVDA 664
Cdd:PLN03140   326 DTIVGDEMIRgISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLMSLLQpapeTFDLF 405

                           90       100
                   ....*....|....*....|..
gi 2569209806  665 DEIIVLNQGKVAERGNHQTLLD 686
Cdd:PLN03140   406 DDIILLSEGQIVYQGPRDHILE 427
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 600-668 1.13e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 42.35  E-value: 1.13e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2569209806  600 LSGGEKQRVAIAR--AILK-NP-PILLYDEATSSLDSVTEENILTSMKEMVKDRTSVFIAHRLSTIVDADEII 668
Cdd:TIGR02168 1090 LSGGEKALTALALlfAIFKvKPaPFCILDEVDAPLDDANVERFANLLKEFSKNTQFIVITHNKGTMEVADQLY 1162
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
 463-631 1.21e-03

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 42.03  E-value: 1.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 463 IRFEDVYFEYleGQKVL-NGVSFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQQGNIYIaGQNIRdvgleslrkaVGV 541
Cdd:PRK11819  325 IEAENLSKSF--GDRLLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETVK----------LAY 391

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 542 VPQ--DAVLFHNTIFYN-------LMYGN--INATAedvYrVARLAgihdaiLKMPhkyDTQ--VGErglkLSGGEKQRV 608
Cdd:PRK11819  392 VDQsrDALDPNKTVWEEisggldiIKVGNreIPSRA---Y-VGRFN------FKGG---DQQkkVGV----LSGGERNRL 454

                         170       180
                  ....*....|....*....|....*.
gi 2569209806 609 AIARaILK---NppILLYDEATSSLD 631
Cdd:PRK11819  455 HLAK-TLKqggN--VLLLDEPTNDLD 477
ABC_6TM_T1SS_like cd18555
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ...
 132-424 1.49e-03

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


Pssm-ID: 349999 [Multi-domain]  Cd Length: 294  Bit Score: 41.34  E-value: 1.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 132 VISLSLLAgaKITNVMVPFMFKYAVDslnqmsgHMLNLSDAPNTVVTMATAVLIG--YGvsrtgsaLFNELRNAVFGKVA 209
Cdd:cd18555     7 ILLLSLLL--QLLTLLIPILTQYVID-------NVIVPGNLNLLNVLGIGILILFllYG-------LFSFLRGYIIIKLQ 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 210 QSSIRRIAKNVFLHLHNLDLGFHLSRQTGAL-----SKAIDRG---TRGISFVLSALVFnlgPTLFEMMLVSGILYykcg 281
Cdd:cd18555    71 TKLDKSLMSDFFEHLLKLPYSFFENRSSGDLlfranSNVYIRQilsNQVISLIIDLLLL---VIYLIYMLYYSPLL---- 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 282 ghfALVTLgTLSAYTAFTVAVTQWRTQFRIEMNKADN-EAGNAAIDSLLNYETVKYFNNEKYeaeRYDGFLKVYES---S 357
Cdd:cd18555   144 ---TLIVL-LLGLLIVLLLLLTRKKIKKLNQEEIVAQtKVQSYLTETLYGIETIKSLGSEKN---IYKKWENLFKKqlkA 216

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2569209806 358 SLKTTSTLAMLNFGQSAIFSVGLTAIMVLASKGIMSGTMTVGDLVMVNGLLFQLSLPLNFLGTVYRE 424
Cdd:cd18555   217 FKKKERLSNILNSISSSIQFIAPLLILWIGAYLVINGELTLGELIAFSSLAGSFLTPIVSLINSYNQ 283
PLN03140 PLN03140
ABC transporter G family member; Provisional
 363-673 2.23e-03

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 41.76  E-value: 2.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806  363 STLAMLNFgqSAIFSVGLT-AIMVLASKGIMSGTMTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDMNTLFTLLSV 441
Cdd:PLN03140   766 GVGALLGF--TILFNVLFTlALTYLNPLGKKQAIISEETAEEMEGEEDSIPRSLSSADGNNTREVAIQRMSNPEGLSKNR 843

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806  442 DTKIKEKEMAPP-----LIVTPqeATIRFEDV-YFEYLEGQ-----------KVLNGVSFEVPAGKKVAIVGGSGSGKST 504
Cdd:PLN03140   844 DSSLEAANGVAPkrgmvLPFTP--LAMSFDDVnYFVDMPAEmkeqgvtedrlQLLREVTGAFRPGVLTALMGVSGAGKTT 921

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806  505 IVRLLfrfyEPQQGNIYIAGqNIRDVGL----ESLRKAVGVVPQDAVlfHN---TIFYNLMYGN-----INATAED---- 568
Cdd:PLN03140   922 LMDVL----AGRKTGGYIEG-DIRISGFpkkqETFARISGYCEQNDI--HSpqvTVRESLIYSAflrlpKEVSKEEkmmf 994

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806  569 ---VYRVARLAGIHDAILKMPhkydtqvGERGLklSGGEKQRVAIARAILKNPPILLYDEATSSLDSVTEENILTSMKEM 645
Cdd:PLN03140   995 vdeVMELVELDNLKDAIVGLP-------GVTGL--STEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNT 1065

                          330       340       350
                   ....*....|....*....|....*....|.
gi 2569209806  646 VKD-RTSVFIAHRLST-IVDA-DEIIVLNQG 673
Cdd:PLN03140  1066 VDTgRTVVCTIHQPSIdIFEAfDELLLMKRG 1096
ABC_6TM_PrtD_LapB_HlyB_like cd18782
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ...
 194-412 2.30e-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: 40.65  E-value: 2.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 194 SALFNELRNAVFGKVAQSSIRRIAKNVFLHLHNLDLGFHLSRQTGALSKAID-----RG---TRGISFVLSAlVFNLGpT 265
Cdd:cd18782    55 EAVLTALRTYLFTDTANRIDLELGGTIIDHLLRLPLGFFDKRPVGELSTRISeldtiRGfltGTALTTLLDV-LFSVI-Y 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 266 LFEMMLVSGILyykcgghfALVTLGTLSAY---TAFTVAVTQWRTQFRIEMNKADNeagNAAIDSLLNYETVKYFNNEKY 342
Cdd:cd18782   133 IAVLFSYSPLL--------TLVVLATVPLQlllTFLFGPILRRQIRRRAEASAKTQ---SYLVESLTGIQTVKAQNAELK 201

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2569209806 343 EAERYDGFLKVYESSSLKTTSTLAMLNFGQSAIFSVGLTAIMVLASKGIMSGTMTVGDLV-------MVNGLLFQLS 412
Cdd:cd18782   202 ARWRWQNRYARSLGEGFKLTVLGTTSGSLSQFLNKLSSLLVLWVGAYLVLRGELTLGQLIafrilsgYVTGPILRLS 278
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
 592-670 7.98e-03

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


Pssm-ID: 273184 [Multi-domain]  Cd Length: 925  Bit Score: 39.61  E-value: 7.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2569209806 592 QVGERGLKLSGGEKQRVAIARAILK---NPPILLYDEATSSL--DSVTE-ENILTSMKEmvKDRTSVFIAHRLSTIVDAD 665
Cdd:TIGR00630 822 RLGQPATTLSGGEAQRIKLAKELSKrstGRTLYILDEPTTGLhfDDIKKlLEVLQRLVD--KGNTVVVIEHNLDVIKTAD 899


                  ....*
gi 2569209806 666 EIIVL 670
Cdd:TIGR00630 900 YIIDL 904
 
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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